GRS - Genome Report System

Botrytis cinerea T4 GRS

Functional annotation

BofuT4_P062770.1

Gene Identifier

DbXrefs

Domain/Motif (Interproscan results)

Localization / Targeting

Predicted function

Blast based analysis

Analysis	Hit	start	end	length	Note	Hit coverage	Hit length	Hit pident	Hit pcons	eValue	Hit description
blastp_kegg	bfu:BC1G_06394	30	122	93	n/a	26.50	351	77.42	0.00	2e-34	hypothetical protein K13953 alcohol dehydrogenase propanol-preferring [EC:1.1.1.1]
	ssl:SS1G_13409	30	122	93	n/a	26.05	357	69.89	4.30	1e-30	hypothetical protein K13953 alcohol dehydrogenase propanol-preferring [EC:1.1.1.1]
	pno:SNOG_08675	30	122	93	n/a	26.42	352	61.29	9.68	2e-26	hypothetical protein K13953 alcohol dehydrogenase propanol-preferring [EC:1.1.1.1]
	mgr:MGG_03880	30	122	93	n/a	26.42	352	56.99	10.75	1e-24	MG03880.4 hypothetical protein K13953 alcohol dehydrogenase propanol-preferring [EC:1.1.1.1]
	ncr:NCU01754	32	122	91	n/a	25.78	353	54.95	15.38	8e-24	alcohol dehydrogenase I K13953 alcohol dehydrogenase propanol-preferring [EC:1.1.1.1]
	zma:100274539	32	122	91	n/a	25.78	353	54.95	10.99	1e-22	hypothetical protein LOC100274539 K13953 alcohol dehydrogenase propanol-preferring [EC:1.1.1.1]
	act:ACLA_066630	32	122	91	n/a	26.00	350	50.55	16.48	5e-21	alcohol dehydrogenase K13953 alcohol dehydrogenase propanol-preferring [EC:1.1.1.1]
	ang:An17g01530	32	122	91	n/a	26.00	350	51.65	14.29	5e-21	adhA alcohol-dehydrogenase adhA from patent WO8704464-A-Aspergillus niger (EC:1.1.1.1) K13953 alcohol dehydrogenase propanol-preferring [EC:1.1.1.1]
	act:ACLA_009560	32	122	91	n/a	26.00	350	49.45	18.68	8e-21	alcohol dehydrogenase K13953 alcohol dehydrogenase propanol-preferring [EC:1.1.1.1]
	pan:PODANSg6586	32	92	61	n/a	17.23	354	70.49	13.11	1e-20	hypothetical protein K13953 alcohol dehydrogenase propanol-preferring [EC:1.1.1.1]
blastp_uniprot_sprot	sp\|Q9P6C8\|ADH1_NEUCR	32	122	91	n/a	25.78	353	54.95	15.38	7e-25	Alcohol dehydrogenase 1 OS Neurospora crassa GN adh-1 PE 3 SV 1
	sp\|P41747\|ADH1_ASPFN	32	122	91	n/a	26.00	350	47.25	18.68	3e-21	Alcohol dehydrogenase 1 OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM 12722 / SRRC 167) GN adh1 PE 2 SV 2
	sp\|P07754\|ADH3_EMENI	32	122	91	Gaps:2	26.42	352	48.39	16.13	1e-19	Alcohol dehydrogenase 3 OS Emericella nidulans GN alcC PE 3 SV 1
	sp\|P08843\|ADH1_EMENI	32	122	91	n/a	26.00	350	46.15	16.48	1e-19	Alcohol dehydrogenase 1 OS Emericella nidulans GN alcA PE 3 SV 2
	sp\|O13309\|ADH2_PICST	32	122	91	n/a	26.15	348	47.25	14.29	1e-18	Alcohol dehydrogenase 2 OS Pichia stipitis GN ADH2 PE 3 SV 1
	sp\|O00097\|ADH1_PICST	32	122	91	n/a	26.15	348	47.25	13.19	4e-18	Alcohol dehydrogenase 1 OS Pichia stipitis GN ADH1 PE 3 SV 1
	sp\|O94038\|ADH2_CANAL	32	122	91	n/a	26.15	348	49.45	9.89	1e-17	Alcohol dehydrogenase 2 OS Candida albicans GN ADH2 PE 1 SV 1
	sp\|P49385\|ADH4_KLULA	17	122	106	Gaps:3	29.07	375	40.37	15.60	4e-17	Alcohol dehydrogenase 4 mitochondrial OS Kluyveromyces lactis GN ADH4 PE 3 SV 2
	sp\|Q07288\|ADH1_KLUMA	33	122	90	n/a	25.86	348	45.56	13.33	9e-17	Alcohol dehydrogenase 1 OS Kluyveromyces marxianus GN ADH1 PE 3 SV 1
	sp\|P20369\|ADH1_KLULA	32	122	91	n/a	26.00	350	45.05	14.29	1e-16	Alcohol dehydrogenase 1 OS Kluyveromyces lactis GN ADH1 PE 3 SV 1
blastp_pdb	2hcy_D	32	122	91	n/a	26.22	347	43.96	15.38	2e-16	mol:protein length:347 Alcohol dehydrogenase 1
	2hcy_C	32	122	91	n/a	26.22	347	43.96	15.38	2e-16	mol:protein length:347 Alcohol dehydrogenase 1
	2hcy_B	32	122	91	n/a	26.22	347	43.96	15.38	2e-16	mol:protein length:347 Alcohol dehydrogenase 1
	2hcy_A	32	122	91	n/a	26.22	347	43.96	15.38	2e-16	mol:protein length:347 Alcohol dehydrogenase 1
	1llu_H	32	92	61	n/a	17.84	342	49.18	13.11	1e-10	mol:protein length:342 Alcohol Dehydrogenase
	1llu_G	32	92	61	n/a	17.84	342	49.18	13.11	1e-10	mol:protein length:342 Alcohol Dehydrogenase
