ID H1VBL1_COLHI Unreviewed; 1103 AA.
AC H1VBL1;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN ORFNames=CH063_01733 {ECO:0000313|EMBL:CCF37614.1}, CH63R_04436
GN {ECO:0000313|EMBL:OBR12140.1};
OS Colletotrichum higginsianum (strain IMI 349063) (Crucifer anthracnose
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum destructivum species complex.
OX NCBI_TaxID=759273 {ECO:0000313|EMBL:CCF37614.1, ECO:0000313|Proteomes:UP000007174};
RN [1] {ECO:0000313|EMBL:CCF37614.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMI 349063 {ECO:0000313|EMBL:CCF37614.1};
RA Ma L.-J., O'Connell R., van Themaat E.V.L., Stueber K., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Heiman D., Howarth C., Larimer J., Lui A.,
RA MacDonald P.J.P., McCowen C., Montmayeur A., Murphy C., Neiman D.,
RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., Stolte C.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The genome sequence of Colletotrichum higginsianum IMI 34906.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000007174}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMI 349063 {ECO:0000313|Proteomes:UP000007174};
RX PubMed=22885923; DOI=10.1038/ng.2372;
RA O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA Ma L.-J., Vaillancourt L.J.;
RT "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT by genome and transcriptome analyses.";
RL Nat. Genet. 44:1060-1065(2012).
RN [3] {ECO:0000313|EMBL:OBR12140.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMI 349063 {ECO:0000313|EMBL:OBR12140.1};
RA O'Connell R., Zambounis A., Thon M., Dallery J.-F.;
RT "Resequencing and annotation of the Colletotrichum higginsianum genome.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|Proteomes:UP000092177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMI 349063 {ECO:0000313|Proteomes:UP000092177};
RX PubMed=28851275; DOI=10.1186/s12864-017-4083-x;
RA Dallery J.-F., Lapalu N., Zampounis A., Pigne S., Luyten I., Amselem J.,
RA Wittenberg A.H.J., Zhou S., de Queiroz M.V., Robin G.P., Auger A.,
RA Hainaut M., Henrissat B., Kim K.-T., Lee Y.-H., Lespinet O., Schwartz D.C.,
RA Thon M.R., O'Connell R.J.;
RT "Gapless genome assembly of Colletotrichum higginsianum reveals chromosome
RT structure and association of transposable elements with secondary
RT metabolite gene clusters.";
RL BMC Genomics 18:667-667(2017).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.7;
CC Evidence={ECO:0000256|ARBA:ARBA00024632,
CC ECO:0000256|RuleBase:RU000442};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966,
CC ECO:0000256|RuleBase:RU000442};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU000442}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC {ECO:0000256|ARBA:ARBA00005755, ECO:0000256|RuleBase:RU000442}.
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DR EMBL; CACQ02002546; CCF37614.1; -; Genomic_DNA.
DR EMBL; LTAN01000003; OBR12140.1; -; Genomic_DNA.
DR RefSeq; XP_018160657.1; XM_018299411.1.
DR STRING; 759273.H1VBL1; -.
DR EnsemblFungi; CCF37614; CCF37614; CH063_01733.
DR GeneID; 28863518; -.
DR KEGG; chig:CH63R_04436; -.
DR VEuPathDB; FungiDB:CH63R_04436; -.
DR eggNOG; KOG0969; Eukaryota.
DR HOGENOM; CLU_000203_2_0_1; -.
DR OrthoDB; 211439at2759; -.
DR Proteomes; UP000007174; Unassembled WGS sequence.
DR Proteomes; UP000092177; Chromosome 3.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd05777; DNA_polB_delta_exo; 1.
DR CDD; cd05533; POLBc_delta; 1.
DR Gene3D; 1.10.132.60; DNA polymerase family B, C-terminal domain; 1.
DR Gene3D; 3.30.342.10; DNA Polymerase, chain B, domain 1; 1.
DR Gene3D; 1.10.287.690; Helix hairpin bin; 1.
DR Gene3D; 3.90.1600.10; Palm domain of DNA polymerase; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR InterPro; IPR006172; DNA-dir_DNA_pol_B.
DR InterPro; IPR017964; DNA-dir_DNA_pol_B_CS.
