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Database: UniProt
Entry: A0A016VN40_9BILA
LinkDB: A0A016VN40_9BILA
Original site: A0A016VN40_9BILA 
ID   A0A016VN40_9BILA        Unreviewed;      1093 AA.
AC   A0A016VN40;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-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   Name=Acey_s0007.g3535 {ECO:0000313|EMBL:EYC28994.1};
GN   Synonyms=Acey-F10C2.4 {ECO:0000313|EMBL:EYC28994.1};
GN   ORFNames=Y032_0007g3535 {ECO:0000313|EMBL:EYC28994.1};
OS   Ancylostoma ceylanicum.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC   Ancylostomatinae; Ancylostoma.
OX   NCBI_TaxID=53326 {ECO:0000313|EMBL:EYC28994.1, ECO:0000313|Proteomes:UP000024635};
RN   [1] {ECO:0000313|Proteomes:UP000024635}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX   PubMed=25730766; DOI=10.1038/ng.3237;
RA   Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA   Aroian R.V.;
RT   "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT   ceylanicum identify infection-specific gene families.";
RL   Nat. Genet. 47:416-422(2015).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EYC28994.1}.
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DR   EMBL; JARK01001343; EYC28994.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A016VN40; -.
DR   STRING; 53326.A0A016VN40; -.
DR   Proteomes; UP000024635; Unassembled WGS sequence.
DR   GO; GO:0043625; C:delta DNA polymerase complex; IEA:UniProt.
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; 2.40.50.730; -; 2.
DR   Gene3D; 1.10.132.60; DNA polymerase family B, C-terminal domain; 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   Reference proteome {ECO:0000313|Proteomes:UP000024635};
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          171..464
FT                   /note="DNA-directed DNA polymerase family B exonuclease"
FT                   /evidence="ECO:0000259|Pfam:PF03104"
FT   DOMAIN          528..960
FT                   /note="DNA-directed DNA polymerase family B
FT                   multifunctional"
FT                   /evidence="ECO:0000259|Pfam:PF00136"
FT   DOMAIN          998..1071
FT                   /note="C4-type zinc-finger of DNA polymerase delta"
FT                   /evidence="ECO:0000259|Pfam:PF14260"
FT   REGION          15..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1093 AA;  122700 MW;  21A2A894662344E4 CRC64;
     MKLFSINKRI VFQMSPPKKR SSTLPSAAAP KRRKGDEEPA NKGAFESQLE QLSQNSEAES
     CASTWDRVDL EEGLGTTKSI TLQVFDIESY HEPGSATSFD RTNVKLYGVN RAGNSICAIV
     TGYFPHFYFQ APENFAPEHL DVAQRNLNNA VAVSLRRANS NLQMSSTVVD NLVRLSIVHG
     ENVYYYRGSE KKYPFIKVSG TTNALNKAKQ ELKNGGFSFG HGPVKVGTLY EANIDAEVKF
     MAHSGIVGCG WVEIPAGKVV IHHSKSQSSR CQLEVEVKLS DLIVHDPEGE WAAVAPIRTL
     SFDIECMGRR GIFPDANEDP VIQIANMVKV EGESEPFIRN CFVLGTCSPV IGSDIIQCSS
     EKELLEKWAE FVRAVDPDIM TGYNILNFDL PYILDRAKVL KLPSVAMLGR QRDRASSVRD
     AAISSKQMGS RVNKSIDIHG RVIFDVLQVV LRDYKLRSYT LNSVSYHFLS EQKEDVEHSI
     ISDLQKGDEH TRRRLAVYCM KDAVLPLRLL EKLLSVINYM EMARVTGVPL NYLLTRGQQI
     KILSMMLRKC KADHFFLPVI EVQGGDNEGY EGATVIEPLR GFYNEPIATL DFASLYPSIM
     IAHNLCYTTL LKKPEGEEGK DYIKTPSGNY FATKERRRGL LPVILEDLLA ARKRAKNEMK
     HEKDEFRKMV LNGRQLALKV SANSVYGFTG AVVGKLPCLE ISQSVTAFGR QMIDLTKTEV
     EKRYTAGALD GKCPANAQVV YGDTDSVMVK FGVKTVAEAM EIGLHAATEV SKIFTPPIKL
     EFEKVYFPYL LINKKRYAGL YFTKPDKHDK MDCKGLETVR RDNCPLVAKV LNTCLEKLMI
     DRDANSALEF AKRVISDLLC NKIDISMLII SKELTKSGEK YQAKQAHVEL AARMRKRDPG
     SAPRLGDRVP YVIIAAAKNV PAYEKAEDPN FVLKNNIPID NKHYLTNQLA KPLARIFEPI
     LGDRAERILI EGEHTRVRTV VQSKVGGLAA FTRKQVTCLG CKAVLKDQHR AVCDFCLKKG
     KLPEIYAQRV TNVNIIERHF SRLWTECQNC AKTMHDKVNC SARDCPIYYM REKVRGDLRE
     AHSALERFGV PSW
//
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