	1llu_F	32	92	61	n/a	17.84	342	49.18	13.11	1e-10	mol:protein length:342 Alcohol Dehydrogenase
	1llu_E	32	92	61	n/a	17.84	342	49.18	13.11	1e-10	mol:protein length:342 Alcohol Dehydrogenase
	1llu_D	32	92	61	n/a	17.84	342	49.18	13.11	1e-10	mol:protein length:342 Alcohol Dehydrogenase
	1llu_C	32	92	61	n/a	17.84	342	49.18	13.11	1e-10	mol:protein length:342 Alcohol Dehydrogenase
rpsblast_cdd	gnl\|CDD\|176257	37	122	86	Gaps:1	25.51	341	64.37	8.05	2e-35	cd08297 CAD3 Cinnamyl alcohol dehydrogenases (CAD). These alcohol dehydrogenases are related to the cinnamyl alcohol dehydrogenases (CAD) members of the medium chain dehydrogenase/reductase family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. Cinnamyl alcohol dehydrogenases (CAD) reduce cinnamaldehydes to cinnamyl alcohols in the last step of monolignal metabolism in plant cells walls. CAD binds 2 zinc ions and is NADPH- dependent. CAD family members are also found in non-plant species e.g. in yeast where they have an aldehyde reductase activity. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins is a diverse group of proteins related to the first identified member class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities including the founding alcohol dehydrogenase (ADH) quinone reductase sorbitol dehydrogenase formaldehyde dehydrogenase butanediol DH ketose reductase cinnamyl reductase and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants mammals) or tetramers (yeast bacteria) and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine two cysteines and a water molecule. The second zinc seems to play a structural role affects subunit interactions and is typically coordinated by 4 cysteines.
	gnl\|CDD\|31264	34	122	89	Gaps:1	25.96	339	47.73	15.91	1e-25	COG1064 AdhP Zn-dependent alcohol dehydrogenases [General function prediction only].
	gnl\|CDD\|176207	38	122	85	Gaps:1	25.45	330	53.57	10.71	5e-25	cd08245 CAD Cinnamyl alcohol dehydrogenases (CAD) and related proteins. Cinnamyl alcohol dehydrogenases (CAD) members of the medium chain dehydrogenase/reductase family reduce cinnamaldehydes to cinnamyl alcohols in the last step of monolignal metabolism in plant cells walls. CAD binds 2 zinc ions and is NADPH- dependent. CAD family members are also found in non-plant species e.g. in yeast where they have an aldehyde reductase activity. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins is a diverse group of proteins related to the first identified member class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities including the founding alcohol dehydrogenase (ADH) quinone reductase sorbitol dehydrogenase formaldehyde dehydrogenase butanediol DH ketose reductase cinnamyl reductase and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants mammals) or tetramers (yeast bacteria) and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine two cysteines and a water molecule. The second zinc seems to play a structural role affects subunit interactions and is typically coordinated by 4 cysteines.
	gnl\|CDD\|176240	39	117	79	Gaps:2	21.21	363	53.25	11.69	1e-24	cd08279 Zn_ADH_class_III Class III alcohol dehydrogenase. Glutathione-dependent formaldehyde dehydrogenases (FDHs Class III ADH) are members of the zinc-dependent/medium chain alcohol dehydrogenase family. FDH converts formaldehyde and NAD(P) to formate and NAD(P)H. The initial step in this process the spontaneous formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione followed by FDH-mediated oxidation (and detoxification) of the adduct to S-formylglutathione. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. Class III ADH are also known as glutathione-dependent formaldehyde dehydrogenase (FDH) which convert aldehydes to corresponding carboxylic acid and alcohol. ADH is a member of the medium chain alcohol dehydrogenase family (MDR) which has a NAD(P)(H)-binding domain in a Rossmann fold of an beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants mammals) or tetramers (yeast bacteria) and have 2 tightly bound zinc atoms per subunit a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding.
