GRS - Genome Report System

Botrytis cinerea T4 GRS

Functional annotation

BofuT4_P062780.1

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	1	157	157	n/a	44.73	351	100.00	0.00	2e-87	hypothetical protein K13953 alcohol dehydrogenase propanol-preferring [EC:1.1.1.1]
	ssl:SS1G_13409	1	144	144	n/a	40.34	357	94.44	3.47	1e-75	hypothetical protein K13953 alcohol dehydrogenase propanol-preferring [EC:1.1.1.1]
	pno:SNOG_08675	1	157	157	Gaps:1	44.89	352	77.22	11.39	2e-65	hypothetical protein K13953 alcohol dehydrogenase propanol-preferring [EC:1.1.1.1]
	pan:PODANSg6586	1	157	157	n/a	44.35	354	70.70	14.65	5e-61	hypothetical protein K13953 alcohol dehydrogenase propanol-preferring [EC:1.1.1.1]
	ncr:NCU01754	1	157	157	n/a	44.48	353	72.61	11.46	8e-61	alcohol dehydrogenase I K13953 alcohol dehydrogenase propanol-preferring [EC:1.1.1.1]
	zma:100274539	1	157	157	n/a	44.48	353	69.43	13.38	1e-60	hypothetical protein LOC100274539 K13953 alcohol dehydrogenase propanol-preferring [EC:1.1.1.1]
	fgr:FG10855.1	1	157	157	n/a	40.46	388	66.88	14.01	3e-58	hypothetical protein K13953 alcohol dehydrogenase propanol-preferring [EC:1.1.1.1]
	nfi:NFIA_113720	1	154	154	n/a	43.63	353	70.78	12.99	4e-58	alcohol dehydrogenase K13953 alcohol dehydrogenase propanol-preferring [EC:1.1.1.1]
	pcs:Pc12g07100	1	154	154	n/a	43.87	351	70.13	14.29	9e-58	Pc12g07100 K13953 alcohol dehydrogenase propanol-preferring [EC:1.1.1.1]
	afv:AFLA_048690	1	154	154	n/a	44.00	350	68.18	16.23	2e-57	alcohol dehydrogenase putative K13953 alcohol dehydrogenase propanol-preferring [EC:1.1.1.1]
blastp_uniprot_sprot	sp\|Q9P6C8\|ADH1_NEUCR	1	157	157	n/a	44.48	353	72.61	11.46	1e-61	Alcohol dehydrogenase 1 OS Neurospora crassa GN adh-1 PE 3 SV 1
	sp\|P41747\|ADH1_ASPFN	1	154	154	n/a	44.00	350	68.18	16.23	3e-58	Alcohol dehydrogenase 1 OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM 12722 / SRRC 167) GN adh1 PE 2 SV 2
	sp\|P08843\|ADH1_EMENI	1	154	154	n/a	44.00	350	65.58	16.23	3e-56	Alcohol dehydrogenase 1 OS Emericella nidulans GN alcA PE 3 SV 2
	sp\|P07754\|ADH3_EMENI	1	154	154	n/a	43.75	352	63.64	16.88	9e-53	Alcohol dehydrogenase 3 OS Emericella nidulans GN alcC PE 3 SV 1
	sp\|O00097\|ADH1_PICST	1	157	157	Gaps:2	44.54	348	62.58	14.19	2e-48	Alcohol dehydrogenase 1 OS Pichia stipitis GN ADH1 PE 3 SV 1
	sp\|P43067\|ADH1_CANAL	1	157	157	Gaps:2	44.29	350	60.65	14.19	6e-46	Alcohol dehydrogenase 1 OS Candida albicans GN ADH1 PE 1 SV 1
	sp\|P07246\|ADH3_YEAST	1	157	157	Gaps:2	41.33	375	56.77	18.06	8e-46	Alcohol dehydrogenase 3 mitochondrial OS Saccharomyces cerevisiae GN ADH3 PE 1 SV 2
	sp\|O94038\|ADH2_CANAL	1	157	157	Gaps:2	44.54	348	56.13	15.48	1e-43	Alcohol dehydrogenase 2 OS Candida albicans GN ADH2 PE 1 SV 1
