GRS - Genome Report System

Sclerotinia sclerotiorum GRS

Functional annotation

SS1G_11189.1

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_11189	1	423	423	n/a	100.00	423	96.69	0.00	0.0	hypothetical protein
	bfu:BC1G_08658	1	423	423	Gaps:1	100.00	424	82.08	4.95	0.0	hypothetical protein
	mgr:MGG_09716	3	422	420	Gaps:13	96.93	424	60.58	13.63	1e-142	MG09716.4 hypothetical protein
	ncr:NCU07536	3	422	420	Gaps:8	98.35	423	58.41	14.90	1e-140	similar to carboxypeptidase
	pan:PODANSg4554	25	422	398	Gaps:6	92.71	425	60.41	14.47	1e-135	hypothetical protein
	pno:SNOG_09739	7	422	416	Gaps:11	97.60	417	55.53	15.48	1e-120	hypothetical protein
	cim:CIMG_07026	1	422	422	Gaps:10	100.00	420	47.38	17.14	1e-108	hypothetical protein
	pno:SNOG_07428	1	419	419	Gaps:19	99.28	415	47.57	21.60	1e-108	hypothetical protein
	ure:UREG_01322	1	422	422	Gaps:13	100.00	417	46.28	20.14	1e-106	hypothetical protein
	pan:PODANSg2278	19	422	404	Gaps:20	94.37	426	48.51	16.17	1e-106	hypothetical protein
blastp_uniprot_sprot	sp\|C5FH26\|MCPAL_NANOT	3	422	420	Gaps:16	99.04	416	48.79	17.48	1e-113	Metallocarboxypeptidase A-like protein MCYG_01475 OS Nannizzia otae (strain CBS 113480) GN MCYG_01475 PE 3 SV 1
	sp\|C5FVN6\|MCPA_NANOT	3	419	417	Gaps:7	98.58	422	45.91	18.99	1e-111	Metallocarboxypeptidase A OS Nannizzia otae (strain CBS 113480) GN MCPA PE 3 SV 1
	sp\|B6V865\|MCPA_TRITO	24	419	396	Gaps:5	93.13	422	46.56	19.08	1e-109	Metallocarboxypeptidase A OS Trichophyton tonsurans GN MCPA PE 3 SV 1
	sp\|A6XGK3\|MCPA_TRIRU	24	419	396	Gaps:5	93.13	422	46.82	18.58	1e-109	Metallocarboxypeptidase A OS Trichophyton rubrum GN MCPA PE 1 SV 1
	sp\|B8XGR3\|MCPA_TRIEQ	24	419	396	Gaps:5	93.13	422	46.56	19.08	1e-109	Metallocarboxypeptidase A OS Trichophyton equinum GN MCPA PE 3 SV 1
	sp\|Q9UI42\|CBPA4_HUMAN	12	419	408	Gaps:18	96.44	421	35.96	19.21	2e-61	Carboxypeptidase A4 OS Homo sapiens GN CPA4 PE 1 SV 2
	sp\|P00730\|CBPA1_BOVIN	9	419	411	Gaps:20	97.14	419	36.12	16.95	3e-59	Carboxypeptidase A1 OS Bos taurus GN CPA1 PE 1 SV 3
	sp\|P00731\|CBPA1_RAT	17	419	403	Gaps:18	95.23	419	34.59	19.30	5e-58	Carboxypeptidase A1 OS Rattus norvegicus GN Cpa1 PE 2 SV 2
	sp\|P48052\|CBPA2_HUMAN	27	419	393	Gaps:23	92.60	419	35.57	19.07	1e-57	Carboxypeptidase A2 OS Homo sapiens GN CPA2 PE 1 SV 3
	sp\|Q6P8K8\|CBPA4_MOUSE	12	419	408	Gaps:19	96.43	420	33.58	18.27	1e-56	Carboxypeptidase A4 OS Mus musculus GN Cpa4 PE 2 SV 2
blastp_pdb	2boa_B	27	419	393	Gaps:18	96.78	404	36.83	18.41	9e-61	mol:protein length:404 CARBOXYPEPTIDASE A4
	2boa_A	27	419	393	Gaps:18	96.78	404	36.83	18.41	9e-61	mol:protein length:404 CARBOXYPEPTIDASE A4
	1aye_A	27	419	393	Gaps:23	96.76	401	35.57	19.07	3e-58	mol:protein length:401 PROCARBOXYPEPTIDASE A2
	1dtd_A	118	419	302	Gaps:9	96.70	303	38.91	18.43	6e-57	mol:protein length:303 CARBOXYPEPTIDASE A2
	1pca_A	21	419	399	Gaps:37	98.26	403	36.11	16.67	1e-55	mol:protein length:403 PROCARBOXYPEPTIDASE A PCPA
	2pcu_A	118	419	302	Gaps:10	96.39	305	40.14	18.37	2e-55	mol:protein length:305 Carboxypeptidase A4
	2bo9_C	118	419	302	Gaps:10	95.45	308	40.14	18.37	3e-55	mol:protein length:308 CARBOXYPEPTIDASE A4
	2bo9_A	118	419	302	Gaps:10	95.45	308	40.14	18.37	3e-55	mol:protein length:308 CARBOXYPEPTIDASE A4
	1cps_A	112	419	308	Gaps:9	97.39	307	40.13	15.72	8e-54	mol:protein length:307 CARBOXYPEPTIDASE A
	1cbx_A	112	419	308	Gaps:9	97.39	307	40.13	15.72	8e-54	mol:protein length:307 CARBOXYPEPTIDASE A
