ID W0JMD8_9EURY Unreviewed; 1201 AA.
AC W0JMD8;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 46.
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=HALLA_04915 {ECO:0000313|EMBL:AHF98314.1};
OS Halostagnicola larsenii XH-48.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Halostagnicola.
OX NCBI_TaxID=797299 {ECO:0000313|EMBL:AHF98314.1, ECO:0000313|Proteomes:UP000019024};
RN [1] {ECO:0000313|EMBL:AHF98314.1, ECO:0000313|Proteomes:UP000019024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XH-48 {ECO:0000313|EMBL:AHF98314.1,
RC ECO:0000313|Proteomes:UP000019024};
RG DOE Joint Genome Institute;
RA Anderson I., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL Submitted (JAN-2014) 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=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}.
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DR EMBL; CP007055; AHF98314.1; -; Genomic_DNA.
DR RefSeq; WP_049951506.1; NZ_CP007055.1.
DR AlphaFoldDB; W0JMD8; -.
DR STRING; 797299.HALLA_04915; -.
DR GeneID; 25143853; -.
DR KEGG; hlr:HALLA_04915; -.
DR PATRIC; fig|797299.3.peg.46; -.
DR eggNOG; arCOG04447; Archaea.
DR HOGENOM; CLU_001154_0_0_2; -.
DR OrthoDB; 7529at2157; -.
DR Proteomes; UP000019024; 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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000019024};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00324}.
FT DOMAIN 7..953
FT /note="DNA polymerase II large subunit DP2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03833"
FT REGION 285..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 599..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..315
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..614
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1201 AA; 132995 MW; DB47E24C7E4FAC11 CRC64;
MREVDQRYFS RLESQLDEAF DVAETAKERG ADPEPEVEIP VAKDMADRVE NILGIDGVAE
RVRELEGQMS REEAALALAE DFAEGNVGDY ETKAGKIEGA VRTAVALLTE GVVAAPIEGI
DKVELLSNDD GTEFVNVYYA GPIRSAGGTA QALSVLVGDY TRALVGIDQY NARSEEIERY
AEEISLYDKE TGLQYSPKDP ETKFIAKHLP IMLDGEATGD EEVSGFRDLE RVDTNSARGG
MCLVLAEGIA LKAPKIQRYT SQLEEIDWPW LQDLIDGNYY ENDDEAAADE SKAADDGDDD
DEADAEAAAE EDDAPPEETG PVRPAPSKKF LRDLIAGRPV FSHPSAKGGF RLRYGRSRNH
GFATGGVHPA TMHLVDDFLA TGTQIKTERP GKAHGVVPVD SIEGPTVKLA NGDVRRIDDP
EEALEIRNGV EEILDTGEYL INYGEFVENN HPLAPASYVF EWWIQDMDEA GADAQALLDD
PRIDAEHPPA EDALEWAREY DAPLHPDYTY LWHDLAVDDF CALADAVANA HIENGGETLV
LERSETVRDA LETIIVEHRQ REGRLEVDDW VPLARTLGVV RDEDGELTRT WTDDDLSERA
RTWGDSDGAD SGDDKRNSSG GANAIKAVNE VAPFTVRERA PTRIGNRMGR PEKSESRDLS
PAVHTLFPIG EAGGAQRDIA KAGKHADTMS DTPGVVEIQI GRHRCGECDT ETFKNRCPDC
GARTEPDYRC PSCDSAIEPD EAGRVECDRC DTEATCVESR EIDLNKEYRD ALETVGEREN
AFDILKGVKG LTSADKIPEP MEKGILRAKH DVSSFKDGTV RYDMTDLPVT SVRASELDID
VGQLQALGYE EDIHGEPLVH EDQLVELKVQ DIVLSDGAAE HMLKTADFID DLLEQYYGLE
PFYELGEREE LVGELVFGMA PHTSAATVGR VIGFTSAAVG YAHPYFHAAK RRNCDGDEDC
VMLLMDGLLN FSMSFLPDQR GGKMDAPLVM SSRIDPSEID DEAHNIDIVS RYPREFYEAT
LEMADPGEVD VQIAEETLGT DEEYTGFEHT HDTSDIAMGP DLSAYKTLGS MMDKMDAQLE
LSRKLKAVDE TDVAERVIEY HFLPDLIGNL RAFSRQETRC LDCGEKFRRM PLTETCRECG
GRVNLTVHQG SVNKYMQTAI EVAEEYDCRP YTKQRLEVLE KSLESVFEND KNKQSGIEDF
M
//
