ID F9CUT9_9ARCH Unreviewed; 1111 AA.
AC F9CUT9;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 48.
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 ORFNames=MY1_1899 {ECO:0000313|EMBL:EGP94643.1};
OS Nitrosarchaeum koreense MY1.
OC Archaea; Nitrososphaerota; Nitrososphaeria; Nitrosopumilales;
OC Nitrosopumilaceae; Nitrosarchaeum.
OX NCBI_TaxID=1001994 {ECO:0000313|EMBL:EGP94643.1, ECO:0000313|Proteomes:UP000004440};
RN [1] {ECO:0000313|EMBL:EGP94643.1, ECO:0000313|Proteomes:UP000004440}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MY1 {ECO:0000313|EMBL:EGP94643.1,
RC ECO:0000313|Proteomes:UP000004440};
RX PubMed=21914867; DOI=10.1128/JB.05717-11;
RA Kim B.K., Jung M.Y., Yu D.S., Park S.J., Oh T.K., Rhee S.K., Kim J.F.;
RT "Genome Sequence of an Ammonia-Oxidizing Soil Archaeon, "Candidatus
RT Nitrosoarchaeum koreensis" MY1.";
RL J. Bacteriol. 193:5539-5540(2011).
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=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 -!- 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, 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}.
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:EGP94643.1}.
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DR EMBL; AFPU01000001; EGP94643.1; -; Genomic_DNA.
DR AlphaFoldDB; F9CUT9; -.
DR STRING; 1001994.MY1_1899; -.
DR PATRIC; fig|1001994.6.peg.1869; -.
DR Proteomes; UP000004440; Unassembled WGS sequence.
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; IPR016033; PolC_DP2_N.
DR NCBIfam; TIGR00354; polC; 1.
DR PANTHER; PTHR42210; DNA POLYMERASE II LARGE SUBUNIT; 1.
DR PANTHER; PTHR42210:SF1; DNA POLYMERASE II LARGE SUBUNIT; 1.
DR Pfam; PF03833; PolC_DP2; 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};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00324}.
FT DOMAIN 7..862
FT /note="DNA polymerase II large subunit DP2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03833"
SQ SEQUENCE 1111 AA; 124614 MW; 4FE45693E01F445C CRC64;
MPNYYLDYYS NLSKDTYAIF EHAAMAKSTL VDSSGIIEPK IAFDLADRVS KMHDIDIAEP
LRVLLQIHGK ELSALILSKE IALGKYSLND ATLEEKLDLA VRVGLAIVTE GVTIAPLQGI
SEVKIKKNKD GSEYLSVSIA GPMRSAGGTE SAVTILIADH VRKAVGLSKY QANCFDDETG
RFIEELRIYE REASSFQFHI LDEDIEHVIS HLPVELNGVD TDPFEVVNHK GMTRITTNRV
RGGALRVLND GLIGRSKKLL KRIEMYQLDG WEWLGDLKGA VQTGDNQEDA AAKRMREVIT
GRSVLSMPNK LGGFRLRYGR ACNTGFAAVG INPVIAEILD HTIAVGTQVK TDIPGKGATV
AFVDSIDTPI VRLKNGNVIK IKDVKHGIEI KGEIEKILHL GDILISFGDF LENNAQLIPS
GYVEEFWIEE LKEKLAKYAP DDEFLIQFLT KIPTLDEALK LSIDFQIPLH PQYLYYWDQI
SSEEFLQILH PVKINENSIE YSIETKNILE KLGVPHKMNN TQIILEKEEA RIFYNLLFRH
EPEINDLSIP QIISKSSGII IKNKFSTSIG VRIGRPEKAA PRQMKPPTHV LFPINDKGGP
TRDLLKASRQ DNFFTNIFNR SCQGCNEPSI GIKCSKCGIK TTIVYRCGNC RDILDNPFCE
KCKRKASSHS HQAFPLKSKL LLAQEKMGLR AQEPFKGVKE LINQDRIAEP LEKGLVRQNF
GLTVFKDGTV RFDATNSPLT QFQPSWIGTS IEKLNELGYT HDIDGKPLTD PNQTVELRMQ
DVIIPNESGK YLVSICKYID TILEKFYEKS IFYNVKNTDD LIGHLIIGLA PHTSVGIVGR
IIGYTETHVC FATPNWHSAK RRDADGDADS IMLLMDSLLN FSRQFLSDRI GGLMDAPLLI
QPLVLPHESQ PQAHNLEVVK FLPLEFFKST IQQNKAPDVA CVEIIKSRLE TERQFFGYYF
THSTTSLTTS KSRSAYSTLG SMLDKFDMQI KNAELIDAVN TSEIVSNVIS THLVPDIMGN
LRAYARQNFR CTGCGKSYRR IPLIQTCICG HNLIPTITRG SVEKYLKLAK RLVDKYDVGA
YQRGRIHALS DEIDLVFGKN KGDQSLLSDY T
//
