GRS - Genome Report System

Sclerotinia sclerotiorum GRS

Functional annotation

SS1G_10768.1

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_10768	1	564	564	n/a	97.75	577	90.78	0.00	0.0	hypothetical protein
	bfu:BC1G_03776	58	497	440	Gaps:59	84.93	458	55.53	11.57	1e-102	hypothetical protein
	fgr:FG08067.1	25	340	316	Gaps:31	69.13	447	30.74	18.45	3e-26	hypothetical protein
	fgr:FG09084.1	25	289	265	Gaps:38	45.27	603	32.97	16.85	5e-23	hypothetical protein
	mgr:MGG_09995	24	333	310	Gaps:34	21.52	1431	24.68	22.40	2e-15	MG09995.4 hypothetical protein
	pno:SNOG_08347	189	333	145	Gaps:13	49.03	310	32.24	19.74	2e-14	hypothetical protein
	pan:PODANSg2443	24	269	246	Gaps:17	41.00	622	27.84	16.86	3e-14	hypothetical protein
	ani:AN6382.2	20	279	260	Gaps:30	42.54	630	27.99	19.40	9e-12	hypothetical protein
	nfi:NFIA_048470	153	330	178	Gaps:19	12.53	1492	33.16	12.83	5e-11	hypothetical protein
blastp_uniprot_sprot	no results
blastp_pdb	no results
rpsblast_cdd	gnl\|CDD\|176558	164	562	399	Gaps:121	98.00	300	32.31	17.01	9e-32	cd08621 PI-PLCXDc_like_2 Catalytic domain of uncharacterized hypothetical proteins similar to eukaryotic phosphatidylinositol-specific phospholipase C X domain containing proteins. This subfamily corresponds to the catalytic domain present in a group of uncharacterized hypothetical proteins found in bacteria and fungi which are similar to eukaryotic phosphatidylinositol-specific phospholipase C X domain containing proteins (PI-PLCXD). The typical eukaryotic phosphoinositide-specific phospholipase C (PI-PLC EC 3.1.4.11) has a multidomain organization that consists of a PLC catalytic core domain and various regulatory domains. The catalytic core domain is assembled from two highly conserved X- and Y-regions split by a divergent linker sequence. In contrast eukaryotic PI-PLCXDs contain a single TIM-barrel type catalytic domain X domain and are more closely related to bacterial PI-PLCs which participate in Ca2+-independent PI metabolism hydrolyzing the membrane lipid phosphatidylinositol (PI) to produce phosphorylated myo-inositol and diacylglycerol (DAG). Although the biological function of eukaryotic PI-PLCXDs still remains unclear it may distinct from that of typical eukaryotic PI-PLCs.
	gnl\|CDD\|176529	159	297	139	Gaps:27	49.31	288	30.28	16.90	1e-22	cd08587 PI-PLCXDc_like Catalytic domain of phosphatidylinositol-specific phospholipase C X domain containing and similar proteins. This family corresponds to the catalytic domain present in phosphatidylinositol-specific phospholipase C X domain containing proteins (PI-PLCXD) which are bacterial phosphatidylinositol-specific phospholipase C (PI-PLC EC 4.6.1.13) sequence homologs mainly found in eukaryota. The typical eukaryotic phosphoinositide-specific phospholipase C (PI-PLC EC 3.1.4.11) have a multidomain organization that consists of a PLC catalytic core domain and various regulatory domains. The catalytic core domain is assembled from two highly conserved X- and Y-regions split by a divergent linker sequence. In contrast eukaryotic PI-PLCXDs and their bacterial homologs contain a single TIM-barrel type catalytic domain X domain which is more closely related to that of bacterial PI-PLCs. Although the biological function of eukaryotic PI-PLCXDs still remains unclear it may be distinct from that of typical eukaryotic PI-PLCs.
	gnl\|CDD\|176500	164	297	134	Gaps:16	45.02	271	26.23	25.41	2e-18	cd08557 PI-PLCc_bacteria_like Catalytic domain of bacterial phosphatidylinositol-specific phospholipase C and similar proteins. This subfamily corresponds to the catalytic domain present in bacterial phosphatidylinositol-specific phospholipase C (PI-PLC EC 4.6.1.13) and their sequence homologs found in eukaryota. Bacterial PI-PLCs participate in Ca2+-independent PI metabolism hydrolyzing the membrane lipid phosphatidylinositol (PI) to produce phosphorylated myo-inositol and diacylglycerol (DAG). Although their precise physiological function remains unclear bacterial PI-PLCs may function as virulence factors in some pathogenic bacteria. Bacterial PI-PLCs contain a single TIM-barrel