	gnl\|CDD\|176186	38	121	84	Gaps:3	24.04	337	43.21	13.58	9e-22	cd05283 CAD1 Cinnamyl alcohol dehydrogenases (CAD). Cinnamyl alcohol dehydrogenases (CAD) members of the medium chain dehydrogenase/reductase family reduce cinnamaldehydes to cinnamyl alcohols in the last step of monolignal metabolism in plant cells walls. CAD binds 2 zinc ions and is NADPH- dependent. CAD family members are also found in non-plant species e.g. in yeast where they have an aldehyde reductase activity. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins is a diverse group of proteins related to the first identified member class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities including the founding alcohol dehydrogenase (ADH) quinone reductase sorbitol dehydrogenase formaldehyde dehydrogenase butanediol DH ketose reductase cinnamyl reductase and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants mammals) or tetramers (yeast bacteria) and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine two cysteines and a water molecule. The second zinc seems to play a structural role affects subunit interactions and is typically coordinated by 4 cysteines.
	gnl\|CDD\|176239	39	117	79	Gaps:2	21.10	365	54.55	9.09	3e-21	cd08278 benzyl_alcohol_DH Benzyl alcohol dehydrogenase. Benzyl alcohol dehydrogenase is similar to liver alcohol dehydrogenase but has some amino acid substitutions near the active site which may determine the enzyme's specificity of oxidizing aromatic substrates. Also known as aryl-alcohol dehydrogenases they catalyze the conversion of an aromatic alcohol + NAD+ to an aromatic aldehyde + NADH + H+. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR) which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants mammals) or tetramers (yeast bacteria) and have 2 tightly bound zinc atoms per subunit a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis the zinc ion helps coordinate the alcohol followed by deprotonation of a histidine the ribose of NAD a serine then the alcohol which allows the transfer of a hydride to NAD+ creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria the active site zinc binds an aldehyde polarizing it and leading to the reverse reaction.
	gnl\|CDD\|176258	39	121	83	Gaps:5	26.14	329	47.67	11.63	4e-21	cd08298 CAD2 Cinnamyl alcohol dehydrogenases (CAD). These alcohol dehydrogenases are related to the cinnamyl alcohol dehydrogenases (CAD) members of the medium chain dehydrogenase/reductase family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. Cinnamyl alcohol dehydrogenases (CAD) reduce cinnamaldehydes to cinnamyl alcohols in the last step of monolignal metabolism in plant cells walls. CAD binds 2 zinc ions and is NADPH- dependent. CAD family members are also found in non-plant species e.g. in yeast where they have an aldehyde reductase activity. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins is a diverse group of proteins related to the first identified member class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities including the founding alcohol dehydrogenase (ADH) quinone reductase sorbitol dehydrogenase formaldehyde dehydrogenase butanediol DH ketose reductase cinnamyl reductase and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants mammals) or tetramers (yeast bacteria) and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine two cysteines and a water molecule. The second zinc seems to play a structural role affects subunit interactions and is typically coordinated by 4 cysteines.
