GRS - Genome Report System

Botrytis cinerea B0510 GRS

Functional annotation

BC1G_00059.1

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	bfu:BC1G_00059	1	229	229	n/a	100.00	229	100.00	0.00	1e-130	hypothetical protein
	ssl:SS1G_04704	1	228	228	n/a	99.56	229	96.49	1.32	1e-126	mitochondrial peroxiredoxin PRX1
	pno:SNOG_00787	4	227	224	n/a	98.25	228	92.86	2.68	1e-119	hypothetical protein
	tml:GSTUM_00008955001	1	228	228	Gaps:1	100.00	229	86.03	5.68	1e-112	hypothetical protein
	fgr:FG07536.1	6	224	219	n/a	96.90	226	84.93	5.48	1e-107	hypothetical protein
	mgr:MGG_08256	1	223	223	Gaps:1	100.00	224	82.14	8.04	1e-106	MG08256.4 hypothetical protein
	pan:PODANSg2348	1	222	222	n/a	99.11	224	78.83	9.46	1e-103	hypothetical protein
	ncr:NCU06031	2	223	222	n/a	98.67	225	78.38	10.81	1e-103	mitochondrial peroxiredoxin PRX1
	pgu:PGUG_05748	7	220	214	n/a	95.54	224	81.78	8.88	1e-102	hypothetical protein
	dha:DEHA2F09680g	1	220	220	n/a	97.35	226	78.64	9.55	1e-101	DEHA2F09680p
blastp_uniprot_sprot	sp\|P34227\|PRX1_YEAST	9	218	210	Gaps:2	80.46	261	60.00	15.71	2e-70	Mitochondrial peroxiredoxin PRX1 OS Saccharomyces cerevisiae GN PRX1 PE 1 SV 1
	sp\|O35244\|PRDX6_RAT	6	221	216	Gaps:13	99.55	224	52.47	12.56	7e-56	Peroxiredoxin-6 OS Rattus norvegicus GN Prdx6 PE 1 SV 3
	sp\|P30041\|PRDX6_HUMAN	6	221	216	Gaps:13	99.55	224	52.02	12.56	1e-55	Peroxiredoxin-6 OS Homo sapiens GN PRDX6 PE 1 SV 3
	sp\|Q5ZJF4\|PRDX6_CHICK	9	222	214	Gaps:13	98.66	224	51.13	14.93	3e-55	Peroxiredoxin-6 OS Gallus gallus GN PRDX6 PE 2 SV 3
	sp\|O77834\|PRDX6_BOVIN	6	221	216	Gaps:13	99.55	224	51.57	12.56	3e-55	Peroxiredoxin-6 OS Bos taurus GN PRDX6 PE 1 SV 3
	sp\|Q5R7E0\|PRDX6_PONAB	6	221	216	Gaps:13	99.55	224	51.57	13.00	4e-55	Peroxiredoxin-6 OS Pongo abelii GN PRDX6 PE 2 SV 3
	sp\|Q9TSX9\|PRDX6_PIG	6	221	216	Gaps:13	99.55	224	51.12	13.00	5e-55	Peroxiredoxin-6 OS Sus scrofa GN PRDX6 PE 2 SV 3
	sp\|Q54SE2\|PRDXL_DICDI	9	223	215	Gaps:8	86.72	241	47.85	22.49	7e-55	Peroxiredoxin-like protein DDB_G0282517 mitochondrial OS Dictyostelium discoideum GN DDB_G0282517 PE 3 SV 1
	sp\|Q2PFL9\|PRDX6_MACFA	6	221	216	Gaps:13	99.55	224	52.02	11.21	2e-54	Peroxiredoxin-6 OS Macaca fascicularis GN PRDX6 PE 2 SV 3
	sp\|O08709\|PRDX6_MOUSE	6	221	216	Gaps:13	99.55	224	51.12	10.76	4e-53	Peroxiredoxin-6 OS Mus musculus GN Prdx6 PE 1 SV 3
blastp_pdb	1prx_B	6	221	216	Gaps:13	99.55	224	51.57	13.00	2e-56	mol:protein length:224 HORF6
	1prx_A	6	221	216	Gaps:13	99.55	224	51.57	13.00	2e-56	mol:protein length:224 HORF6
	2v41_H	9	222	214	Gaps:10	93.56	233	48.62	18.81	4e-55	mol:protein length:233 PEROXIREDOXIN 6.
	2v41_G	9	222	214	Gaps:10	93.56	233	48.62	18.81	4e-55	mol:protein length:233 PEROXIREDOXIN 6.
	2v41_F	9	222	214	Gaps:10	93.56	233	48.62	18.81	4e-55	mol:protein length:233 PEROXIREDOXIN 6.
	2v41_E	9	222	214	Gaps:10	93.56	233	48.62	18.81	4e-55	mol:protein length:233 PEROXIREDOXIN 6.
	2v41_D	9	222	214	Gaps:10	93.56	233	48.62	18.81	4e-55	mol:protein length:233 PEROXIREDOXIN 6.
	2v41_C	9	222	214	Gaps:10	93.56	233	48.62	18.81	4e-55	mol:protein length:233 PEROXIREDOXIN 6.