rpsblast_cdd	gnl\|CDD\|133106	118	422	305	Gaps:3	100.00	304	56.91	17.11	1e-136	cd06248 M14_CPA_CPB_like Peptidase M14 Carboxypeptidase A/B-like subfamily: This is one of two main M14 carboxypeptidase subfamilies defined by sequence and structural homology the other being N/E. Carboxypeptidases (CPs) hydrolyze single C-terminal amino acids from polypeptide chains. They have a recognition site for the free C-terminal carboxyl group which is a key determinant of specificity. Majority of the proteins in this subfamily have not been characterized as yet. The A/B enzymes are normally synthesized as inactive precursors containing preceding signal peptide followed by a globular N-terminal pro-region linked to the enzyme the proenzymes are called procarboxypeptidases. These enzymes exhibit distinct substrate specificity pattern Carboxypeptidase A-like (CPA-like) enzymes favor hydrophobic residues while carboxypeptidase B-like (CPB-like) enzymes only cleave the basic residues lysine or arginine. There are nine members in the A/B family: CPA1 CPA2 CPA3 CPA4 CPA5 CPA6 CPB CPO and CPU. CPA1 CPA2 and CPB are produced by the pancreas. The A forms have slightly different specificities with CPA1 preferring aliphatic and small aromatic residues and CPA2 preferring the bulkier aromatic side chains. CPA3 is found in secretory granules of mast cells and functions in inflammatory processes. CPA4 detected in hormone-regulated tissues is thought to play a role in prostate cancer. CPA5 is present in discrete regions of pituitary and other tissues and cleaves aliphatic C-terminal residues. CPA6 is highly expressed in embryonic brain and optic muscle suggesting that it may play a specific role in cell migration and axonal guidance. CPU (also called CPB2) is produced and secreted by the liver as the inactive precursor PCPU commonly referred to as thrombin-activatable fibrinolysis inhibitor (TAFI). Little is known about CPO but it has been suggested to have specificity for acidic residues.
	gnl\|CDD\|133072	121	419	299	Gaps:8	98.98	294	42.27	19.24	5e-93	cd03860 M14_CP_A-B_like The Peptidase M14 Carboxypeptidase (CP) A/B subfamily is one of two main M14 CP subfamilies defined by sequence and structural homology the other being the N/E subfamily. CPs hydrolyze single C-terminal amino acids from polypeptide chains. They have a recognition site for the free C-terminal carboxyl group which is a key determinant of specificity. Enzymes belonging to the A/B subfamily are normally synthesized as inactive precursors containing preceding signal peptide followed by a globular N-terminal pro-region linked to the enzyme these proenzymes are called procarboxypeptidases. The A/B enzymes can be further divided based on their substrate specificity Carboxypeptidase A-like (CPA-like) enzymes favor hydrophobic residues while carboxypeptidase B-like (CPB-like) enzymes only cleave the basic residues lysine or arginine. There are nine members in the A/B family: CPA1 CPA2 CPA3 CPA4 CPA5 CPA6 CPB CPO and CPU. CPA1 CPA2 and CPB are produced by the pancreas. The A forms have slightly different specificities with CPA1 preferring aliphatic and small aromatic residues and CPA2 preferring the bulkier aromatic side chains. CPA3 is found in secretory granules of mast cells and functions in inflammatory processes. CPA4 is detected in hormone-regulated tissues and is thought to play a role in prostate cancer. CPA5 is present in discrete regions of pituitary and other tissues and cleaves aliphatic C-terminal residues. CPA6 is highly expressed in embryonic brain and optic muscle suggesting that it may play a specific role in cell migration and axonal guidance. CPU (also called CPB2) is produced and secreted by the liver as the inactive precursor PCPU commonly referred to as thrombin-activatable fibrinolysis inhibitor (TAFI). Little is known about CPO but it has been suggested to have specificity for acidic residues.