	gnl\|CDD\|31262	39	118	80	Gaps:2	21.31	366	51.28	12.82	6e-21	COG1062 AdhC Zn-dependent alcohol dehydrogenases class III [Energy production and conversion].
	gnl\|CDD\|176187	39	117	79	Gaps:2	23.82	340	46.91	16.05	1e-19	cd05284 arabinose_DH_like D-arabinose dehydrogenase. This group contains arabinose dehydrogenase (AraDH) and related alcohol dehydrogenases. AraDH is a member of the medium chain dehydrogenase/reductase family and catalyzes the NAD(P)-dependent oxidation of D-arabinose and other pentoses the initial step in the metabolism of d-arabinose into 2-oxoglutarate. Like the alcohol dehydrogenases AraDH binds a zinc in the catalytic cleft as well as a distal structural zinc. AraDH forms homotetramers as a dimer of dimers. AraDH replaces a conserved catalytic His with replace with Arg compared to the canonical ADH site. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR) which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants mammals) or tetramers (yeast bacteria) and have 2 tightly bound zinc atoms per subunit a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis the zinc ion helps coordinate the alcohol followed by deprotonation of a histidine the ribose of NAD a serine then the alcohol which allows the transfer of a hydride to NAD+ creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria the active site zinc binds an aldehyde polarizing it and leading to the reverse reaction.
	gnl\|CDD\|176216	39	129	91	Gaps:2	26.33	338	46.07	16.85	6e-19	cd08254 hydroxyacyl_CoA_DH 6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase N-benzyl-3-pyrrolidinol dehydrogenase and other MDR family members. This group contains enzymes of the zinc-dependent alcohol dehydrogenase family including members (aka MDR) identified as 6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase and N-benzyl-3-pyrrolidinol dehydrogenase. 6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase catalyzes the conversion of 6-Hydroxycyclohex-1-enecarbonyl-CoA and NAD+ to 6-Ketoxycyclohex-1-ene-1-carboxyl-CoA NADH and H+. This group displays the characteristic catalytic and structural zinc sites of the zinc-dependent alcohol dehydrogenases. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR) which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants mammals) or tetramers (yeast bacteria) and have 2 tightly bound zinc atoms per subunit a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis the zinc ion helps coordinate the alcohol followed by deprotonation of a histidine the ribose of NAD a serine then the alcohol which allows the transfer of a hydride to NAD+ creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria the active site zinc binds an aldehyde polarizing it and leading to the reverse reaction.
rpsblast_kog	gnl\|CDD\|35246	28	127	100	Gaps:3	28.06	360	42.57	14.85	2e-26	KOG0023 KOG0023 KOG0023 Alcohol dehydrogenase class V [Secondary metabolites biosynthesis transport and catabolism].
	gnl\|CDD\|35245	39	118	80	Gaps:1	21.07	375	45.57	16.46	3e-17	KOG0022 KOG0022 KOG0022 Alcohol dehydrogenase class III [Secondary metabolites biosynthesis transport and catabolism].
	gnl\|CDD\|35247	59	117	59	Gaps:2	17.23	354	44.26	13.11	9e-09	KOG0024 KOG0024 KOG0024 Sorbitol dehydrogenase [Secondary metabolites biosynthesis transport and catabolism].
	gnl\|CDD\|36411	34	117	84	Gaps:3	25.30	336	38.82	7.06	1e-08	KOG1197 KOG1197 KOG1197 Predicted quinone oxidoreductase [Energy production and conversion General function prediction only].
	gnl\|CDD\|35248	52	119	68	n/a	19.21	354	36.76	23.53	7e-07	KOG0025 KOG0025 KOG0025 Zn2+-binding dehydrogenase (nuclear receptor binding factor-1) [Transcription Energy production and conversion].

