UniProt: A0A1B1DWA0

Database: UniProt
Entry: A0A1B1DWA0_9APIC

LinkDB:  A0A1B1DWA0_9APIC 
Original site:  A0A1B1DWA0_9APIC

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Ontology (8)   
   GO (8)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (15)   
   InterPro (10)   
   Pfam (3)   
   PROSITE (1)   
   SMART (1)   
All databases (27)   

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ID   A0A1B1DWA0_9APIC        Unreviewed;      1092 AA.
AC   A0A1B1DWA0;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN   ORFNames=PCOAH_00015320 {ECO:0000313|EMBL:ANQ07063.1};
OS   Plasmodium coatneyi.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium.
OX   NCBI_TaxID=208452 {ECO:0000313|EMBL:ANQ07063.1, ECO:0000313|Proteomes:UP000092716};
RN   [1] {ECO:0000313|Proteomes:UP000092716}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hackeri {ECO:0000313|Proteomes:UP000092716};
RA   Chien J.-T., Pakala S.B., Geraldo J.A., Lapp S.A., Barnwell J.W.,
RA   Kissinger J.C., Galinski M.R., Humphrey J.C.;
RT   "First high quality genome sequence of Plasmodium coatneyi using continuous
RT   long reads from single molecule, real-time sequencing.";
RL   Submitted (JUN-2016) 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; CP016244; ANQ07063.1; -; Genomic_DNA.
DR   RefSeq; XP_019913758.1; XM_020058341.1.
DR   AlphaFoldDB; A0A1B1DWA0; -.
DR   EnsemblProtists; ANQ07063; ANQ07063; PCOAH_00015320.
DR   GeneID; 30908258; -.
DR   VEuPathDB; PlasmoDB:PCOAH_00015320; -.
DR   OrthoDB; 211439at2759; -.
DR   Proteomes; UP000092716; Chromosome 6.
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          168..469
FT                   /note="DNA-directed DNA polymerase family B exonuclease"
FT                   /evidence="ECO:0000259|Pfam:PF03104"
FT   DOMAIN          534..965
FT                   /note="DNA-directed DNA polymerase family B
FT                   multifunctional"
FT                   /evidence="ECO:0000259|Pfam:PF00136"
FT   DOMAIN          1001..1071
FT                   /note="C4-type zinc-finger of DNA polymerase delta"
FT                   /evidence="ECO:0000259|Pfam:PF14260"
SQ   SEQUENCE   1092 AA;  125796 MW;  53118FCA7E142BBC CRC64;
     MESMKKCPFT SVIPYGMLYE KLKKEKNNQL PENVVIQEFD QLLATYERPS PYDANGLIHI
     SNKSDLFLFQ IDIEYTVDSI FKNMVSTNDG SALTDIYSTY RTMLQNSEKN YISVPVIHIY
     TVTNDGYSVL VSVHNFFPYF YVEMPSNFQK EDLLKLECMM NDNLNMNNQY KMYDQKILNI
     EIVKTESLMY YKREGKKDFL KITVLLPKMV PTLKKFFEGV VNVNGKNIGG IVYEANLPFI
     LRYIIDKKIT GSSWLLCKKE HFYIRPKHKK ISNCSFEIDI SYEHLEPMPL ENEYQQIPKL
     RILSFDIECI KLDGKGFPEA KNDPIIQISS ILYFQGDPIG KCSKFIFTLK ECASIPGSNV
     IWFHDEKTLL DAWNEFITRL DPDFLTGYNI INFDLPYILN RGTALNLKKL KMLGRIKSIS
     SVVKESNFSS KQFGNHETKE ININGRIQFD VYDLIRRDYK LKSYTLNYVS FEFLKEQKED
     VHYSIMNDLQ NESPESRKRI ATYCIKDGIL PLRLIDKLLF IYNYVEMARV TGTPFVYLLT
     RGQQIKVTSQ LYRKCKELNY VIPSTYIKPA SNEKYEGATV LEPIKGYYIE PISTLDFASL
     YPSIMIAHNL CYSTLVKNNS ELEGLKQEEV TSIQGKSNIK FVKGSVKKGI LPLIVEELID
     ARKKVKLLIK NETNKITKMV LNGRQLALKI SANSVYGYTG AASGGQLPCL EVAVSITTLG
     RSMIDKTKES VEKYYSKSNG FEHNSTVVYG DTDSVMIKFG TSSIAEAMAL GKDAAQRISK
     EFLHPIKLEF EKVYCPYLLL NKKRYAGLLY TTPEKHDKMD CKGIETVRRD FCILIQQMME
     TVLNKLLIEK NLNSAIEYTK SKIKDLLTNN IDMSLLVVTK SLGKTDYETR LPHVELAKKL
     KQRDSATAPN VGDRVSYIII KGVKGQAQYE RAEDPLYVLD NNLAIDYNHY LDAIKNTLSR
     IFEVIMNNSD SLFCGEHTRH KTILTSSQTA LSKFLQKAVR CIGCNSSIKK PPLCNHCKSN
     KEFSIYMQKM NLFKNKQNEF FQLWTECQRC QGNLHAEVIC MNRDCPIFYR RAKIKKDMAN
     VQEQISALRA DW
//

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