	gnl\|CDD\|128879	121	408	288	Gaps:11	100.00	277	42.96	16.25	2e-82	smart00631 Zn_pept Zn_pept.
	gnl\|CDD\|143996	127	414	288	Gaps:16	100.00	276	42.39	17.39	2e-72	pfam00246 Peptidase_M14 Zinc carboxypeptidase.
	gnl\|CDD\|133081	118	419	302	Gaps:9	97.34	301	40.27	18.77	1e-68	cd03870 M14_CPA Peptidase M14 Carboxypeptidase (CP) A (CPA) belongs to the A/B subfamily of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding CPs which hydrolyze single C-terminal amino acids from polypeptide chains and have a recognition site for the free C-terminal carboxyl group which is a key determinant of specificity. CPA enzymes generally favor hydrophobic residues. A/B subfamily enzymes are normally synthesized as inactive precursors containing preceding signal peptide followed by a globular N-terminal pro-region linked to the enzyme these proenzymes are called procarboxypeptidases. The procarboxypeptidase A (PCPA) is produced by the exocrine pancreas and stored as a stable zymogen in the pancreatic granules until secretion into the digestive tract occurs. This subfamily includes CPA1 CPA2 and CPA4 forms. Within these A forms there are slightly different specificities with CPA1 preferring aliphatic and small aromatic residues and CPA2 preferring the bulkier aromatic side chains. CPA4 detected in hormone-regulated tissues is thought to play a role in prostate cancer.
	gnl\|CDD\|133082	118	416	299	Gaps:8	97.00	300	37.11	18.90	6e-59	cd03871 M14_CPB Peptidase M14 Carboxypeptidase B (CPB) belongs to the carboxypeptidase A/B subfamily of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding CPs which hydrolyze single C-terminal amino acids from polypeptide chains and have a recognition site for the free C-terminal carboxyl group which is a key determinant of specificity. Carboxypeptidase B (CPB) enzymes only cleave the basic residues lysine or arginine. A/B subfamily enzymes are normally synthesized as inactive precursors containing preceding signal peptide followed by a globular N-terminal pro-region linked to the enzyme these proenzymes are called procarboxypeptidases. The procarboxypeptidase B (PCPB) is produced by the exocrine pancreas and stored as stable zymogen in the pancreatic granules until secretion into the digestive tract occurs. PCPB has been reported to be a good serum marker for the diagnosis of acute pancreatitis and graft rejection in pancreas transplant recipients.
	gnl\|CDD\|133105	118	419	302	Gaps:13	98.99	298	33.56	22.37	5e-51	cd06247 M14_CPO Peptidase M14 carboxypeptidase (CP) O (CPO also known as metallocarboxypeptidase C EC 3.4.17.) belongs to the carboxypeptidase A/B subfamily of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding CPs which hydrolyze single C-terminal amino acids from polypeptide chains and have a recognition site for the free C-terminal carboxyl group which is a key determinant of specificity. CPO has not been well characterized as yet and little is known about it. Based on modeling studies CPO has been suggested to have specificity for acidic residues rather than aliphatic/aromatic residues as in A-like enzymes or basic residues as in B-like enzymes. It remains to be demonstrated that CPO is functional as an MCP.