	sp\|O13309\|ADH2_PICST	1	157	157	Gaps:2	44.54	348	60.65	14.19	7e-43	Alcohol dehydrogenase 2 OS Pichia stipitis GN ADH2 PE 3 SV 1
	sp\|P49384\|ADH3_KLULA	1	157	157	Gaps:2	41.44	374	52.26	18.06	1e-41	Alcohol dehydrogenase 3 mitochondrial OS Kluyveromyces lactis GN ADH3 PE 3 SV 2
blastp_pdb	2hcy_D	1	157	157	Gaps:2	44.67	347	47.74	20.00	3e-35	mol:protein length:347 Alcohol dehydrogenase 1
	2hcy_C	1	157	157	Gaps:2	44.67	347	47.74	20.00	3e-35	mol:protein length:347 Alcohol dehydrogenase 1
	2hcy_B	1	157	157	Gaps:2	44.67	347	47.74	20.00	3e-35	mol:protein length:347 Alcohol dehydrogenase 1
	2hcy_A	1	157	157	Gaps:2	44.67	347	47.74	20.00	3e-35	mol:protein length:347 Alcohol dehydrogenase 1
	1llu_H	1	154	154	Gaps:5	43.57	342	37.58	18.79	1e-18	mol:protein length:342 Alcohol Dehydrogenase
	1llu_G	1	154	154	Gaps:5	43.57	342	37.58	18.79	1e-18	mol:protein length:342 Alcohol Dehydrogenase
	1llu_F	1	154	154	Gaps:5	43.57	342	37.58	18.79	1e-18	mol:protein length:342 Alcohol Dehydrogenase
	1llu_E	1	154	154	Gaps:5	43.57	342	37.58	18.79	1e-18	mol:protein length:342 Alcohol Dehydrogenase
	1llu_D	1	154	154	Gaps:5	43.57	342	37.58	18.79	1e-18	mol:protein length:342 Alcohol Dehydrogenase
	1llu_C	1	154	154	Gaps:5	43.57	342	37.58	18.79	1e-18	mol:protein length:342 Alcohol Dehydrogenase
rpsblast_cdd	gnl\|CDD\|176257	1	154	154	Gaps:2	44.57	341	48.68	17.76	2e-50	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	1	157	157	Gaps:10	44.54	339	35.76	19.21	2e-26	COG1064 AdhP Zn-dependent alcohol dehydrogenases [General function prediction only].
	gnl\|CDD\|176207	1	153	153	Gaps:7	44.24	330	26.71	22.60	1e-21	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\|169856	1	154	154	Gaps:8	44.38	338	36.67	17.33	3e-21	PRK09422 PRK09422 alcohol dehydrogenase Provisional.
	gnl\|CDD\|176187	5	153	149	Gaps:5	42.35	340	29.17	20.83	3e-17	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\|143884	5	117	113	Gaps:2	84.73	131	36.94	19.82	1e-14	pfam00107 ADH_zinc_N Zinc-binding dehydrogenase.
	gnl\|CDD\|176224	4	154	151	Gaps:7	41.96	367	31.17	14.94	2e-14	cd08263 Zn_ADH10 Alcohol dehydrogenases of the MDR family. 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.
	gnl\|CDD\|176202	5	153	149	Gaps:5	41.71	350	28.08	17.12	1e-13	cd08240 6_hydroxyhexanoate_dh_like 6-hydroxyhexanoate dehydrogenase. 6-hydroxyhexanoate dehydrogenase an enzyme of the zinc-dependent alcohol dehydrogenase-like family of medium chain dehydrogenases/reductases catalyzes the conversion of 6-hydroxyhexanoate and NAD(+) to 6-oxohexanoate + NADH and 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\|31263	4	146	143	Gaps:5	41.71	350	26.03	16.44	2e-12	COG1063 Tdh Threonine dehydrogenase and related Zn-dependent dehydrogenases [Amino acid transport and metabolism / General function prediction only].
