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DP2L_METMP
ID   DP2L_METMP              Reviewed;        1131 AA.
AC   Q6M191;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=MMP0026;
OS   Methanococcus maripaludis (strain S2 / LL).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=267377;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S2 / LL;
RX   PubMed=15466049; DOI=10.1128/jb.186.20.6956-6969.2004;
RA   Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J.,
RA   Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M.,
RA   Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A.,
RA   Moore B.C., Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D.,
RA   Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W.,
RA   Olson M.V., Leigh J.A.;
RT   "Complete genome sequence of the genetically tractable hydrogenotrophic
RT   methanogen Methanococcus maripaludis.";
RL   J. Bacteriol. 186:6956-6969(2004).
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}.
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DR   EMBL; BX950229; CAF29582.1; -; Genomic_DNA.
DR   RefSeq; WP_011169970.1; NC_005791.1.
DR   AlphaFoldDB; Q6M191; -.
DR   SMR; Q6M191; -.
DR   STRING; 267377.MMP0026; -.
DR   EnsemblBacteria; CAF29582; CAF29582; MMP0026.
DR   GeneID; 2762226; -.
DR   KEGG; mmp:MMP0026; -.
DR   PATRIC; fig|267377.15.peg.26; -.
DR   eggNOG; arCOG04447; Archaea.
DR   HOGENOM; CLU_001154_0_0_2; -.
DR   OMA; KRRNCDG; -.
DR   OrthoDB; 559at2157; -.
DR   BioCyc; MMAR267377:MMP_RS00160-MON; -.
DR   Proteomes; UP000000590; 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; 1.
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   Reference proteome; Transferase.
FT   CHAIN           1..1131
FT                   /note="DNA polymerase II large subunit"
FT                   /id="PRO_0000294686"
SQ   SEQUENCE   1131 AA;  128381 MW;  3A000B7DAC5961DE CRC64;
     MLHVSASKGM TEYFKNILDD VSNLYNLAEE CRKNGYDVTD HVEIPLAKDM ADRVEGIVGP
     KNVAERIREL VSEFGKEPAA LEIAKEIVEG KFGEFGREVG AEQAVRTALA VITEGIVAAP
     LEGIAYVKIK KNSDNSEYLA IYFAGPIRSA GGTAQALAVL VGDYVRKNMG LDRFKPTEDE
     VERYGEEVDL YQSEVTTFQY QPKAEEIRVA VRNISVEITG EATDDVEVSG HRDLPRVETN
     QIRGGALLAL VEGVLLKAPK ILRHVDKLNI EGWNWLKELK SKKEEVIEEL EEENDEYNYE
     DEEDLSQYED YEVEAVTKFI GEVIAGRPVF SHPSKKGGFR LRYGRSRNTG FATDGFHPAI
     MYLVDDFMAV GTQLKTERPG KATCVVPVDS IEGPIVKLND GSVLKIDTVE KAKQYTDEVQ
     EILFLGDILV NYGDFLENNH TVLPSSWCTE WYEKILKSQN LEYTEEFIKN PGQKEAVNYA
     KITKTPLHPK YTYFWHDISK ENISTLRSWV IGGKYNPSND SWELNYDPED EEISNAKRYL
     ELIGCPHIVM EEKVEIFEYY PFLYSLGYDF DEKRDMIDNI DEKLQNTKNN MHFINTIAPF
     EIRRNAYIYV GARMGRPEKA AARKMKPPVN GLFPIGNAGA LVRLINKAVD EGKTDEIEIA
     NVKCSCGKVS LYRTCPFCGN SVEPTGPSRI KLPIKDYWYK TLENLKINKP GDVKCIKGMT
     SKDKIIEPLE KAILRAKNNI YVFKDGTTRF DCTDVPVTHF KPVEIHVPIE KLKSLGYLKD
     IHGNPLENED QVLELKVQDV IVPESCMDYF LNVSGFIDDL LEKYYKKDRF YNVNTREDLV
     GHLIIGMAPH TSAGMVGRII GYSNANVGYA HPYFHASKRR NCDGDEDAFF LLLDAFMNFS
     KRFLPDKRGG QMDAPLVLTT ILDPKEVDGE VHNMDSMWEY PLEFYEKSLE GIAPKEIKKM
     METIEDRLDK DSQYEGIGYT HETSKIDEGP PICAYKTLGS MMEKTSAQLA VAKKIRATDE
     RDVAEKVIQS HFVPDLIGNL RAFSRQGVRC KCGAKYRRMP LKGVCRKCGS RLILTVSKGA
     VEKYMNVSQT MAEKYDASDY IKQRLEIIKS GIDSLFVNDK RKQVKIEDFF K
 
 
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