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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//