type catalytic domain. Its catalytic mechanism is based on general base and acid catalysis utilizing two well conserved histidines and consists of two steps a phosphotransfer and a phosphodiesterase reaction. Eukaryotic homologs in this family are named as phosphatidylinositol-specific phospholipase C X domain containing proteins (PI-PLCXD). They are distinct from the typical eukaryotic phosphoinositide-specific phospholipases C (PI-PLC EC 3.1.4.11) which have a multidomain organization that consists of a PLC catalytic core domain and various regulatory domains. The catalytic core domain is assembled from two highly conserved X- and Y-regions split by a divergent linker sequence. In contrast eukaryotic PI-PLCXDs contain a single TIM-barrel type catalytic domain X domain which is closely related to that of bacterial PI-PLCs. Although the biological function of eukaryotic PI-PLCXDs still remains unclear it may be distinct from that of typical eukaryotic PI-PLCs. This family also includes a distinctly different type of eukaryotic PLC glycosylphosphatidylinositol-specific phospholipase C (GPI-PLC) an integral membrane protein characterized in the protozoan parasite Trypanosoma brucei. T. brucei GPI-PLC hydrolyzes the GPI-anchor on the variant specific glycoprotein (VSG) releasing dimyristyl glycerol (DMG) which may facilitate the evasion of the protozoan to the host's immune system. It does not require Ca2+ for its activity and is more closely related to bacterial PI-PLCs but not mammalian PI-PLCs.
	gnl\|CDD\|176555	159	297	139	Gaps:36	49.31	290	27.27	17.48	3e-09	cd08616 PI-PLCXD1c Catalytic domain of phosphatidylinositol-specific phospholipase C X domain containing 1. This subfamily corresponds to the catalytic domain present in a group of phosphatidylinositol-specific phospholipase C X domain containing 1 (PI-PLCXD1) 2 (PI-PLCXD2) and 3 (PI-PLCXD3) which are bacterial phosphatidylinositol-specific phospholipase C (PI-PLC EC 4.6.1.13) sequence homologs found in vertebrates. The typical eukaryotic phosphoinositide-specific phospholipase C (PI-PLC EC 3.1.4.11) has a multidomain organization that consists of a PLC catalytic core domain and various regulatory domains. The catalytic core domain is assembled from two highly conserved X- and Y-regions split by a divergent linker sequence. In contrast members in this group contain a single TIM-barrel type catalytic domain X domain and are more closely related to bacterial PI-PLCs which participate in Ca2+-independent PI metabolism hydrolyzing the membrane lipid phosphatidylinositol (PI) to produce phosphorylated myo-inositol and diacylglycerol (DAG). Although the biological function of eukaryotic PI-PLCXDs still remains unclear it may distinct from that of typical eukaryotic PI-PLCs.
	gnl\|CDD\|176557	164	283	120	Gaps:24	37.01	281	31.73	19.23	3e-08	cd08620 PI-PLCXDc_like_1 Catalytic domain of uncharacterized hypothetical proteins similar to eukaryotic phosphatidylinositol-specific phospholipase C X domain containing proteins. This subfamily corresponds to the catalytic domain present in a group of uncharacterized hypothetical proteins found in bacteria and fungi which are similar to eukaryotic phosphatidylinositol-specific phospholipase C X domain containing proteins (PI-PLCXD). The typical eukaryotic phosphoinositide-specific phospholipase C (PI-PLC EC 3.1.4.11) has a multidomain organization that consists of a PLC catalytic core domain and various regulatory domains. The catalytic core domain is assembled from two highly conserved X- and Y-regions split by a divergent linker sequence. In contrast eukaryotic PI-PLCXDs contain a single TIM-barrel type catalytic domain X domain and are more closely related to bacterial PI-PLCs which participate in Ca2+-independent PI metabolism hydrolyzing the membrane lipid phosphatidylinositol (PI) to produce phosphorylated myo-inositol and diacylglycerol (DAG). Although the biological function of eukaryotic PI-PLCXDs still remains unclear it may distinct from that of typical eukaryotic PI-PLCs.
