ID A0A016WIZ0_9BILA Unreviewed; 1458 AA.
AC A0A016WIZ0;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN Name=Acey_s0650.g1135 {ECO:0000313|EMBL:EYC39595.1};
GN Synonyms=Acey-Y47D3A.29 {ECO:0000313|EMBL:EYC39595.1};
GN ORFNames=Y032_0650g1135 {ECO:0000313|EMBL:EYC39595.1};
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:EYC39595.1, 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|RuleBase:RU000442};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:EYC39595.1}.
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DR EMBL; JARK01000250; EYC39595.1; -; Genomic_DNA.
DR Proteomes; UP000024635; Unassembled WGS sequence.
DR GO; GO:0042575; C:DNA polymerase complex; IEA:UniProt.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:1902975; P:mitotic DNA replication initiation; IEA:InterPro.
DR CDD; cd05776; DNA_polB_alpha_exo; 1.
DR CDD; cd05532; POLBc_alpha; 1.
DR Gene3D; 2.40.50.730; -; 1.
DR Gene3D; 3.30.70.2820; -; 1.
DR Gene3D; 1.10.3200.20; DNA Polymerase alpha, zinc finger; 1.
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; IPR024647; DNA_pol_a_cat_su_N.
DR InterPro; IPR042087; DNA_pol_B_thumb.
DR InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR InterPro; IPR038256; Pol_alpha_znc_sf.
DR InterPro; IPR045846; POLBc_alpha.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR015088; Znf_DNA-dir_DNA_pol_B_alpha.
DR NCBIfam; TIGR00592; pol2; 1.
DR PANTHER; PTHR45861; DNA POLYMERASE ALPHA CATALYTIC SUBUNIT; 1.
DR PANTHER; PTHR45861:SF1; DNA POLYMERASE ALPHA CATALYTIC SUBUNIT; 1.
DR Pfam; PF12254; DNA_pol_alpha_N; 1.
DR Pfam; PF00136; DNA_pol_B; 1.
DR Pfam; PF03104; DNA_pol_B_exo1; 1.
DR Pfam; PF08996; zf-DNA_Pol; 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 DNA replication {ECO:0000256|RuleBase:RU000442};
KW DNA-binding {ECO:0000256|RuleBase:RU000442};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW ECO:0000256|RuleBase:RU000442};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW 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};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 29..92
FT /note="DNA polymerase alpha catalytic subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12254"
FT DOMAIN 455..718
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 784..1225
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 1270..1451
FT /note="Zinc finger DNA-directed DNA polymerase family B
FT alpha"
FT /evidence="ECO:0000259|Pfam:PF08996"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 77..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 815..847
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..158
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 818..845
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1458 AA; 164107 MW; 7A39C92999E367DF CRC64;
MSDAENEVEC RRSSRRRESA RQQSRRSALE AMKEARRSGK AHRVDLDSLI GNVYEEVDED
EYNEIVRKRQ AADFVVDDDG SGYVDHGADI FDDEEDEEDD MVDRKSKKKR KDKKDPTQKK
GLDSYFAPAA HDRGKVKDDT EVKLDDDEDL KDMLAGINDE ALEMDFSSQP SPAPTSSSTR
NPFKREASPT IAPRKVKVMK LATPTARSVP PPIRHAQAVP QNSVKAEVQV DDDDDYGAPD
FDDYYEPPPP AAPLSPKAAK SPKKVANSAP SVEVKAEVKK EVEEMQVEPS SLVEDTKPVP
KPTPQVMLSA ADWDDSQEAA DEPAVEVVAG SEAFYVKEDG QQMIRMYWLD AFEDPVKHSG
TVYLFGRVNV SGNKWASCCV TVKNIFRQVF FLPRDTKFVR GASTNEQVKD ADVFEEVKVM
MKRHCGTASF KCRQARKRFM HDGTISGEHS SDEVKVIEVQ YESNHPKLPT DLSGETFSAV
FNTTTTAMER LLVEKAMMGP GWVDVTNYTE VTAKQSYCDY EFSVDMERMR NLNYNSAITQ
AAPPVRMLVL NVLTTLNDKK ENEICMISML YNPACNLSNP STDQKDLHRL CMFTKPYGGT
LPFDIKDQLN RRGLSDIVLT AGNEKALLSL FLAKVHKYEP DIIVGHDLSA SISVLVSRMD
KLKVANWSRT SRLKRTINVG KVAHNKAGQW ELTAGRMLVD SRLSAMELVR SRSYDLSELV
TQLLGVHREN IYANEVAAKF SSSQQLLNLI QWSWMDPWFS LRVIAQINAL QLAVQITNIV
GGVTSRTLMG GRAERNEYLL LHAFNKANYI APNKYQPSFR KGKHEKEVKN EDGENADDNE
ADGKSKNKAQ YSGGLVLEPK KGLYDTLILL LDFNSLYPSI IQEYNICFTT VAHTKDGDDL
PDIPSSSLAE GILPCEIRGL VERRRQVKSL MKEAPESKKK QYDIRQMALK LTANSMYGCL
GFQQSRFYAK PLAALITSKG REILMHTKDL VEKLGYSVVY GDTDSIMINT NSTDLKQAKK
LGFEIKRQVN QCHRLLELEL DGVFKRMLLL KKKKYAALTV NPDNELDTKK ELKGLDIVRR
DWSQLAKEAG NAVVDLILDP KLSRDELVAE IHESLQKLRA RLDKGMDTKL FEISKQLTRN
PKDYHDLKSQ PHAAVAMRLN ETGKFSLRHG DIVEYIICED GTTNSAMQRA YHRTELESNP
ELKIDLHYYL AQQVHPVVSR LCAPIEETDA VRIAEALGMD STSYRRSAAA HASDAAAAED
EWAWQGPITY DHCEALTFTC PSTGCGNVLR IRKAVEEQGS TFKLSLEACD KCGAELSPYS
AYICNRVEDA LREFVARHLS SCFKCDDAVC EFRTKVHLMK WCREGLECPK CPGGVLRKEY
SAKDLFDQEM FLKQVVDVPT ALQELKPEQQ RSIQTKPGFA STMALYNNLS AIVARYLDRN
AYSKVDLAFI FAPMMKIA
//
