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
//