GRS - Genome Report System

Sclerotinia sclerotiorum GRS

Functional annotation

SS1G_13409.1

Gene Identifier

Domain/Motif (Interproscan results)

Localization / Targeting

Blast based analysis

Analysis	Hit	start	end	length	Note	Hit coverage	Hit length	Hit pident	Hit pcons	eValue	Hit description
blastp_kegg	ssl:SS1G_13409	1	357	357	n/a	100.00	357	94.12	0.00	0.0	hypothetical protein K13953 alcohol dehydrogenase propanol-preferring [EC:1.1.1.1]
	bfu:BC1G_06394	1	338	338	n/a	96.30	351	88.17	3.55	1e-167	hypothetical protein K13953 alcohol dehydrogenase propanol-preferring [EC:1.1.1.1]
	pno:SNOG_08675	1	338	338	Gaps:1	96.31	352	76.99	7.96	1e-143	hypothetical protein K13953 alcohol dehydrogenase propanol-preferring [EC:1.1.1.1]
	ncr:NCU01754	3	338	336	n/a	95.18	353	70.54	11.31	1e-138	alcohol dehydrogenase I K13953 alcohol dehydrogenase propanol-preferring [EC:1.1.1.1]
	zma:100274539	3	336	334	n/a	94.62	353	67.96	13.17	1e-135	hypothetical protein LOC100274539 K13953 alcohol dehydrogenase propanol-preferring [EC:1.1.1.1]
	pan:PODANSg6586	3	338	336	Gaps:1	95.20	354	69.73	12.17	1e-129	hypothetical protein K13953 alcohol dehydrogenase propanol-preferring [EC:1.1.1.1]
	fgr:FG10855.1	3	336	334	Gaps:35	95.10	388	60.16	12.74	1e-127	hypothetical protein K13953 alcohol dehydrogenase propanol-preferring [EC:1.1.1.1]
	cim:CIMG_06053	1	338	338	n/a	95.21	355	64.79	12.43	1e-126	hypothetical protein K13953 alcohol dehydrogenase propanol-preferring [EC:1.1.1.1]
	afv:AFLA_048690	3	338	336	n/a	96.00	350	66.96	13.99	1e-126	alcohol dehydrogenase putative K13953 alcohol dehydrogenase propanol-preferring [EC:1.1.1.1]
	aor:AO090009000634	3	338	336	n/a	96.00	350	66.96	13.99	1e-126	alcohol dehydrogenase class V K13953 alcohol dehydrogenase propanol-preferring [EC:1.1.1.1]
blastp_uniprot_sprot	sp\|Q9P6C8\|ADH1_NEUCR	3	338	336	n/a	95.18	353	70.54	11.31	1e-139	Alcohol dehydrogenase 1 OS Neurospora crassa GN adh-1 PE 3 SV 1
	sp\|P41747\|ADH1_ASPFN	3	338	336	n/a	96.00	350	66.96	13.99	1e-127	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	3	338	336	n/a	96.00	350	63.99	14.58	1e-119	Alcohol dehydrogenase 1 OS Emericella nidulans GN alcA PE 3 SV 2
	sp\|P07754\|ADH3_EMENI	3	338	336	Gaps:2	96.02	352	63.31	13.02	1e-116	Alcohol dehydrogenase 3 OS Emericella nidulans GN alcC PE 3 SV 1
	sp\|O94038\|ADH2_CANAL	3	338	336	Gaps:2	95.98	348	56.29	12.57	1e-103	Alcohol dehydrogenase 2 OS Candida albicans GN ADH2 PE 1 SV 1
	sp\|O00097\|ADH1_PICST	3	337	335	Gaps:2	95.69	348	59.46	12.91	1e-103	Alcohol dehydrogenase 1 OS Pichia stipitis GN ADH1 PE 3 SV 1
	sp\|O13309\|ADH2_PICST	3	338	336	Gaps:2	95.98	348	57.49	13.47	1e-102	Alcohol dehydrogenase 2 OS Pichia stipitis GN ADH2 PE 3 SV 1
	sp\|P49384\|ADH3_KLULA	3	338	336	Gaps:2	89.30	374	51.80	16.17	5e-99	Alcohol dehydrogenase 3 mitochondrial OS Kluyveromyces lactis GN ADH3 PE 3 SV 2
	sp\|P43067\|ADH1_CANAL	2	338	337	Gaps:2	95.71	350	57.91	11.94	1e-98	Alcohol dehydrogenase 1 OS Candida albicans GN ADH1 PE 1 SV 1
	sp\|P49385\|ADH4_KLULA	4	338	335	Gaps:2	88.80	375	52.55	15.92	1e-98	Alcohol dehydrogenase 4 mitochondrial OS Kluyveromyces lactis GN ADH4 PE 3 SV 2
blastp_pdb	2hcy_D	3	338	336	Gaps:2	96.25	347	49.70	15.87	2e-90	mol:protein length:347 Alcohol dehydrogenase 1
	2hcy_C	3	338	336	Gaps:2	96.25	347	49.70	15.87	2e-90	mol:protein length:347 Alcohol dehydrogenase 1
	2hcy_B	3	338	336	Gaps:2	96.25	347	49.70	15.87	2e-90	mol:protein length:347 Alcohol dehydrogenase 1
	2hcy_A	3	338	336	Gaps:2	96.25	347	49.70	15.87	2e-90	mol:protein length:347 Alcohol dehydrogenase 1
	1llu_H	3	336	334	Gaps:6	95.91	342	40.24	15.85	3e-61	mol:protein length:342 Alcohol Dehydrogenase
	1llu_G	3	336	334	Gaps:6	95.91	342	40.24	15.85	3e-61	mol:protein length:342 Alcohol Dehydrogenase