Other analysis

Functional Gbrowse

Structural Gbrowse

Genome Mapping at gene locus

Analysis	Hit name	RefStart	RefEnd	Hit length	Hit identity	Hit coverage	eValue	Hit description
RepeatMasker_ALL_Repbase	no results
TRF	no results
REPET	no results
sim4_Bot_allest	YCNA_551466	93546	93927	631	99.02	48.49	n/a	Botrytis cinerea HortResearch libraries
	YCNA_551182	93546	93927	607	99.02	50.41	n/a	Botrytis cinerea HortResearch libraries
	YCMA_575731	93515	93927	658	99.11	51.22	n/a	Botrytis cinerea HortResearch libraries
	YCMA_571528	93487	93927	475	99.18	76.84	n/a	Botrytis cinerea HortResearch libraries
	YCMA_569060	93487	93927	665	99.18	54.89	n/a	Botrytis cinerea HortResearch libraries
	YCMA_566804	93487	93927	618	99.18	59.06	n/a	Botrytis cinerea HortResearch libraries
	YCMA_566781	93513	93927	592	99.12	57.26	n/a	Botrytis cinerea HortResearch libraries
	YCMA_566689	93487	93927	434	99.18	84.10	n/a	Botrytis cinerea HortResearch libraries
	YCMA_566415	93487	93927	498	99.18	73.29	n/a	Botrytis cinerea HortResearch libraries
	YCMA_563391	93487	93927	476	99.18	76.68	n/a	Botrytis cinerea HortResearch libraries
	YCIA_545664	93478	93927	570	99.20	65.61	n/a	Botrytis cinerea HortResearch libraries
	YCHA_544302	93484	93927	475	98.92	77.68	n/a	Botrytis cinerea HortResearch libraries
	YCGA_539540	93488	93927	560	99.18	65.00	n/a	Botrytis cinerea HortResearch libraries
	YCGA_535815	93483	93927	565	99.19	65.31	n/a	Botrytis cinerea HortResearch libraries
	YCMA_556854	93486	93927	547	98.63	66.91	n/a	Botrytis cinerea HortResearch libraries
	YCMA_576599	93513	93927	576	99.11	58.68	n/a	Botrytis cinerea HortResearch libraries
	YCMA_563266	93530	93927	430	99.07	74.65	n/a	Botrytis cinerea HortResearch libraries
	YCIA_547258	93487	93927	556	99.18	65.47	n/a	Botrytis cinerea HortResearch libraries
	YCMA_566851	93513	93927	534	98.82	63.30	n/a	Botrytis cinerea HortResearch libraries
	YCIA_545379	93582	93811	149	97.99	100.00	n/a	Botrytis cinerea HortResearch libraries
	B1BC_045_008_B01	93523	93927	541	98.78	60.81	n/a	BC ATCC 58025 (G3)
	B1BC_045_038_B02	93513	93927	670	98.82	50.60	n/a	BC ATCC 58025 (G3)
	B1BC_045_039_A05	93492	93927	687	98.89	52.40	n/a	BC ATCC 58025 (G3)
	AL116780	93500	93620	132	100.00	91.67	n/a	BT4 Mycelium - nitrate starvation library
	PD0ABA34YF14FM1	93475	93927	691	99.20	54.56	n/a	BT4 young mycelium library
	PD0ABA34YE06FM1	93485	93927	681	99.18	53.89	n/a	BT4 young mycelium library
	PD0ABA30YM12FM1	93474	93927	598	99.21	63.21	n/a	BT4 young mycelium library
	PD0ABA28YG13FM1	93472	93927	707	99.21	53.75	n/a	BT4 young mycelium library
	PD0ABA28YE04FM1	93492	93927	716	99.17	50.28	n/a	BT4 young mycelium library
	PD0ABA21YP09FM1	93473	93927	726	99.21	52.20	n/a	BT4 young mycelium library
	PD0ABA11YC16FM1	93480	93927	658	99.19	56.53	n/a	BT4 young mycelium library
	PD0AEA6YF11CM1	93466	93927	699	99.22	55.08	n/a	BT4 appressoria on teflon library
	PD0AEA2YP14CM1	93476	93927	606	99.20	62.05	n/a	BT4 appressoria on teflon library
	PD0AGA8YP22CM1	93458	93927	698	99.24	56.45	n/a	BT4 mycelium - different stresses library
	PD0AGA6YD20CM1	93469	93927	601	99.22	63.73	n/a	BT4 mycelium - different stresses library
