GRS - Genome Report System

Botrytis cinerea B0510 GRS

Functional annotation

BC1G_08158.1

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_08158	1	1456	1456	n/a	100.00	1456	94.51	0.00	0.0	hypothetical protein K02320 DNA polymerase alpha subunit A [EC:2.7.7.7]
	ssl:SS1G_08778	1	1456	1456	Gaps:2	100.00	1458	87.65	3.50	0.0	hypothetical protein K02320 DNA polymerase alpha subunit A [EC:2.7.7.7]
	fgr:FG05421.1	6	1456	1451	Gaps:33	97.19	1494	64.33	13.22	0.0	hypothetical protein K02320 DNA polymerase alpha subunit A [EC:2.7.7.7]
	pan:PODANSg5499	1	1455	1455	Gaps:56	99.93	1472	63.43	12.85	0.0	hypothetical protein K02320 DNA polymerase alpha subunit A [EC:2.7.7.7]
	ncr:NCU07870	1	1453	1453	Gaps:37	99.80	1479	63.89	12.74	0.0	similar to DNA polymerase alpha catalytic subunit K02320 DNA polymerase alpha subunit A [EC:2.7.7.7]
	mgr:MGG_06397	1	1456	1456	Gaps:71	99.93	1482	62.26	13.50	0.0	MG06397.4 hypothetical protein K02320 DNA polymerase alpha subunit A [EC:2.7.7.7]
	act:ACLA_069720	5	1448	1444	Gaps:33	99.59	1461	62.41	13.47	0.0	DNA polymerase alpha catalytic subunit putative K02320 DNA polymerase alpha subunit A [EC:2.7.7.7]
	nfi:NFIA_086070	5	1448	1444	Gaps:34	99.59	1462	62.36	13.46	0.0	DNA polymerase alpha catalytic subunit putative K02320 DNA polymerase alpha subunit A [EC:2.7.7.7]
	afm:AFUA_2G10730	5	1448	1444	Gaps:34	99.59	1462	62.23	13.46	0.0	DNA polymerase alpha catalytic subunit K02320 DNA polymerase alpha subunit A [EC:2.7.7.7]
	ang:An02g02510	5	1448	1444	Gaps:34	99.59	1464	62.41	13.17	0.0	hypothetical protein K02320 DNA polymerase alpha subunit A [EC:2.7.7.7]
blastp_uniprot_sprot	sp\|P28040\|DPOA_SCHPO	10	1449	1440	Gaps:90	99.07	1405	44.61	17.96	0.0	DNA polymerase alpha catalytic subunit OS Schizosaccharomyces pombe GN pol1 PE 1 SV 1
	sp\|P13382\|DPOA_YEAST	344	1448	1105	Gaps:83	76.02	1468	46.68	15.32	0.0	DNA polymerase alpha catalytic subunit A OS Saccharomyces cerevisiae GN POL1 PE 1 SV 2
	sp\|P09884\|DPOLA_HUMAN	308	1449	1142	Gaps:58	78.93	1462	36.92	20.54	0.0	DNA polymerase alpha catalytic subunit OS Homo sapiens GN POLA1 PE 1 SV 2
	sp\|Q9DE46\|DPOLA_XENLA	345	1451	1107	Gaps:62	76.75	1458	38.61	19.75	0.0	DNA polymerase alpha catalytic subunit OS Xenopus laevis GN pola1 PE 2 SV 1
	sp\|O89042\|DPOLA_RAT	343	1438	1096	Gaps:61	76.43	1451	38.50	20.11	0.0	DNA polymerase alpha catalytic subunit (Fragment) OS Rattus norvegicus GN Pola1 PE 2 SV 1
	sp\|P33609\|DPOLA_MOUSE	308	1449	1142	Gaps:69	78.57	1465	38.05	20.16	0.0	DNA polymerase alpha catalytic subunit OS Mus musculus GN Pola1 PE 1 SV 2
	sp\|Q9FHA3\|DPOLA_ARATH	310	1444	1135	Gaps:123	78.95	1492	35.91	16.72	1e-176	DNA polymerase alpha catalytic subunit OS Arabidopsis thaliana GN POLA PE 3 SV 1
	sp\|Q94636\|DPOLA_OXYNO	306	1449	1144	Gaps:106	79.76	1492	33.28	19.41	1e-170	DNA polymerase alpha catalytic subunit OS Oxytricha nova PE 3 SV 1
	sp\|O48653\|DPOLA_ORYSJ	2	1447	1446	Gaps:129	81.94	1534	35.88	15.43	1e-166	DNA polymerase alpha catalytic subunit OS Oryza sativa subsp. japonica GN Os01g0868300 PE 2 SV 2
	sp\|Q27152\|DPOLA_OXYTR	342	1399	1058	Gaps:82	73.10	1513	33.82	19.71	1e-162	DNA polymerase alpha catalytic subunit OS Oxytricha trifallax PE 3 SV 1
blastp_pdb	1tgo_A	606	1223	618	Gaps:74	74.51	773	31.60	19.79	3e-47	mol:protein length:773 PROTEIN (THERMOSTABLE B DNA POLYMERASE)
	2vwj_A	606	1223	618	Gaps:74	74.51	773	31.60	19.62	8e-47	mol:protein length:773 DNA POLYMERASE
	2vwk_A	606	1223	618	Gaps:74	74.51	773	31.60	19.62	8e-47	mol:protein length:773 DNA POLYMERASE
	2xhb_A	606	1223	618	Gaps:74	74.51	773	31.42	19.79	2e-46	mol:protein length:773 DNA POLYMERASE
	1qht_A	608	1223	616	Gaps:68	73.81	775	30.94	19.93	3e-45	mol:protein length:775 PROTEIN (DNA POLYMERASE)