	gnl\|CDD\|176198	4	148	145	Gaps:13	44.31	343	26.32	17.11	7e-12	cd08236 sugar_DH NAD(P)-dependent sugar dehydrogenases. This group contains proteins identified as sorbitol dehydrogenases and other sugar dehydrogenases of the medium-chain dehydrogenase/reductase family (MDR) which includes zinc-dependent alcohol dehydrogenase and related proteins. Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway which interconverts glucose and fructose. Sorbitol dehydrogenase is tetrameric and has a single catalytic zinc per subunit. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. Related proteins include threonine dehydrogenase formaldehyde dehydrogenase and butanediol dehydrogenase. The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants mammals) or tetramers (yeast bacteria) and have 2 tightly bound zinc atoms per subunit. Horse liver alcohol dehydrogenase is a dimeric enzyme and each subunit has two domains. The NAD binding domain is in a Rossmann fold and the catalytic domain contains a zinc ion to which substrates bind. There is a cleft between the domains that closes upon formation of the ternary complex.
rpsblast_kog	gnl\|CDD\|35246	1	157	157	Gaps:6	42.50	360	34.64	22.88	2e-34	KOG0023 KOG0023 KOG0023 Alcohol dehydrogenase class V [Secondary metabolites biosynthesis transport and catabolism].

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	YCOA_572637	94449	94829	381	100.00	100.00	n/a	Botrytis cinerea HortResearch libraries
	YCMA_571601	94236	94749	514	100.00	100.00	n/a	Botrytis cinerea HortResearch libraries
	YCOA_572637	94449	94829	381	100.00	100.00	n/a	Botrytis cinerea HortResearch libraries
	YCNA_551466	94135	94478	631	98.54	54.20	n/a	Botrytis cinerea HortResearch libraries
	YCMA_575731	94135	94475	658	97.93	51.37	n/a	Botrytis cinerea HortResearch libraries
	YCNA_551182	94135	94454	607	98.11	52.39	n/a	Botrytis cinerea HortResearch libraries
	YCMA_569060	94135	94453	665	98.11	47.67	n/a	Botrytis cinerea HortResearch libraries
	BcA1_3466_N02	94135	94534	724	98.49	54.97	n/a	BC A1 mycelium
	B1BC_045_052_F04	94135	94681	894	99.27	60.96	n/a	BC ATCC 58025 (G3)
	B1BC_045_042_B06	94135	94629	789	99.19	62.48	n/a	BC ATCC 58025 (G3)
	B1BC_045_032_A12	94135	94603	705	99.14	66.24	n/a	BC ATCC 58025 (G3)
	B1BC_045_038_B02	94135	94484	670	97.99	51.94	n/a	BC ATCC 58025 (G3)
	B1BC_045_039_A05	94135	94478	687	97.97	50.07	n/a	BC ATCC 58025 (G3)
	AL113869	94262	94901	640	99.69	100.00	n/a	BT4 Mycelium - nitrate starvation library
	AL114462	94221	94870	700	98.16	93.14	n/a	BT4 Mycelium - nitrate starvation library
	AL114143	94210	94835	626	99.20	100.00	n/a	BT4 Mycelium - nitrate starvation library
	AL115374	94135	94570	615	99.08	70.57	n/a	BT4 Mycelium - nitrate starvation library
	PD0ABA19YJ11FM1	94143	94809	665	99.70	100.00	n/a	BT4 young mycelium library
	PD0ABA27YI23FM1	94135	94755	734	99.19	84.33	n/a	BT4 young mycelium library
