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Database: UniProt
Entry: A0A256ID50_9EURY
LinkDB: A0A256ID50_9EURY
Original site: A0A256ID50_9EURY 
ID   A0A256ID50_9EURY        Unreviewed;      1362 AA.
AC   A0A256ID50;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
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=DJ70_13800 {ECO:0000313|EMBL:OYR54458.1};
OS   Halorubrum halodurans.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Halorubraceae; Halorubrum.
OX   NCBI_TaxID=1383851 {ECO:0000313|EMBL:OYR54458.1, ECO:0000313|Proteomes:UP000216308};
RN   [1] {ECO:0000313|EMBL:OYR54458.1, ECO:0000313|Proteomes:UP000216308}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Cb34 {ECO:0000313|EMBL:OYR54458.1,
RC   ECO:0000313|Proteomes:UP000216308};
RX   PubMed=24782836; DOI=10.3389/fmicb.2014.00140;
RA   Fullmer M.S., Soucy S.M., Swithers K.S., Makkay A.M., Wheeler R.,
RA   Ventosa A., Gogarten J.P., Papke R.T.;
RT   "Population and genomic analysis of the genus Halorubrum.";
RL   Front. Microbiol. 5:140-140(2014).
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:OYR54458.1}.
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DR   EMBL; NHPJ01000121; OYR54458.1; -; Genomic_DNA.
DR   OrthoDB; 7529at2157; -.
DR   Proteomes; UP000216308; 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   GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR   CDD; cd00081; Hint; 1.
DR   CDD; cd00350; rubredoxin_like; 1.
DR   Gene3D; 2.170.16.10; Hedgehog/Intein (Hint) domain; 1.
DR   HAMAP; MF_00324; DNApol_II_L_arch; 1.
DR   InterPro; IPR003587; Hint_dom_N.
DR   InterPro; IPR036844; Hint_dom_sf.
DR   InterPro; IPR006141; Intein_N.
DR   InterPro; IPR004475; PolC_DP2.
DR   InterPro; IPR016033; PolC_DP2_N.
DR   NCBIfam; TIGR01445; intein_Nterm; 1.
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; PF14890; Intein_splicing; 1.
DR   Pfam; PF03833; PolC_DP2; 1.
DR   PIRSF; PIRSF016275; PolC_DP2; 2.
DR   SMART; SM00306; HintN; 1.
DR   SUPFAM; SSF51294; Hedgehog/intein (Hint) domain; 1.
DR   PROSITE; PS50817; INTEIN_N_TER; 1.
PE   3: Inferred from homology;
KW   Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813};
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}; Protein splicing {ECO:0000256|ARBA:ARBA00023000};
KW   Reference proteome {ECO:0000313|Proteomes:UP000216308};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00324}.
FT   DOMAIN          933..1055
FT                   /note="Hint"
FT                   /evidence="ECO:0000259|SMART:SM00306"
FT   REGION          277..332
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1048..1072
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        287..314
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1362 AA;  150002 MW;  EF6F57C844EDF54F CRC64;
     MRADDERYFA RLEERLDEAF EVAGTAKAQG KDPKPEIEIP VARDMADRVE NILGIDGVAE
     RVRELEGEMS REEAALELVT DFVEGTVGDY DSRAGKIEGA VRTAVALLTE GVVAAPIEGI
     DRVELLENDD GTEFINVYYA GPIRSAGGTA QALSVLVADY ARALLGIDEY HARTEEVERY
     AEEIALYDRE TGLQYTPKDE EAKFIAENIP IMLDGEATGD EEVSGFRDLE RVDTNSARGG
     MCLVAAEGIA LKAPKIQRYT RDLEEVDWPW LQDLIDGTIG KDGGDGEEEG GGDDAGEGDG
     GDDGTTDGNA DEASGDDAAD PAGPPRPKPS RKFLRDLIAG RPVFTHPSEA GGFRLRYGRA
     RNHGFATAGV HPATMHLVDD FLATGTQIKT ERPGKAAGVV PVDSIEGPTV KLANGEVRRI
     DDPEEALAVR NGVEEILDLG EYLVNYGEFV ENNHPLAPAS YVYEWWVQEF AAAGADVQAL
     ADDPNVDLER PEPGAALEWA EAYDCPLHPA YTYLWHDVSV ADVEALAEAV AGGEVVEGVL
     AIEHTERVAR ALETLLVEHA ATPDALRIPT WRPLARSLGV DDGLRKEWTP EDLPREAREW
     DGGDDAVKAV NAVAPFAVRE RAPVRIGNRM GRPEKSESRD LSPAVHTLFP INEAGGPQRD
     VAEAARTMDD RGRRGHLELE VADRACPDCG THTYRSACPD CGTHTEPHYE CGDCGTVCEP
     DEAGRVECPR CEWEVTAATR QEVDLNDAYR SALESVGERE SAFEILKGVQ GLTSTNKTPE
     PIEKGILRAK NGVTSFKDGT VRYDMTDLPV TSVRPEELDV TADHFRELGY ETDIDGDPLR
     HDDQLVELKV QDVVLSDGAA EHMLRTADFV DDLLEQFYDL PRFYEVNERD DLVGELVFGM
     APHTSAATVG RVIGFTSAAV GYAHPYFHAA KRRNCFHPAT TIAYLEEGER REISIEAFVE
     SRLGDPETDD FGTLVQELDG DVRVPSIDER GNGTTRSVTA VSKHPSQDHF VRIRTRSGRT
     IRVTPDHTML RVADGEIRRT PARELAVGDR VPAAHSGERE QSTDASAASA DGGVDVDEIV
     EAELVESGVE YTYNITVSDT HRLSANELWV EQCDGDEDCV MLLMDGLLNF SKTFLPNQRG
     GKMDAPLVMS SRIDPSEIDD EAHNMDIVRR YPLEFYEATR EMADPEVVED RIKLGEDTLG
     TDDEYRGFDH THDTTDIAMG PDLSAYKTLG DMMEKMNAQL ELARKLRAVD ETDVAERVIE
     YHFLPDIIGN LRAFSRQETR CLDCGEKYRR MPLSGDCREC GGRVNLTVHE GSVSKYVDTA
     IEVAERFDCR PYTKQRLYVL EDALESIFED DTNKQSGIAD FM
//
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