	PD0AGA5YG03CM1	93469	93927	642	99.22	59.66	n/a	BT4 mycelium - different stresses library
	PD0AGA3YC09CM1	93465	93927	537	98.97	72.07	n/a	BT4 mycelium - different stresses library
	PD0AGA19YH15CM1	93455	93927	638	99.24	62.23	n/a	BT4 mycelium - different stresses library
	PD0AGA19YC13CM1	93465	93927	613	99.22	63.13	n/a	BT4 mycelium - different stresses library
	PD0AGA15YG13CM1	93458	93927	520	99.24	75.77	n/a	BT4 mycelium - different stresses library
	PD0AHA3YE19CM1	93458	93927	698	99.24	56.45	n/a	BT4 appressoria on teflon library
	PD0AHA17YM07CM1	93454	93927	613	99.25	64.93	n/a	BT4 appressoria on teflon library
	PD0AHA16YE17CM1	93469	93927	644	99.22	59.47	n/a	BT4 appressoria on teflon library
	PD0AHA16YB23CM1	93454	93927	641	99.25	62.09	n/a	BT4 appressoria on teflon library
	PD0AHA11YM24CM1	93454	93927	674	99.25	59.05	n/a	BT4 appressoria on teflon library
	PD0AHA8YB11CM1	93532	93931	461	98.43	69.20	n/a	BT4 appressoria on teflon library
	PD0AHA17YH14CM1	93603	93927	652	97.99	38.19	n/a	BT4 appressoria on teflon library
	PD0AHA12YH18CM1	93454	93927	641	98.74	62.09	n/a	BT4 appressoria on teflon library
sim4_Bot_allest4_clctg	no results
sim4_Ss_allest	no results
blastx_uniprot_sprot	Q9P6C8	93575	93923	353	75.00	24.93	n/a	Alcohol dehydrogenase 1 - Neurospora crassa
	P07754	93572	93923	352	67.78	25.57	n/a	Alcohol dehydrogenase 3 - Emericella nidulans (Aspergillus nidulans)
	P41747	93572	93923	349	65.17	25.50	n/a	Alcohol dehydrogenase 1 - Aspergillus flavus
	O94038	93708	93923	348	76.39	20.69	n/a	Alcohol dehydrogenase 2 - Candida albicans (Yeast)
	O13309	93702	93923	348	70.27	21.26	n/a	Alcohol dehydrogenase 2 - Pichia stipitis (Yeast)
	Q9P4C2	93708	93923	348	72.22	20.69	n/a	Alcohol dehydrogenase 2 - Kluyveromyces marxianus (Yeast) (Candida kefyr)
	P20369	93708	93923	350	72.22	20.57	n/a	Alcohol dehydrogenase 1 - Kluyveromyces lactis (Yeast) (Candida sphaerica)
	Q07288	93708	93923	348	70.83	20.69	n/a	Alcohol dehydrogenase 1 - Kluyveromyces marxianus (Yeast) (Candida kefyr)
	P08843	93572	93923	350	62.92	25.43	n/a	Alcohol dehydrogenase 1 - Emericella nidulans (Aspergillus nidulans)
	O00097	93702	93923	348	68.92	21.26	n/a	Alcohol dehydrogenase 1 - Pichia stipitis (Yeast)
blastx_uniprot_trembl	Q2HYZ7	93566	93923	352	83.52	25.85	n/a	Alcohol dehydrogenase - Curvularia lunata
	A1YDT6	93566	93923	352	82.42	25.85	n/a	Can a 1 allergen-like - Curvularia lunata
	Q0UHT9	93566	93923	352	79.12	25.85	n/a	Putative uncharacterized protein - Phaeosphaeria nodorum (Septoria nodorum)
	A4R4C9	93566	93923	352	76.67	25.57	n/a	Putative uncharacterized protein - Magnaporthe grisea (Rice blast fungus) (Pyricularia grisea)
	Q2GPB9	93575	93923	356	78.41	24.72	n/a	Alcohol dehydrogenase I - Chaetomium globosum (Soil fungus)
	Q27JP7	93575	93923	353	75.00	24.93	n/a	Alcohol dehydrogenase I - Metarhizium anisopliae
	A2R9I3	93575	93923	350	71.26	24.86	n/a	Alcohol-dehydrogenase adhA from patent WO8704464-A-Aspergillus niger - Aspergillus niger
	Q0CA77	93572	93923	350	69.32	25.14	n/a	Alcohol dehydrogenase I - Aspergillus terreus (strain NIH 2624)
blastx_FNG30_prot	SS1G_13409.1	93702	93923	357	91.89	20.73	n/a	sclerotinia_sclerotiorum hypothetical protein translation 358 aa