	gnl\|CDD\|176528	164	270	107	Gaps:17	33.69	279	29.79	19.15	4e-08	cd08586 PI-PLCc_BcPLC_like Catalytic domain of Bacillus cereus phosphatidylinositol-specific phospholipases C and similar proteins. This subfamily corresponds to the catalytic domain present in Bacillus cereus phosphatidylinositol-specific phospholipase C (PI-PLC EC 4.6.1.13) and its sequence homologs found in bacteria and eukaryota. Bacterial PI-PLCs participate in Ca2+-independent PI metabolism hydrolyzing the membrane lipid phosphatidylinositol (PI) to produce phosphorylated myo-inositol and diacylglycerol (DAG). Although their precise physiological function remains unclear bacterial PI-PLCs may function as virulence factors in some pathogenic bacteria. Bacterial PI-PLCs contain a single TIM-barrel type catalytic domain. Their catalytic mechanism is based on general base and acid catalysis utilizing two well conserved histidines and consists of two steps a phosphotransfer and a phosphodiesterase reaction. This family also includes some uncharacterized eukaryotic homologs which contains a single TIM-barrel type catalytic domain X domain. They are similar to bacterial PI-PLCs and distinct from typical eukaryotic PI-PLCs which have a multidomain organization that consists of a PLC catalytic core domain and various regulatory domains and strictly require Ca2+ for their catalytic activities. The prototype of this family is Bacillus cereus PI-PLC which has a moderate thermal stability and is active as a monomer.
	gnl\|CDD\|176556	152	267	116	Gaps:16	36.49	285	30.77	15.38	6e-08	cd08619 PI-PLCXDc_plant Catalytic domain of phosphatidylinositol-specific phospholipase C X domain containing proteins found in plants. The CD corresponds to the catalytic domain present in uncharacterized plant phosphatidylinositol-specific phospholipase C X domain containing proteins (PI-PLCXD). The typical eukaryotic phosphoinositide-specific phospholipase C (PI-PLC EC 3.1.4.11) has a multidomain organization that consists of a PLC catalytic core domain and various regulatory domains. The catalytic core domain is assembled from two highly conserved X- and Y-regions split by a divergent linker sequence. In contrast plant PI-PLCXDs contain a single TIM-barrel type catalytic domain X domain and are more closely related to bacterial PI-PLCs which participate in Ca2+-independent PI metabolism hydrolyzing the membrane lipid phosphatidylinositol (PI) to produce phosphorylated myo-inositol and diacylglycerol (DAG). Although the biological function of plant PI-PLCXDs still remains unclear it may distinct from that of typical eukaryotic PI-PLCs.
	gnl\|CDD\|176559	166	268	103	Gaps:12	35.14	276	25.77	20.62	4e-07	cd08622 PI-PLCXDc_CG14945_like Catalytic domain of Drosophila melanogaster CG14945-like proteins similar to phosphatidylinositol-specific phospholipase C X domain containing. This subfamily corresponds to the catalytic domain present in uncharacterized metazoan Drosophila melanogaster CG14945-like proteins which are similar to eukaryotic phosphatidylinositol-specific phospholipase C X domain containing proteins (PI-PLCXD). The typical eukaryotic phosphoinositide-specific phospholipase C (PI-PLC EC 3.1.4.11) has a multidomain organization that consists of a PLC catalytic core domain and various regulatory domains. The catalytic core domain is assembled from two highly conserved X- and Y-regions split by a divergent linker sequence. In contrast eukaryotic PI-PLCXDs contain a single TIM-barrel type catalytic domain X domain and are more closely related to bacterial PI-PLCs which participate in Ca2+-independent PI metabolism hydrolyzing the membrane lipid phosphatidylinositol (PI) to produce phosphorylated myo-inositol and diacylglycerol (DAG). Although the biological function of eukaryotic PI-PLCXDs still remains unclear it may distinct from that of typical eukaryotic PI-PLCs.
rpsblast_kog	gnl\|CDD\|39507	137	269	133	Gaps:17	42.48	306	26.92	19.23	1e-07	KOG4306 KOG4306 KOG4306 Glycosylphosphatidylinositol-specific phospholipase C [Signal transduction mechanisms].

Other analysis

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Ortholog