	PD0ABA17YF03FM1	94135	94584	771	99.11	58.11	n/a	BT4 young mycelium library
	PD0ABA24YP09FM1	94135	94582	656	99.10	67.99	n/a	BT4 young mycelium library
	PD0ABA15YD06FM1	94135	94562	625	99.06	68.16	n/a	BT4 young mycelium library
	PD0ABA28YM05FM1	94135	94526	739	98.71	52.64	n/a	BT4 young mycelium library
	PD0ABA28YE04FM1	94135	94510	716	98.93	52.09	n/a	BT4 young mycelium library
	PD0ABA39YI07FM1	94135	94500	653	98.63	55.74	n/a	BT4 young mycelium library
	PD0ABA21YP09FM1	94135	94500	726	98.63	50.14	n/a	BT4 young mycelium library
	PD0ABA34YB02FM1	94135	94495	669	98.61	53.66	n/a	BT4 young mycelium library
	PD0AEA5YH07CM1	94250	94919	670	100.00	100.00	n/a	BT4 appressoria on teflon library
	PD0AEA6YJ18CM1	94143	94808	664	99.25	100.00	n/a	BT4 appressoria on teflon library
	PD0AGA18YB21CM1	94189	94917	728	99.73	100.00	n/a	BT4 mycelium - different stresses library
	PD0AGA8YP22CM1	94135	94457	698	98.44	45.99	n/a	BT4 mycelium - different stresses library
	PD0AHA11YP21CM1	94271	94853	583	99.83	100.00	n/a	BT4 appressoria on teflon library
	PD0AHA3YI15CM1	94135	94685	659	98.91	83.31	n/a	BT4 appressoria on teflon library
	PD0AHA17YH14CM1	94143	94556	652	99.51	63.19	n/a	BT4 appressoria on teflon library
	PD0AHA3YE19CM1	94135	94457	698	98.44	45.99	n/a	BT4 appressoria on teflon library
	YCHA_541266	94566	95088	524	96.76	100.00	n/a	Botrytis cinerea HortResearch libraries
	B3BC_116_205_A07	94685	95094	410	100.00	100.00	n/a	B0510 Germinated spores on hydrophobic surfaces library
	AL113421	94489	95068	580	99.83	100.00	n/a	BT4 Mycelium - nitrate starvation library
	AL114812	94490	95045	556	99.82	100.00	n/a	BT4 Mycelium - nitrate starvation library
	AL114598	94674	95073	400	100.00	100.00	n/a	BT4 Mycelium - nitrate starvation library
	PD0ABA8YH18FM1	94490	95089	599	100.00	100.00	n/a	BT4 young mycelium library
	PD0ABA19YA12FM1	94657	95088	432	100.00	100.00	n/a	BT4 young mycelium library
	PD0ACA25YE13FM1	94767	95032	266	100.00	100.00	n/a	BT4 mycelium - pH stress library
	PD0AEA4YL23CM1	94472	95091	620	100.00	100.00	n/a	BT4 appressoria on teflon library
	BcA1_3479_D17	94244	94971	727	100.00	100.00	n/a	BC A1 mycelium
	AL115373	94398	95013	616	99.68	100.00	n/a	BT4 Mycelium - nitrate starvation library
	AL116307	94382	95094	726	93.11	100.00	n/a	BT4 Mycelium - nitrate starvation library
	PD0ABA11YC16NM1r	94219	95070	852	100.00	100.00	n/a	BT4 young mycelium library
	PD0ABA22YN10FM1	94231	94972	742	99.87	100.00	n/a	BT4 young mycelium library
	PD0ABA29YK06FM1	94376	94984	609	100.00	100.00	n/a	BT4 young mycelium library
sim4_Bot_allest4_clctg	SCL_bt4ctg_0799_bt4_SuperContig_59_1_bt4ctg_0800.Contig1_v5	94135	95094	1341	99.38	71.59	n/a	all_lib_clone_nr:61
sim4_Ss_allest	G781P583FC8.T0	94286	94934	809	87.11	71.94	n/a	Ss ESTs grown as developing sclerotia
	G786P519FB7.T0	94282	94934	860	86.73	68.37	n/a	Ss ESTs grown as mycelia at neutral pH