	1llu_F	3	336	334	Gaps:6	95.91	342	40.24	15.85	3e-61	mol:protein length:342 Alcohol Dehydrogenase
	1llu_E	3	336	334	Gaps:6	95.91	342	40.24	15.85	3e-61	mol:protein length:342 Alcohol Dehydrogenase
	1llu_D	3	336	334	Gaps:6	95.91	342	40.24	15.85	3e-61	mol:protein length:342 Alcohol Dehydrogenase
	1llu_C	3	336	334	Gaps:6	95.91	342	40.24	15.85	3e-61	mol:protein length:342 Alcohol Dehydrogenase
rpsblast_cdd	gnl\|CDD\|176257	8	340	333	Gaps:3	97.36	341	53.31	15.06	1e-136	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	10	338	329	Gaps:12	94.69	339	43.30	19.63	8e-88	COG1064 AdhP Zn-dependent alcohol dehydrogenases [General function prediction only].
	gnl\|CDD\|176207	9	336	328	Gaps:9	96.67	330	41.07	17.55	9e-87	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\|176186	9	338	330	Gaps:21	96.44	337	31.38	19.38	5e-65	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\|176256	10	336	327	Gaps:10	95.80	333	36.36	16.61	9e-63	cd08296 CAD_like 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 (ADHs) 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	10	340	331	Gaps:14	96.15	338	38.46	17.85	2e-61	PRK09422 PRK09422 alcohol dehydrogenase Provisional.
	gnl\|CDD\|176187	10	338	329	Gaps:16	96.18	340	34.25	18.96	1e-59	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\|176258	10	328	319	Gaps:19	93.62	329	37.01	14.94	2e-58	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\|176178	34	311	278	Gaps:10	99.63	271	38.52	15.93	1e-53	cd05188 MDR Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family. The medium chain reductase/dehydrogenases (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. ADH-like proteins typically form dimers (typically higher plants mammals) or tetramers (yeast bacteria) and generally 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. 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. Other MDR members have only a catalytic zinc and some contain no coordinated zinc.
	gnl\|CDD\|176220	10	336	327	Gaps:11	95.78	332	32.08	17.30	7e-53	cd08259 Zn_ADH5 Alcohol dehydrogenases of the MDR family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. This group contains proteins that share the characteristic catalytic and structural zinc-binding sites of the zinc-dependent alcohol dehydrogenase family. 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 (His-51) the ribose of NAD a serine (Ser-48) 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	1	338	338	Gaps:17	94.72	360	42.52	17.30	7e-98	KOG0023 KOG0023 KOG0023 Alcohol dehydrogenase class V [Secondary metabolites biosynthesis transport and catabolism].
	gnl\|CDD\|35245	10	338	329	Gaps:41	94.93	375	28.65	12.36	2e-34	KOG0022 KOG0022 KOG0022 Alcohol dehydrogenase class III [Secondary metabolites biosynthesis transport and catabolism].
	gnl\|CDD\|35247	30	317	288	Gaps:18	81.92	354	30.34	17.59	5e-32	KOG0024 KOG0024 KOG0024 Sorbitol dehydrogenase [Secondary metabolites biosynthesis transport and catabolism].
	gnl\|CDD\|36412	9	340	332	Gaps:54	95.10	347	21.52	16.97	9e-27	KOG1198 KOG1198 KOG1198 Zinc-binding oxidoreductase [Energy production and conversion General function prediction only].
	gnl\|CDD\|36411	5	278	274	Gaps:35	72.92	336	35.92	17.55	2e-26	KOG1197 KOG1197 KOG1197 Predicted quinone oxidoreductase [Energy production and conversion General function prediction only].
	gnl\|CDD\|35248	10	320	311	Gaps:49	84.75	354	26.67	18.33	9e-16	KOG0025 KOG0025 KOG0025 Zn2+-binding dehydrogenase (nuclear receptor binding factor-1) [Transcription Energy production and conversion].
	gnl\|CDD\|36410	157	318	162	Gaps:15	49.85	343	22.81	17.54	2e-08	KOG1196 KOG1196 KOG1196 Predicted NAD-dependent oxidoreductase [General function prediction only].

Other analysis

Functional Gbrowse

Ortholog