	gnl\|CDD\|133104	117	416	300	Gaps:7	97.67	300	33.79	19.11	2e-50	cd06246 M14_CPB2 Peptidase M14 Carboxypeptidase (CP) B2 (CPB2 also known as plasma carboxypeptidase B carboxypeptidase U and CPU) belongs to the carboxpeptidase A/B subfamily of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding CPs which hydrolyze single C-terminal amino acids from polypeptide chains and have a recognition site for the free C-terminal carboxyl group which is a key determinant of specificity. CPB2 enzyme displays B-like activity it only cleaves the basic residues lysine or arginine. It is produced and secreted by the liver as the inactive precursor procarboxypeptidase U or PCPB2 commonly referred to as thrombin-activatable fibrinolysis inhibitor (TAFI). It circulates in plasma as a zymogen bound to plasminogen and the active enzyme TAFIa inhibits fibrinolysis. It is highly regulated increased TAFI concentrations are thought to increase the risk of thrombosis and coronary artery disease by reducing fibrinolytic activity while low TAFI levels have been correlated with chronic liver disease.
	gnl\|CDD\|133083	121	418	298	Gaps:7	97.00	300	32.65	20.27	5e-46	cd03872 M14_CPA6 Carboxypeptidase (CP) A6 (CPA6 also known as CPAH EC 3.4.17.1) belongs to the carboxypeptidase A/B subfamily of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding CPs which hydrolyze single C-terminal amino acids from polypeptide chains and have a recognition site for the free C-terminal carboxyl group which is a key determinant of specificity. CPA6 prefers large hydrophobic C-terminal amino acids as well as histidine while peptides with a penultimate glycine or proline are very poorly cleaved. Several neuropeptides are processed by CPA6 including Met- and Leu-enkephalin angiotensin I and neurotensin. CPA6 converts enkephalin and neurotensin into forms known to be inactive toward their receptors but converts inactive angiotensin I into the biologically active angiotensin II. Thus CPA6 plays a possible role in the regulation of neuropeptides in the extracellular environment within the olfactory bulb where it is highly expressed. It is also broadly expressed in embryonic tissue being found in neuronal tissues bone skin as well as the lateral rectus eye muscle. A disruption in the CPA6 gene is linked to Duane syndrome a defect in the abducens nerve/lateral rectus muscle connection.
	gnl\|CDD\|133071	118	415	298	Gaps:19	100.00	295	33.22	17.97	2e-45	cd03859 M14_CPT Peptidase M14-like domain of carboxypeptidase (CP) T (CPT) CPT belongs to the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding CPs which hydrolyze single C-terminal amino acids from polypeptide chains and have a recognition site for the free C-terminal carboxyl group which is a key determinant of specificity. CPT has moderate similarity to CPA and CPB and exhibits dual-substrate specificity by cleaving C-terminal hydrophobic amino acid residues like CPA and C-terminal positively charged residues like CPB. CPA and CPB are M14 family peptidases but do not belong to this CPT group. The substrate specificity difference between CPT and CPA and CPB is ascribed to a few amino acid substitutions at the substrate-binding pocket while the spatial organization of the binding site remains the same as in all Zn-CPs. CPT has increased thermal stability in presence of Ca2+ ions and two disulfide bridges which give an additional stabilization factor.
rpsblast_kog	gnl\|CDD\|37861	1	419	419	Gaps:12	99.28	418	36.14	20.00	1e-100	KOG2650 KOG2650 KOG2650 Zinc carboxypeptidase [Function unknown].
rpsblast_kog	gnl\|CDD\|37860	113	292	180	Gaps:13	35.80	500	25.14	15.64	2e-10	KOG2649 KOG2649 KOG2649 Zinc carboxypeptidase [General function prediction only].

Other analysis

Functional Gbrowse

Ortholog