	3iay_A	494	1228	735	Gaps:89	77.48	919	26.83	19.80	3e-43	mol:protein length:919 DNA polymerase delta catalytic subunit
	3a2f_A	606	1223	618	Gaps:75	74.45	775	31.20	19.76	4e-43	mol:protein length:775 DNA polymerase
	2jgu_A	606	1223	618	Gaps:75	74.45	775	31.37	19.24	1e-42	mol:protein length:775 DNA POLYMERASE
	1qqc_A	606	1223	618	Gaps:78	74.51	773	31.94	19.27	3e-39	mol:protein length:773 DNA POLYMERASE II
	1wns_A	615	1223	609	Gaps:74	73.00	774	31.33	19.65	3e-39	mol:protein length:774 DNA POLYMERASE
rpsblast_cdd	gnl\|CDD\|161943	29	1223	1195	Gaps:80	99.91	1172	34.93	18.02	0.0	TIGR00592 pol2 DNA polymerase (pol2). This family is based on the phylogenomic analysis of JA Eisen (1999 Ph.D. Thesis Stanford University).
	gnl\|CDD\|99915	841	1241	401	Gaps:5	99.50	400	55.78	18.84	0.0	cd05532 POLBc_alpha DNA polymerase type-B alpha subfamily catalytic domain. Three DNA-dependent DNA polymerases type B (alpha delta and epsilon) have been identified as essential for nuclear DNA replication in eukaryotes. DNA polymerase (Pol) alpha is almost exclusively required for the initiation of DNA replication and the priming of Okazaki fragments during elongation. In most organisms no specific repair role other than check point control has been assigned to this enzyme. Pol alpha contains both polymerase and exonuclease domains but lacks exonuclease activity suggesting that the exonuclease domain may be for structural purposes only..
	gnl\|CDD\|30766	477	1229	753	Gaps:93	84.60	792	32.39	18.96	1e-112	COG0417 PolB DNA polymerase elongation subunit (family B) [DNA replication recombination and repair].
	gnl\|CDD\|143908	797	1245	449	Gaps:46	99.78	458	32.17	18.38	1e-106	pfam00136 DNA_pol_B DNA polymerase family B. This region of DNA polymerase B appears to consist of more than one structural domain possibly including elongation DNA-binding and dNTP binding activities.
	gnl\|CDD\|128762	621	1008	388	Gaps:36	84.93	471	35.75	15.50	1e-78	smart00486 POLBc DNA polymerase type-B family. DNA polymerase alpha delta epsilon and zeta chain (eukaryota) DNA polymerases in archaea DNA polymerase II in e. coli mitochondrial DNA polymerases and and virus DNA polymerases.
	gnl\|CDD\|99819	540	779	240	Gaps:7	99.57	234	42.92	17.17	2e-77	cd05776 DNA_polB_alpha_exo inactive DEDDy 3'-5' exonuclease domain of eukaryotic DNA polymerase alpha a family-B DNA polymerase. The 3'-5' exonuclease domain of eukaryotic DNA polymerase alpha. DNA polymerase alpha is a family-B DNA polymerase with a catalytic subunit that contains a DnaQ-like 3'-5' exonuclease domain. It is one of the three DNA-dependent type B DNA polymerases (delta and epsilon are the other two) that have been identified as essential for nuclear DNA replication in eukaryotes. DNA polymerase alpha is almost exclusively required for the initiation of DNA replication and the priming of Okazaki fragments during elongation. It associates with DNA primase and is the only enzyme able to start DNA synthesis de novo. The catalytic subunit contains both polymerase and 3'-5' exonuclease domains but only exhibits polymerase activity. The 3'-5' exonuclease domain contains three sequence motifs termed ExoI ExoII and ExoIII without the four conserved acidic residues that are crucial for metal binding and catalysis. This explains why in most organisms that no specific repair role other than check point control has been assigned to this enzyme. The exonuclease domain may have a structural role.
