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DP2L_METBU
ID   DP2L_METBU              Reviewed;        1145 AA.
AC   Q12TF2;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 2.
DT   03-AUG-2022, entry version 74.
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=Mbur_2423;
OS   Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 /
OS   ACE-M).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanococcoides.
OX   NCBI_TaxID=259564;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6242 / NBRC 107633 / OCM 468 / ACE-M;
RX   PubMed=19404327; DOI=10.1038/ismej.2009.45;
RA   Allen M.A., Lauro F.M., Williams T.J., Burg D., Siddiqui K.S.,
RA   De Francisci D., Chong K.W., Pilak O., Chew H.H., De Maere M.Z., Ting L.,
RA   Katrib M., Ng C., Sowers K.R., Galperin M.Y., Anderson I.J., Ivanova N.,
RA   Dalin E., Martinez M., Lapidus A., Hauser L., Land M., Thomas T.,
RA   Cavicchioli R.;
RT   "The genome sequence of the psychrophilic archaeon, Methanococcoides
RT   burtonii: the role of genome evolution in cold adaptation.";
RL   ISME J. 3:1012-1035(2009).
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   -!- SEQUENCE CAUTION:
CC       Sequence=ABE53274.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000300; ABE53274.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_048063431.1; NC_007955.1.
DR   AlphaFoldDB; Q12TF2; -.
DR   SMR; Q12TF2; -.
DR   STRING; 259564.Mbur_2423; -.
DR   EnsemblBacteria; ABE53274; ABE53274; Mbur_2423.
DR   GeneID; 3999013; -.
DR   KEGG; mbu:Mbur_2423; -.
DR   HOGENOM; CLU_001154_0_0_2; -.
DR   OrthoDB; 559at2157; -.
DR   Proteomes; UP000001979; 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..1145
FT                   /note="DNA polymerase II large subunit"
FT                   /id="PRO_0000294685"
FT   REGION          284..303
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        286..303
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1145 AA;  127582 MW;  2E4E696ABF9D18E4 CRC64;
     MAEIVASDEM NEYFNTLEGT LKKEIDIVND ARSRGKDPKP HVEIPLAKDL ADRVENLIGV
     KGVAELIRKL EETMSREEAA LALGREVAQG KVGEFDSKSE AIEAAIRVSV AMLTEGVVAA
     PIEGIDRASI GKNDDGSEYV SIFYAGPIRS AGGTAQALSV LVGDYVRRGV GIDRYKPRKE
     EVERYIEEIM LYKRVASLQY TPSEEEIRLI VENCPICIDG EPTEAEEVEG HRNLERIDTN
     RVRGGMALVL AEGLALKAPK IQKHVKNLKI DGWEWLEQLI SGVKSSSESD EDEETDGKPK
     IKPKDKYMRD LIAGRPVFSH PSRPGGFRLR YGRSRNTSFA AAGISPAGMI VMDDFIAPGT
     QLKVERPGKA AGMAPVDSIE GPTVRLNNGD VIRIDTIDEA YALRSEVEEI IDIGEILINY
     GDFLENNHPL APSPYCFEWW IQEYRKAAPD TETNEAELKE PTQEVALDLC KELNIPLHPK
     FTYLWHDIDN SQYTALADLI SKDGLLEADG SFLKLPLQRT IDTGMKKVLE DLLVQHKIQG
     QALTIEEPLP LIHSLGLDEE LSKGWDSLGH EELLENINEI AGFVVRPRAP TRIGARMGRP
     EKSDKRKMTP APHALFPIAE AGGNTRSLEK AANFKVNTNS KAGTIPVEIG NRICPACGVE
     GFEFRCECGE YTLPKLFCPR CGISVNKEKC PKCNSKTTCT SMRKIDFKSI YQKAFESIGE
     RDHLDSFKGV KKMMSKHMTP EPLEKGILRA KHGLFTFKDG TVRYDMSDIP LTHIRPAEIG
     VSCERMIELG YLKDIYGKPL IDSEQVLCLK VQDLVISYDA ADYILRITQY IDDLLVKYYK
     VAPYYNAKHI DDIVGVLLMG LAPHTSAGVL GRLIGFTTAS VGYAHPYFHA AKRRNCDGDE
     DCVMLLMDGL LNFSRDYLPD KRGGQMDAPL VLTTRLDPSE VDKEAHNIDM CASYPLEFYE
     ATQNIANPKD FEGTMDLVSG RLGTTLQYEE FMFTHDTSNI AAGPLKSAYK TLGTMVEKMD
     AQLELAKKIR AVDAPDVAER VLTSHFLPDM FGNLRAFSRQ RTRCVKCAAK FRRPPLTGSC
     PKCGGRVILT VHEGAVKKYL QVSIKIAEEY NVSSYTKQRI ELIGYDMKSL FENDKSKQMG
     LSDFM
 
 
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