	2v41_B	9	222	214	Gaps:10	93.56	233	48.62	18.81	4e-55	mol:protein length:233 PEROXIREDOXIN 6.
	2v41_A	9	222	214	Gaps:10	93.56	233	48.62	18.81	4e-55	mol:protein length:233 PEROXIREDOXIN 6.
rpsblast_cdd	gnl\|CDD\|48565	11	219	209	Gaps:8	100.00	203	62.56	13.30	2e-85	cd03016 PRX_1cys Peroxiredoxin (PRX) family 1-cys PRX subfamily composed of PRXs containing only one conserved cysteine which serves as the peroxidatic cysteine. They are homodimeric thiol-specific antioxidant (TSA) proteins that confer a protective role in cells by reducing and detoxifying hydrogen peroxide peroxynitrite and organic hydroperoxides. As with all other PRXs a cysteine sulfenic acid intermediate is formed upon reaction of 1-cys PRX with its substrates. Having no resolving cysteine the oxidized enzyme is resolved by an external small-molecule or protein reductant such as thioredoxin or glutaredoxin. Similar to typical 2-cys PRX 1-cys PRX forms a functional dimeric unit with a B-type interface as well as a decameric structure which is stabilized in the reduced form of the enzyme. Other oligomeric forms tetramers and hexamers have also been reported. Mammalian 1-cys PRX is localized cellularly in the cytosol and is expressed at high levels in brain eye testes and lung. The seed-specific plant 1-cys PRXs protect tissues from reactive oxygen species during desiccation and are also called rehydrins..
	gnl\|CDD\|171890	9	202	194	Gaps:12	88.37	215	46.32	13.16	6e-54	PRK13189 PRK13189 peroxiredoxin Provisional.
	gnl\|CDD\|30799	8	203	196	Gaps:16	98.97	194	43.23	13.54	2e-51	COG0450 AhpC Peroxiredoxin [Posttranslational modification protein turnover chaperones].
	gnl\|CDD\|106159	8	217	210	Gaps:10	99.01	202	45.00	20.50	1e-49	PRK13190 PRK13190 putative peroxiredoxin Provisional.
	gnl\|CDD\|171891	1	214	214	Gaps:19	94.42	215	42.36	15.27	1e-37	PRK13191 PRK13191 putative peroxiredoxin Provisional.
	gnl\|CDD\|48564	11	187	177	Gaps:16	100.00	173	38.73	17.92	3e-34	cd03015 PRX_Typ2cys Peroxiredoxin (PRX) family Typical 2-Cys PRX subfamily PRXs are thiol-specific antioxidant (TSA) proteins which confer a protective role in cells through its peroxidase activity by reducing hydrogen peroxide peroxynitrite and organic hydroperoxides. The functional unit of typical 2-cys PRX is a homodimer. A unique intermolecular redox-active disulfide center is utilized for its activity. Upon reaction with peroxides its peroxidatic cysteine is oxidized into a sulfenic acid intermediate which is resolved by bonding with the resolving cysteine from the other subunit of the homodimer. This intermolecular disulfide bond is then reduced by thioredoxin tryparedoxin or AhpF. Typical 2-cys PRXs like 1-cys PRXs form decamers which are stabilized by reduction of the active site cysteine. Typical 2-cys PRX interacts through beta strands at one edge of the monomer (B-type interface) to form the functional homodimer and uses an A-type interface (similar to the dimeric interface in atypical 2-cys PRX and PRX5) at the opposite end of the monomer to form the stable decameric (pentamer of dimers) structure..