	SNU08675.1	93566	93923	352	79.12	25.85	n/a	Stagonospora nodorum predicted protein translation
	MGG_03880.5	93566	93923	352	76.67	25.57	n/a	magnaporthe_grisea hypothetical protein translation 353 aa
	jgi:Triree:45647	93702	93923	353	83.78	20.96	n/a	Trichoderma reesei
	CHG10185.1	93575	93923	356	78.41	24.72	n/a	Chaetomium globosum hypothetical protein translation 357 aa
	FG10855.1	93575	93923	388	74.73	23.45	n/a	fusarium_graminearum hypothetical protein 389 aa
	NCU01754.2	93575	93923	353	75.00	24.93	n/a	Neurospora crassa ALCOHOL DEHYDROGENASE I [MIPS] translation 354 aa
	CIMG_06053.2	93560	93923	355	70.33	25.63	n/a	Coccidioides immitis hypothetical protein translation 356 aa
	NCU02476.2	93557	93923	353	67.02	26.63	n/a	Neurospora crassa conserved hypothetical protein translation 354 aa
	AN2286	93572	93923	352	67.78	25.57	n/a	Aspergillus nidulans AN2286.3 alcohol dehydrogenase III translation 353 aa
sim4_B0510_genes	BC1G_06394.1	93566	93927	1056	98.95	27.08	n/a	n/a
sim4_SS_genes	SS1G_13409.1	93566	93923	1074	82.80	25.98	n/a	n/a
blastn_b0510_supercontig	B0510_supercontig_1.34	87739	93980	341132	100.00	n/a	n/a	n/a
blastn_SS_supercontig	SS_supercontig_1.25	93718	93930	505126	81.22	n/a	n/a	n/a
blat_oligo	botrytisP00084587	93152	93542	60	n/a	n/a	n/a	array_gene:BofuT4_P062770_1 . max_over_threshold:1.93 . min_over_threshold:0.38 . percent_hyb_over_threshold:35.71 . flag_cross_hyb_gene:0 . flag_cross_hyb_organism:0
	botrytisP00084588	93156	93546	60	n/a	n/a	n/a	array_gene:BofuT4_P062770_1 . max_over_threshold:6.48 . min_over_threshold:0.48 . percent_hyb_over_threshold:64.28 . flag_cross_hyb_gene:0 . flag_cross_hyb_organism:0
	botrytisP00084589	93163	93553	60	n/a	n/a	n/a	array_gene:BofuT4_P062770_1 . max_over_threshold:22.19 . min_over_threshold:0.73 . percent_hyb_over_threshold:92.85 . flag_cross_hyb_gene:0 . flag_cross_hyb_organism:1
	botrytisP00084590	93175	93565	60	n/a	n/a	n/a	array_gene:BofuT4_P062770_1 . max_over_threshold:75.62 . min_over_threshold:0.91 . percent_hyb_over_threshold:96.42 . flag_cross_hyb_gene:0 . flag_cross_hyb_organism:0
	botrytisP00084591	93763	93822	60	n/a	n/a	n/a	array_gene:BofuT4_P062770_1 . max_over_threshold:127.83 . min_over_threshold:1.9 . percent_hyb_over_threshold:100 . flag_cross_hyb_gene:0 . flag_cross_hyb_organism:0
	botrytisP00084592	93768	93827	60	n/a	n/a	n/a	array_gene:BofuT4_P062770_1 . max_over_threshold:122.73 . min_over_threshold:1.91 . percent_hyb_over_threshold:100 . flag_cross_hyb_gene:0 . flag_cross_hyb_organism:0
	botrytisP00084593	93774	93833	60	n/a	n/a	n/a	array_gene:BofuT4_P062770_1 . max_over_threshold:106.17 . min_over_threshold:1.63 . percent_hyb_over_threshold:100 . flag_cross_hyb_gene:0 . flag_cross_hyb_organism:0
	botrytisP00084594	93791	93850	60	n/a	n/a	n/a	array_gene:BofuT4_P062770_1 . max_over_threshold:125.46 . min_over_threshold:2.12 . percent_hyb_over_threshold:100 . flag_cross_hyb_gene:0 . flag_cross_hyb_organism:0
	botrytisP00084596	93807	93866	60	n/a	n/a	n/a	array_gene:BofuT4_P062770_1 . max_over_threshold:146.49 . min_over_threshold:2.64 . percent_hyb_over_threshold:100 . flag_cross_hyb_gene:0 . flag_cross_hyb_organism:0

Current manual annotation

Ortholog