	G865P38FF7.T0	94369	94930	746	87.45	67.29	n/a	Ss ESTs in planta set from infected Brassica napus
	G786P524FB7.T0	94378	94934	789	87.45	62.61	n/a	Ss ESTs grown as mycelia at neutral pH
	G865P38RF7.T0	94393	94934	686	88.74	63.41	n/a	Ss ESTs in planta set from infected Brassica napus
	G781P560FG6.T0	94384	94934	784	87.84	61.86	n/a	Ss ESTs grown as developing sclerotia
	G781P578FB6.T0	94282	94934	817	85.93	71.36	n/a	Ss ESTs grown as developing sclerotia
	G787P599FA5.T0	94398	94934	753	87.13	62.95	n/a	Ss ESTs grown as developing apothecia
blastx_uniprot_sprot	Q9P6C8	94145	94920	353	78.12	72.52	n/a	Alcohol dehydrogenase 1 - Neurospora crassa
	P41747	94145	94911	349	73.81	72.21	n/a	Alcohol dehydrogenase 1 - Aspergillus flavus
	P08843	94170	94911	350	70.04	70.57	n/a	Alcohol dehydrogenase 1 - Emericella nidulans (Aspergillus nidulans)
	P07754	94145	94911	352	69.57	71.88	n/a	Alcohol dehydrogenase 3 - Emericella nidulans (Aspergillus nidulans)
	O00097	94145	94920	348	65.10	73.28	n/a	Alcohol dehydrogenase 1 - Pichia stipitis (Yeast)
	O13309	94219	94920	348	62.93	66.67	n/a	Alcohol dehydrogenase 2 - Pichia stipitis (Yeast)
	P43067	94145	94920	350	61.57	72.86	n/a	Alcohol dehydrogenase 1 - Candida albicans (Yeast)
	O94038	94145	94920	348	59.22	73.28	n/a	Alcohol dehydrogenase 2 - Candida albicans (Yeast)
	P07246	94219	94920	375	57.76	61.87	n/a	Alcohol dehydrogenase 3 mitochondrial precursor - Saccharomyces cerevisiae (Baker's yeast)
	P49385	94210	94920	375	56.60	62.67	n/a	Alcohol dehydrogenase 4 mitochondrial precursor - Kluyveromyces lactis (Yeast) (Candida sphaerica)
blastx_uniprot_trembl	Q0UHT9	94145	94920	352	82.56	73.30	n/a	Putative uncharacterized protein - Phaeosphaeria nodorum (Septoria nodorum)
	Q2HYZ7	94170	94920	352	81.20	71.02	n/a	Alcohol dehydrogenase - Curvularia lunata
	A1YDT6	94170	94920	352	80.80	71.02	n/a	Can a 1 allergen-like - Curvularia lunata
	Q27JP7	94145	94920	353	77.73	72.52	n/a	Alcohol dehydrogenase I - Metarhizium anisopliae
	Q2GPB9	94145	94920	356	74.62	73.03	n/a	Alcohol dehydrogenase I - Chaetomium globosum (Soil fungus)
	Q2UTQ7	94145	94911	350	73.91	72.29	n/a	Alcohol dehydrogenase - Aspergillus oryzae
	A1D8Y0	94170	94911	353	74.29	69.41	n/a	Alcohol dehydrogenase - Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / NRRL 181) (Aspergillus fischerianus (strain ATCC 1020 / DSM 3700 / NRRL 181))
	Q4WAE4	94170	94911	353	73.88	69.41	n/a	Alcohol dehydrogenase putative - Aspergillus fumigatus (Sartorya fumigata)
blastx_FNG30_prot	SS1G_13409.1	94145	94881	357	95.49	68.35	n/a	sclerotinia_sclerotiorum hypothetical protein translation 358 aa
	SNU08675.1	94145	94920	352	82.56	73.30	n/a	Stagonospora nodorum predicted protein translation
	NCU01754.2	94145	94920	353	78.12	72.52	n/a	Neurospora crassa ALCOHOL DEHYDROGENASE I [MIPS] translation 354 aa
	CHG10185.1	94145	94920	356	74.62	73.03	n/a	Chaetomium globosum hypothetical protein translation 357 aa