	gnl\|CDD\|48520	15	164	150	Gaps:13	99.29	140	42.45	15.11	1e-33	cd02971 PRX_family Peroxiredoxin (PRX) family composed of the different classes of PRXs including many proteins originally known as bacterioferritin comigratory proteins (BCP) based on their electrophoretic mobility before their function was identified. PRXs are thiol-specific antioxidant (TSA) proteins also known as TRX peroxidases and alkyl hydroperoxide reductase C22 (AhpC) proteins. They confer a protective antioxidant role in cells through their peroxidase activity in which hydrogen peroxide peroxynitrate and organic hydroperoxides are reduced and detoxified using reducing equivalents derived from either TRX glutathione trypanothione and AhpF. They are distinct from other peroxidases in that they have no cofactors such as metals or prosthetic groups. The first step of catalysis common to all PRXs is the nucleophilic attack by the catalytic cysteine (also known as the peroxidatic cysteine) on the peroxide leading to cleavage of the oxygen-oxygen bond and the formation of a cysteine sulfenic acid intermediate. The second step of the reaction the resolution of the intermediate distinguishes the different types of PRXs. The presence or absence of a second cysteine (the resolving cysteine) classifies PRXs as either belonging to the 2-cys or 1-cys type. The resolving cysteine of 2-cys PRXs is either on the same chain (atypical) or on the second chain (typical) of a functional homodimer. Structural and motif analysis of this growing family supports the need for a new classification system. The peroxidase activity of PRXs is regulated in vivo by irreversible cysteine over-oxidation into a sulfinic acid phosphorylation and limited proteolysis..
	gnl\|CDD\|106544	11	201	191	Gaps:12	86.98	215	40.64	14.97	2e-31	PRK13599 PRK13599 putative peroxiredoxin Provisional.
	gnl\|CDD\|144244	11	149	139	Gaps:17	100.00	124	41.13	22.58	2e-29	pfam00578 AhpC-TSA AhpC/TSA family. This family contains proteins related to alkyl hydroperoxide reductase (AhpC) and thiol specific antioxidant (TSA).
	gnl\|CDD\|31418	7	171	165	Gaps:12	98.73	157	34.19	20.00	3e-22	COG1225 Bcp Peroxiredoxin [Posttranslational modification protein turnover chaperones].
rpsblast_kog	gnl\|CDD\|36072	9	221	213	Gaps:12	97.77	224	53.42	14.61	4e-71	KOG0854 KOG0854 KOG0854 Alkyl hydroperoxide reductase thiol specific antioxidant and related enzymes [Posttranslational modification protein turnover chaperones].
	gnl\|CDD\|36070	36	200	165	Gaps:11	79.59	196	37.82	17.95	3e-24	KOG0852 KOG0852 KOG0852 Alkyl hydroperoxide reductase thiol specific antioxidant and related enzymes [Posttranslational modification protein turnover chaperones].
	gnl\|CDD\|36073	9	110	102	Gaps:7	45.97	211	29.90	17.53	4e-07	KOG0855 KOG0855 KOG0855 Alkyl hydroperoxide reductase thiol specific antioxidant and related enzymes [Posttranslational modification protein turnover chaperones].

Other analysis

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