	gnl\|CDD\|149913	1263	1448	186	Gaps:10	100.00	186	57.53	8.06	1e-74	pfam08996 zf-DNA_Pol DNA Polymerase alpha zinc finger. The DNA Polymerase alpha zinc finger domain adopts an alpha-helix-like structure followed by three turns all of which involve proline. The resulting motif is a helix-turn-helix motif in contrast to other zinc finger domains which show anti-parallel sheet and helix conformation. Zinc binding occurs due to the presence of four cysteine residues positioned to bind the metal centre in a tetrahedral coordination geometry. Function of this domain is uncertain: it has been proposed that the zinc finger motif may be an essential part of the DNA binding domain.
	gnl\|CDD\|99919	843	1221	379	Gaps:41	96.50	371	37.43	20.39	4e-70	cd05536 POLBc_B3 DNA polymerase type-B B3 subfamily catalytic domain. Archaeal proteins that are involved in DNA replication are similar to those from eukaryotes. Some members of the archaea also possess multiple family B DNA polymerases (B1 B2 and B3). So far there is no specific function(s) has been assigned for different members of the archaea type B DNA polymerases. Phylogenetic analyses of eubacterial archaeal and eukaryotic family B DNA polymerases are support independent gene duplications during the evolution of archaeal and eukaryotic family B DNA polymerases. Structural comparison of the thermostable DNA polymerase type B to its mesostable homolog suggests several adaptations to high temperature such as shorter loops disulfide bridges and increasing electrostatic interaction at subdomain interfaces..
	gnl\|CDD\|168230	618	1221	604	Gaps:135	71.95	788	29.28	18.69	3e-64	PRK05762 PRK05762 DNA polymerase II Reviewed.
	gnl\|CDD\|99912	846	1221	376	Gaps:68	98.45	323	35.85	17.92	2e-59	cd00145 POLBc DNA polymerase type-B family catalytic domain. DNA-directed DNA polymerases elongate DNA by adding nucleotide triphosphate (dNTP) residues to the 5'-end of the growing chain of DNA. DNA-directed DNA polymerases are multifunctional with both synthetic (polymerase) and degradative modes (exonucleases) and play roles in the processes of DNA replication repair and recombination. DNA-dependent DNA polymerases can be classified in six main groups based upon their phylogenetic relationships with E. coli polymerase I (class A) E. coli polymerase II (class B) E. coli polymerase III (class C) euryarchaeota polymerase II (class D) human polymerase beta (class x) E. coli UmuC/DinB and eukaryotic RAP 30/Xeroderma pigmentosum variant (class Y). Family B DNA polymerases include E. coli DNA polymerase II some eubacterial phage DNA polymerases nuclear replicative DNA polymerases (alpha delta epsilon and zeta) and eukaryotic viral and plasmid-borne enzymes. DNA polymerase is made up of distinct domains and sub-domains. The polymerase domain of DNA polymerase type B (Pol domain) is responsible for the template-directed polymerization of dNTPs onto the growing primer strand of duplex DNA that is usually magnesium dependent. In general the architecture of the Pol domain has been likened to a right hand with fingers thumb and palm sub-domains with a deep groove to accommodate the nucleic acid substrate. There are a few conserved motifs in the Pol domain of family B DNA polymerases. The conserved aspartic acid residues in the DTDS motifs of the palm sub-domain is crucial for binding to divalent metal ion and is suggested to be important for polymerase catalysis..
rpsblast_kog	gnl\|CDD\|36188	4	1448	1445	Gaps:78	99.02	1429	41.55	16.61	0.0	KOG0970 KOG0970 KOG0970 DNA polymerase alpha catalytic subunit [Replication recombination and repair].
	gnl\|CDD\|36187	474	1228	755	Gaps:91	68.86	1066	26.70	22.21	1e-52	KOG0969 KOG0969 KOG0969 DNA polymerase delta catalytic subunit [Replication recombination and repair].
	gnl\|CDD\|36186	597	1222	626	Gaps:92	42.74	1488	23.58	19.65	3e-36	KOG0968 KOG0968 KOG0968 DNA polymerase zeta catalytic subunit [Replication recombination and repair].

Other analysis

Functional Gbrowse

Ortholog