ID B5IFQ0_ACIB4 Unreviewed; 1090 AA.
AC B5IFQ0;
DT 14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2008, sequence version 1.
DT 28-JAN-2026, entry version 91.
DE RecName: Full=DNA polymerase II large subunit {ECO:0000256|HAMAP-Rule:MF_00324};
DE Short=Pol II {ECO:0000256|HAMAP-Rule:MF_00324};
DE EC=2.7.7.7 {ECO:0000256|HAMAP-Rule:MF_00324};
DE AltName: Full=Exodeoxyribonuclease large subunit {ECO:0000256|HAMAP-Rule:MF_00324};
DE EC=3.1.11.1 {ECO:0000256|HAMAP-Rule:MF_00324};
GN Name=polC {ECO:0000256|HAMAP-Rule:MF_00324};
GN OrderedLocusNames=Aboo_1172 {ECO:0000313|EMBL:ADD08981.1};
OS Aciduliprofundum boonei (strain DSM 19572 / T469).
OC Archaea; Methanobacteriati; Thermoplasmatota; DHVE2 group;
OC Candidatus Aciduliprofundum.
OX NCBI_TaxID=439481 {ECO:0000313|EMBL:ADD08981.1, ECO:0000313|Proteomes:UP000001400};
RN [1] {ECO:0000313|EMBL:ADD08981.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=T469 {ECO:0000313|EMBL:ADD08981.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Saunders E., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Flores G., Reysenbach A.-L., Woyke T.;
RT "Complete sequence of Aciduliprofundum boonei T469.";
RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Possesses two activities: a DNA synthesis (polymerase) and an
CC exonucleolytic activity that degrades single-stranded DNA in the 3'- to
CC 5'-direction. Has a template-primer preference which is characteristic
CC of a replicative DNA polymerase. {ECO:0000256|ARBA:ARBA00025068,
CC ECO:0000256|HAMAP-Rule:MF_00324}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=DNA(n) + a 2'-deoxyribonucleoside 5'-triphosphate = DNA(n+1) +
CC diphosphate; Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-
CC COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112;
CC EC=2.7.7.7; Evidence={ECO:0000256|ARBA:ARBA00049244,
CC ECO:0000256|HAMAP-Rule:MF_00324};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield
CC nucleoside 5'-phosphates.; EC=3.1.11.1; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00324};
CC -!- SUBUNIT: Heterodimer of a large subunit and a small subunit.
CC {ECO:0000256|ARBA:ARBA00011315, ECO:0000256|HAMAP-Rule:MF_00324}.
CC -!- SIMILARITY: Belongs to the archaeal DNA polymerase II family.
CC {ECO:0000256|ARBA:ARBA00011053, ECO:0000256|HAMAP-Rule:MF_00324}.
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DR EMBL; CP001941; ADD08981.1; -; Genomic_DNA.
DR RefSeq; WP_008085741.1; NC_013926.1.
DR AlphaFoldDB; B5IFQ0; -.
DR STRING; 439481.Aboo_1172; -.
DR GeneID; 8828132; -.
DR KEGG; abi:Aboo_1172; -.
DR eggNOG; arCOG04447; Archaea.
DR HOGENOM; CLU_001154_0_0_2; -.
DR OrthoDB; 7529at2157; -.
DR Proteomes; UP000001400; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008310; F:single-stranded DNA 3'-5' DNA exonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0006308; P:DNA catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006261; P:DNA-templated DNA replication; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00324; DNApol_II_L_arch; 1.
DR InterPro; IPR004475; PolC_DP2.
DR InterPro; IPR056172; PolC_DP2_cat_dom.
DR InterPro; IPR056171; PolC_DP2_central_dom.
DR InterPro; IPR016033; PolC_DP2_N.
DR InterPro; IPR054475; Znf-DPOE.
DR NCBIfam; TIGR00354; polC; 1.
DR NCBIfam; NF003103; PRK04023.1; 1.
DR PANTHER; PTHR42210; DNA POLYMERASE II LARGE SUBUNIT; 1.