DR InterPro; IPR006133; DNA-dir_DNA_pol_B_exonuc.
DR InterPro; IPR006134; DNA-dir_DNA_pol_B_multi_dom.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR042087; DNA_pol_B_thumb.
DR InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR025687; Znf-C4pol.
DR NCBIfam; TIGR00592; pol2; 1.
DR PANTHER; PTHR10322; DNA POLYMERASE CATALYTIC SUBUNIT; 1.
DR PANTHER; PTHR10322:SF23; DNA POLYMERASE DELTA CATALYTIC SUBUNIT; 1.
DR Pfam; PF00136; DNA_pol_B; 1.
DR Pfam; PF03104; DNA_pol_B_exo1; 1.
DR Pfam; PF14260; zf-C4pol; 1.
DR PRINTS; PR00106; DNAPOLB.
DR SMART; SM00486; POLBc; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|RuleBase:RU000442};
KW DNA replication {ECO:0000256|RuleBase:RU000442};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU000442};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW ECO:0000256|RuleBase:RU000442};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU000442};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU000442};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU000442};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU000442};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU000442};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000442};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU000442};
KW Zinc-finger {ECO:0000256|RuleBase:RU000442}.
FT DOMAIN 174..471
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 535..966
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 1004..1078
FT /note="C4-type zinc-finger of DNA polymerase delta"
FT /evidence="ECO:0000259|Pfam:PF14260"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 423..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1103 AA; 124809 MW; 96939DC54649D4EE CRC64;
MATVLPQKRV LGETPSTRRN IPSTPSSLKK RKVEGFSSSP AHHFGPQRNS KGLPGSSQPK
SAFESEVLEK LSQDIADRKQ NNTEKDQAWE RPPLVDFNPA RDNLIFQQIE AEEGSLHGGR
ATVKLFGVTE KGHSVMLHVT DFKHYLYVAA PVAFRPEDCN AFKAYLESQV AQHQPCIHSV
AFLMRENIYG FQGNVKSPYL KITVMDPKFI SRVRTTIESG NANWKGLWKG MDGGVMTFDN
IQFVLRFMVD CKIFGMSWVE APATKYQVIP QPQRQSNCQI EAEISYLDLI AHKPVGEWSK
MAPLRIMSFD IECAGRKGIF PEATHDPVIQ IANVVTRYGE KKPFVRNVFC LDTTSPIVAT
QILDFQKEEK MLSEWQKFLI KVDPDILIGY NIANFDFPYL LDRAKHLKVS GFEYWSRIPS
MPSRAKETNF SSKQMGNRDS KATNTNGRLQ LDLLQLVQRD HHLRSYTLNS VCSQFLGEQK
EDVHHTMITE LFNGTPESRR RLALYCLKDA YLPQRLMDKL SCLENYTEMA RVTGIPFNFL
LSRGQQVKFI SQLFRKALEQ KLVIPNMRSE GSDEQYEGAT VIEPTRGYYD VPVATLDFAS
LYPSIMQAHN LCYTTLVNKK AIEKFQLKKD EDYIVTPNGD TFVTNKQRKG LLAQILEELL
SARKQAKREL AVETDPFKKA VLNGRQLALK ISANSVYGLT GATTGKLPCL EIASSTTSFG
RQMIMKTKEE VEKKYCIANG YSHDAQVIYG DTDSVMVKFG TKDLPEAMKL GEEAANHVSS
KFVKPIKLEF EKVYYPYLLI NKKRYAGLYW TKPEKYDKMD TKGIETVRRD NCLLVQTVIE
KVLRMILIDQ DVQGAQDYVK DTIADLLQNK VDMSKLVITK ALTKDDYAAK QAHVELAQRM
KKRDAGSAPG LGDRVAYVMI KGPAGSKNYE KSEDPIYVLE NNVPIDTRYY LDNQLAKPLG
RIFEPILGET KANSLLTGAH TRTIAVSAPT VGGLMKFAKK TQTCMGCKKP LRGKEESAGA
VCSDCAPRVG ELYKKTLDKV SDLEVRFGRL WTQCQRCQGS MHCEVICSSK DCPIFYMRMK
AKKDLEDAGK ELTRFDFDQA AIW
//
