ID A0A024USU1_9STRA Unreviewed; 1050 AA.
AC A0A024USU1;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN ORFNames=H310_01455 {ECO:0000313|EMBL:ETW08977.1};
OS Aphanomyces invadans.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Aphanomyces.
OX NCBI_TaxID=157072 {ECO:0000313|EMBL:ETW08977.1};
RN [1] {ECO:0000313|EMBL:ETW08977.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NJM9701 {ECO:0000313|EMBL:ETW08977.1};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., van West P., Dieguez-Uribeondo J., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Chapman S.B.,
RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Aphanomyces invadans NJM9701.";
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
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; KI913953; ETW08977.1; -; Genomic_DNA.
DR RefSeq; XP_008862782.1; XM_008864560.1.
DR AlphaFoldDB; A0A024USU1; -.
DR STRING; 157072.A0A024USU1; -.
DR EnsemblFungi; H310_01455-t26_1; H310_01455-t26_1-p1; H310_01455.
DR EnsemblProtists; ETW08977; ETW08977; H310_01455.
DR GeneID; 20078505; -.
DR VEuPathDB; FungiDB:H310_01455; -.
DR eggNOG; KOG0969; Eukaryota.
DR OrthoDB; 211439at2759; -.
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}; 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 134..420
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 484..918
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 959..1029
FT /note="C4-type zinc-finger of DNA polymerase delta"
FT /evidence="ECO:0000259|Pfam:PF14260"
SQ SEQUENCE 1050 AA; 117503 MW; 99B90DFE79492C34 CRC64;
MEPPAKKSRV LRTHASTWPR TTLPSLNAAE HDIRFQWIDI SMYDGEPLAV NPYSRTQPIP
GPRTGSSSII RLTGVTEDGH SIMAHIHGFV PYFYASCPDG LKPSDCNIVR EALDAAAKKN
PSDAPAVQLV EIVEDKMSLY GYQFDKKVRL IKIYLSLPNF VPKLRTALES GITIPGYGTR
SYQTYESNVP YILRFMIDQE IQGCNWVELP AATYRFRTPE KQLSLCQMEV DIVYLNLVSH
APVGAWGKLA PLRILSFDIE CMGRTGQFPD ADKDPVIQIA NVVWEQGAEH PVTRNVFVLG
TCKPIVGAHV MEFESEGDML EAWASFVRQV DPDILTGYNI DNFDVPYLIN RGKALKLTPQ
YHCWGRLKNT PNHMEKKAFQ SAQYGKSDNM RTTMHGRTSF DMLPIIRRNQ QLSSYSLNSV
CAQFLGQQKE DVPHGIISDL QRGTDDDRHR LAVYCLKDAV LPLTLLQKLS YLVNYIEMAR
VTGVPLDFLI DRGQQIKVYS MLLRKCRGAG LVVPNLPRAG GGDDIGYEGA TVIEPVKAYY
TVPIATLDFA SLYPSIMQGY NLCYSTLVAP SDINKLPVDA YQTSPSGDVF VRSATKKGIL
PLILEELLSA RKQAKRDMAT APDAMSKAVQ NGRQLALKVS ANSVYGFTGA NVGQLPCIPI
ASSVTAYGRD LLLRTREEVE KVFTIENGYK NNAEVIYGDT DSVMVKFGVE TVAEAMPLAE
EAAKLVSDIF PKPIKLEFEK VYYPYLLMNK KRYAGLLWTK AEKYDKLDTK GLETVRRDNC
LLVRRMVESC LKKILIERNV DAAISYTKHI ISELLQNKID ISLLVITKGL SKSTDSDDYK
VKQAHTELAA RMKKRDPGSA PVLGERVAYV IIDKGKNVPL YDKAEDPVYA LTNNIPIDCD
YYMSNQLQNP IERIFEPIIG LSKVKSDLLA GDHTRKRSKP GLVQNSGGMM NFAVKKQKCL
GCKAPLGGDQ ALCASCIEQE AQVYSKQLSV VVAAEQQFAR LWTQCQNCQG SLHQDVLCTS
RDCPIFYKRI KVQKELGEAQ LALERFKYEW
//