DR PANTHER; PTHR42210:SF1; DNA POLYMERASE II LARGE SUBUNIT; 1.
DR Pfam; PF24846; PolC_DP2_cat; 1.
DR Pfam; PF24844; PolC_DP2_central; 1.
DR Pfam; PF03833; PolC_DP2_N; 1.
DR Pfam; PF22912; zf-DPOE; 1.
DR PIRSF; PIRSF016275; PolC_DP2; 1.
PE 3: Inferred from homology;
KW DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP-
KW Rule:MF_00324};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_00324};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW ECO:0000256|HAMAP-Rule:MF_00324};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW Rule:MF_00324};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00324};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268, ECO:0000256|HAMAP-
KW Rule:MF_00324};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_00324};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_00324}; Reference proteome {ECO:0000313|Proteomes:UP000001400};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00324}.
FT DOMAIN 10..274
FT /note="DNA polymerase II large subunit DP2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03833"
FT DOMAIN 278..651
FT /note="DNA polymerase II large subunit DP2 central"
FT /evidence="ECO:0000259|Pfam:PF24844"
FT DOMAIN 666..960
FT /note="DNA polymerase II large subunit DP2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF24846"
FT DOMAIN 1001..1054
FT /note="DNA polymerase-epsilon zinc finger"
FT /evidence="ECO:0000259|Pfam:PF22912"
SQ SEQUENCE 1090 AA; 123929 MW; E20A461EDFA7FEBC CRC64;
MVEASKDMLR YFEELERNAE EIYKIAREAR SMRFDPVPDV EIPRAKDLAA RVEELTGVKG
IADEIRELSK SHDRGMVSLL MAKRIAKKFD RKDEALDKAI RVGLAILTEG ILVAPLEGIA
NVKIKKNDDG TDYVSIYYAG PIRGAGGTAQ ALSVLIADVV RRELEIGRYK PTEAEIERYK
EEIQLYDRIH HLQYRPTNEE IELVVNNCPV CIDGEGTEKV EVSGYRNLPR IDTNRVRGGM
CLVLAEGLLQ KTKKIKAYVD MLKIDGWDWI KKLIPEVKED KFELKPLKKF MKDVIAGRPI
FSYPMAPGGF RLRYGRCRAG GLATLSVNPA TMYILNKFIA IGTQLKVERP GKAGGMTSCD
SIEGPIVLLK NGDLIQINEL EKAREYYDSV VEIVDVGEML IPYGEFLENN HPLIPGAYAV
EWWEQEAERV GFHGEIKNSF EAFQISEEYS VPLHPDYNLF WHDLSLEELR KLSEFLENHS
FWKDEKLYVE KNWEIKEILK KLGALHLERE YYILDRYAYP LLRGVGLDLK DGKIVRRKEI
KEGNIMDVVS ELAGVKIRER APVRIGARMG RPEKAAPRKM KPPIHSLFPI GDAGGNRRLI
TEAINKKIIP IEIGIRKCPK CGEKTILPFC PKCGAPTQFM EKVVVKKVDI SDLFARAQEY
LGENVDWDVK GVKKMMSQEH IPERLEKGIL RAKNGVYVFK DGTARFDMSD IAITHFRPKE
IGLSVEKARK LGYTKDYLGH DLKDGEQLCE LKVQDIIIPK SAADYLIKIA NYVDDLLEKF
YKMKRFYNVK KREDLIGHLV IGLAPHTSAG ILGRIIGFSD ANVGFAHPFF HAAKRRNCDG
DEDSIMLLLE GLLDFSRKFL PSTRGGLMDA PLVLTTRITP TEIDKEALHV DVMERYPLEF
YEATLKYAKP DEVADIMDFV KKRIETPRQY EGFKFTHDTR DINVGVLTSA YKVLGSMQEK
LDSQLQLARK IRAVDEHDMA ARIIAHHFIP DIMGNLKKFG TQGFRCTKCG AKYRRVPLNN
VCPKCGGNVI LTVSEGSVKK YLDKALNLAE EYDVPLYVKQ RVLALKESVD SLFAEEEEKN
KITLESFLAV
//
