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RECG_SYNY3
ID   RECG_SYNY3              Reviewed;         831 AA.
AC   Q55681;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=ATP-dependent DNA helicase RecG;
DE            EC=3.6.4.12;
GN   Name=recG; OrderedLocusNames=slr0020;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX   PubMed=8590279; DOI=10.1093/dnares/2.4.153;
RA   Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N.,
RA   Sugiura M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region
RT   from map positions 64% to 92% of the genome.";
RL   DNA Res. 2:153-166(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
CC   -!- FUNCTION: Critical role in recombination and DNA repair. Helps process
CC       Holliday junction intermediates to mature products by catalyzing branch
CC       migration. Has a DNA unwinding activity characteristic of a DNA
CC       helicase with a 3'- to 5'- polarity. Unwinds branched duplex DNA (Y-
CC       DNA) (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC   -!- SIMILARITY: Belongs to the helicase family. RecG subfamily.
CC       {ECO:0000305}.
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DR   EMBL; BA000022; BAA10207.1; -; Genomic_DNA.
DR   PIR; S76355; S76355.
DR   AlphaFoldDB; Q55681; -.
DR   SMR; Q55681; -.
DR   DIP; DIP-48810N; -.
DR   IntAct; Q55681; 5.
DR   STRING; 1148.1001580; -.
DR   PaxDb; Q55681; -.
DR   EnsemblBacteria; BAA10207; BAA10207; BAA10207.
DR   KEGG; syn:slr0020; -.
DR   eggNOG; COG1200; Bacteria.
DR   InParanoid; Q55681; -.
DR   OMA; DNGFQAC; -.
DR   PhylomeDB; Q55681; -.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003678; F:DNA helicase activity; IBA:GO_Central.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR   Gene3D; 2.40.50.140; -; 1.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR004609; ATP-dep_DNA_helicase_RecG.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR045562; RecG_dom3_C.
DR   InterPro; IPR033454; RecG_wedge.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF19833; RecG_C; 1.
DR   Pfam; PF17191; RecG_wedge; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   TIGRFAMs; TIGR00643; recG; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding; DNA damage; DNA recombination; DNA repair; DNA-binding;
KW   Helicase; Hydrolase; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..831
FT                   /note="ATP-dependent DNA helicase RecG"
FT                   /id="PRO_0000102159"
FT   DOMAIN          420..581
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          600..765
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   MOTIF           534..537
FT                   /note="DEQH box"
FT   BINDING         433..440
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   831 AA;  93659 MW;  F3641AB9105F4A4C CRC64;
     MQCSLVEVSV SVDWPRLQKA LTVEVERGFQ NLQGKQHRFG DFLCLSFGSP PPPGSSPGDR
     QKWREFAQRF AQYDQLEEAE RKSLVASTRR FLHQLRRSLE SPPRDSVPKK DLLAQVNRPQ
     VSEPRYPKSG QIELHTPLAT VVSQSQHQTK LLKNLGLATV EDLLFYFPRD YLDYAQQVTI
     AELTAGETVT IVGRVVNCTC FTSPKNQNLN ILQIQLRDQT GRIKLSRFYA GKRFAHRGWQ
     EKIKKLYPPQ AVVAASGLVK SSKFGLTLDN PEIEVLDRHS PSIDSFKVGR VLPVYPLTEG
     ITADFLRKLV LACQTAIAKL SDPLPQEIRE KYELIDLQTA IAQIHFPENT EKLSLARRRL
     VFDEFFYLQL GFLQRRYEQK QQQQSAIFTP HGELLEKFSD LLPFRLTQAQ QRVVNEILQD
     LNKPSPMNRL VQGDVGSGKT VVGVFAILAA LQGGYQAALM APTEVLAEQH YQKLVSWFNL
     LYLPVELLTG STKTAKRREI HAQLSTGQLP LLVGTHALIQ ETVNFQRLGL VVIDEQHRFG
     VQQRAKLLAK GNAPHVLSMT ATPIPRTLAL TLHGDLEVSQ IDELPPGRQP IHTSVITAKE
     RPQMYELIRR EVAQGRQVYI IFPAIEESEK LDIKAAVEEH KYLTEKIFPN FNIGLLHGRL
     KSAEKEAALT AFREKQTEII VSTTVIEVGV DVPNATVMVI ENAERFGLSQ LHQLRGRVGR
     GSHQSYCLLV TNSKSNDARQ RLGVMEQSQD GFFIAEMDLR LRGPGEFLGT KQSGLPDFAL
     ASLVEDQEVL LLAREAAETM MVEDPNLEAH PDLKIKLVQR YEKLLGGEIL T
 
 
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