位置:首页 > 蛋白库 > DP2L_METVS
DP2L_METVS
ID   DP2L_METVS              Reviewed;        1131 AA.
AC   A6URH2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=DNA polymerase II large subunit {ECO:0000255|HAMAP-Rule:MF_00324};
DE            Short=Pol II {ECO:0000255|HAMAP-Rule:MF_00324};
DE            EC=2.7.7.7 {ECO:0000255|HAMAP-Rule:MF_00324};
DE   AltName: Full=Exodeoxyribonuclease large subunit {ECO:0000255|HAMAP-Rule:MF_00324};
DE            EC=3.1.11.1 {ECO:0000255|HAMAP-Rule:MF_00324};
GN   Name=polC {ECO:0000255|HAMAP-Rule:MF_00324}; OrderedLocusNames=Mevan_1196;
OS   Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148
OS   / SB).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=406327;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Anderson I.,
RA   Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of Methanococcus vannielii SB.";
RL   Submitted (JUN-2007) 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 (By similarity). {ECO:0000250}.
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; Evidence={ECO:0000255|HAMAP-
CC         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:0000255|HAMAP-
CC         Rule:MF_00324};
CC   -!- SUBUNIT: Heterodimer of a large subunit and a small subunit.
CC       {ECO:0000255|HAMAP-Rule:MF_00324}.
CC   -!- SIMILARITY: Belongs to the archaeal DNA polymerase II family.
CC       {ECO:0000255|HAMAP-Rule:MF_00324}.
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; CP000742; ABR55094.1; -; Genomic_DNA.
DR   RefSeq; WP_012066009.1; NC_009634.1.
DR   AlphaFoldDB; A6URH2; -.
DR   SMR; A6URH2; -.
DR   STRING; 406327.Mevan_1196; -.
DR   EnsemblBacteria; ABR55094; ABR55094; Mevan_1196.
DR   GeneID; 5325524; -.
DR   KEGG; mvn:Mevan_1196; -.
DR   eggNOG; arCOG04447; Archaea.
DR   HOGENOM; CLU_001154_0_0_2; -.
DR   OMA; KRRNCDG; -.
DR   OrthoDB; 559at2157; -.
DR   Proteomes; UP000001107; Chromosome.
DR   GO; GO:0008408; F:3'-5' exonuclease activity; IEA:UniProtKB-UniRule.
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:0008852; F:exodeoxyribonuclease I activity; IEA:UniProtKB-EC.
DR   GO; GO:0000738; P:DNA catabolic process, exonucleolytic; 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   PANTHER; PTHR42210; PTHR42210; 2.
DR   Pfam; PF03833; PolC_DP2; 1.
DR   PIRSF; PIRSF016275; PolC_DP2; 1.
DR   TIGRFAMs; TIGR00354; polC; 1.
PE   3: Inferred from homology;
KW   DNA replication; DNA-binding; DNA-directed DNA polymerase; Exonuclease;
KW   Hydrolase; Multifunctional enzyme; Nuclease; Nucleotidyltransferase;
KW   Transferase.
FT   CHAIN           1..1131
FT                   /note="DNA polymerase II large subunit"
FT                   /id="PRO_1000019391"
SQ   SEQUENCE   1131 AA;  128607 MW;  82E2CC6A4100753E CRC64;
     MLHVSASKNM TEYFKSILND VNNLYFIAEE CRKLGYDVVD KVEIPLAKDM ADRVEGIVGP
     PKVSERIREL VMELGKEPAA LEIAKEIVEG RFGEFGKEEG AEQAVRTALA VITEGIVAAP
     LEGIAHVKIK KNHDGTEYLA IYFAGPIRSA GGTAQALAVL VGDYVRKNMN LDKFKPTDDE
     VERYGEEIDL YQSEVTTFQY QPKIEEIRTA VRNISVEITG EATDDVEVSG HRDLERVETN
     QIRGGALLAL VEGVLLKAPK ILRHVDKLEI EGWNWLKELK NKKEEINEDI KDEKEDFNYE
     EEEDLSQYDD CEIEEVTKFI GEVIAGRPVF AHPSKKGGFR LRYGRSRNTG FATDGFHPAI
     MYLVDDFMAV GTQLKTERPG KATCVVPVDS IDPPIVKLNN HSVLKIDTVE KAIKYRKDVL
     EILFLGDILV NYGDFLENNH VMLPSSWCVE WYEKILKVNN IPYSTEFISN PSPKEAVKFA
     ITTKTPLHPV YTYHWHDISK ENIYSLRNWI LRGNFNKNSD KWEISYDLEN PEDISNKRFL
     ELIGCCHEVV DGKIFILEYY PLLYSLGYDY ENSFDSVENL EEKVSNAKNN MHLINLLSHF
     EIRRNTYIYV GARMGRPEKA ASRKMKPPVN GLFPIGNAGA LVRLINKAVE GGKTDEIEIS
     NVMCSCGKVS LYKKCPFCGK SVIPTGPTRI KLPIKDYWYN ALENLKINKP GDVKCIKGMT
     SKDKIIEPLE KAILRAVNDV YVFKDGTTRF DCTDVPVTHF KPCEINVSVN RLKELGYLRD
     INGNSLENDK QVLELKVQDV IVPESCMDYF LNVSKFIDDL LEKYYKKNRY YNSSNKEDLV
     GHLIIGMAPH TSAGMVGRIV GYSKANVGYA HPYFHASKRR NCDGDEDAFF LLLDAFLNFS
     KKFLPDKRGG QMDAPLVLTT ILDPKEVDGE VHNMDSMWEY PLEFYEKSLE MVTPKEIKKL
     METVEDRLGK DEQYEGIGYT HETLKIDEGP LICSYKTLGS MMDKTSAQLA VAKKIRATDE
     RDVAEKVIQS HFVPDLIGNL RAFSRQGVRC KCGAKYRRIP LKGVCRKCGS RLILTVSKGA
     VEKYMNVSQT MAEKYNVSDY IKQRLEIIRS GIDSLFTNDK RKQVKIEDFF K
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024