	AO090009000634	94145	94911	350	73.91	72.29	n/a	Aspergillus oryzae alcohol dehydrogenase class V
	FG10855.1	94141	94920	388	67.94	67.53	n/a	fusarium_graminearum hypothetical protein 389 aa
	gi:70982604:ref:XP_746830.1:	94170	94911	353	73.88	69.41	n/a	Aspergillus fumigatus Af293 alcohol dehydrogenase
	jgi:Triree:45647	94147	94920	353	68.46	73.65	n/a	Trichoderma reesei
	gi:70998574:ref:XP_754009.1:	94170	94911	350	69.64	70.57	n/a	Aspergillus fumigatus Af293 alcohol dehydrogenase
	AN8979	94170	94911	350	70.04	70.57	n/a	Aspergillus nidulans AN8979.3 alcohol dehydrogenase I translation 351 aa
sim4_B0510_genes	no results
sim4_SS_genes	SS1G_13409.1	94135	94882	1074	86.13	63.78	n/a	n/a
blastn_b0510_supercontig	B0510_supercontig_1.34	94131	99666	341132	99.93	n/a	n/a	n/a
blastn_SS_supercontig	SS_supercontig_1.25	94209	94927	505126	84.56	n/a	n/a	n/a
blat_oligo	botrytisP00084597	94522	94581	60	n/a	n/a	n/a	array_gene:BofuT4_P062780_1 . max_over_threshold:169.45 . min_over_threshold:22.28 . percent_hyb_over_threshold:100 . flag_cross_hyb_gene:0 . flag_cross_hyb_organism:1
	botrytisP00084598	94625	94684	60	n/a	n/a	n/a	array_gene:BofuT4_P062780_1 . max_over_threshold:225.97 . min_over_threshold:18.9 . percent_hyb_over_threshold:100 . flag_cross_hyb_gene:0 . flag_cross_hyb_organism:1
	botrytisP00084599	94682	94741	60	n/a	n/a	n/a	array_gene:BofuT4_P062780_1 . max_over_threshold:182.12 . min_over_threshold:18.76 . percent_hyb_over_threshold:100 . flag_cross_hyb_gene:0 . flag_cross_hyb_organism:1
	botrytisP00084600	94731	94790	60	n/a	n/a	n/a	array_gene:BofuT4_P062780_1 . max_over_threshold:94.15 . min_over_threshold:6.09 . percent_hyb_over_threshold:100 . flag_cross_hyb_gene:0 . flag_cross_hyb_organism:0
	botrytisP00084601	94773	94832	60	n/a	n/a	n/a	array_gene:BofuT4_P062780_1 . max_over_threshold:95.83 . min_over_threshold:6 . percent_hyb_over_threshold:100 . flag_cross_hyb_gene:0 . flag_cross_hyb_organism:0
	botrytisP00084602	94779	94838	60	n/a	n/a	n/a	array_gene:BofuT4_P062780_1 . max_over_threshold:120.45 . min_over_threshold:9.53 . percent_hyb_over_threshold:100 . flag_cross_hyb_gene:0 . flag_cross_hyb_organism:0
	botrytisP00084603	94783	94842	60	n/a	n/a	n/a	array_gene:BofuT4_P062780_1 . max_over_threshold:146.09 . min_over_threshold:10.67 . percent_hyb_over_threshold:100 . flag_cross_hyb_gene:0 . flag_cross_hyb_organism:0
	botrytisP00084604	94789	94848	60	n/a	n/a	n/a	array_gene:BofuT4_P062780_1 . max_over_threshold:118.45 . min_over_threshold:5.42 . percent_hyb_over_threshold:100 . flag_cross_hyb_gene:0 . flag_cross_hyb_organism:0
	botrytisP00084605	94798	94857	60	n/a	n/a	n/a	array_gene:BofuT4_P062780_1 . max_over_threshold:92.93 . min_over_threshold:5.73 . percent_hyb_over_threshold:100 . flag_cross_hyb_gene:0 . flag_cross_hyb_organism:0

Current manual annotation

Ortholog