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UVRC_BURTA
ID   UVRC_BURTA              Reviewed;         740 AA.
AC   Q2SXS5;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 2.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=UvrABC system protein C {ECO:0000255|HAMAP-Rule:MF_00203};
DE            Short=Protein UvrC {ECO:0000255|HAMAP-Rule:MF_00203};
DE   AltName: Full=Excinuclease ABC subunit C {ECO:0000255|HAMAP-Rule:MF_00203};
GN   Name=uvrC {ECO:0000255|HAMAP-Rule:MF_00203}; OrderedLocusNames=BTH_I1739;
OS   Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 /
OS   E264).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=271848;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264;
RX   PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA   Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA   DeShazer D.;
RT   "Bacterial genome adaptation to niches: divergence of the potential
RT   virulence genes in three Burkholderia species of different survival
RT   strategies.";
RL   BMC Genomics 6:174-174(2005).
CC   -!- FUNCTION: The UvrABC repair system catalyzes the recognition and
CC       processing of DNA lesions. UvrC both incises the 5' and 3' sides of the
CC       lesion. The N-terminal half is responsible for the 3' incision and the
CC       C-terminal half is responsible for the 5' incision. {ECO:0000255|HAMAP-
CC       Rule:MF_00203}.
CC   -!- SUBUNIT: Interacts with UvrB in an incision complex.
CC       {ECO:0000255|HAMAP-Rule:MF_00203}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00203}.
CC   -!- SIMILARITY: Belongs to the UvrC family. {ECO:0000255|HAMAP-
CC       Rule:MF_00203}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABC38611.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000086; ABC38611.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_009890027.1; NZ_CP008785.1.
DR   AlphaFoldDB; Q2SXS5; -.
DR   SMR; Q2SXS5; -.
DR   PRIDE; Q2SXS5; -.
DR   EnsemblBacteria; ABC38611; ABC38611; BTH_I1739.
DR   KEGG; bte:BTH_I1739; -.
DR   HOGENOM; CLU_014841_3_0_4; -.
DR   Proteomes; UP000001930; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0009380; C:excinuclease repair complex; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009381; F:excinuclease ABC activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006289; P:nucleotide-excision repair; IEA:UniProtKB-UniRule.
DR   GO; GO:0009432; P:SOS response; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.420.340; -; 1.
DR   Gene3D; 3.40.1440.10; -; 1.
DR   HAMAP; MF_00203; UvrC; 1.
DR   InterPro; IPR000305; GIY-YIG_endonuc.
DR   InterPro; IPR035901; GIY-YIG_endonuc_sf.
DR   InterPro; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif.
DR   InterPro; IPR010994; RuvA_2-like.
DR   InterPro; IPR001943; UVR_dom.
DR   InterPro; IPR036876; UVR_dom_sf.
DR   InterPro; IPR004791; UvrC.
DR   InterPro; IPR001162; UvrC_RNase_H_dom.
DR   InterPro; IPR038476; UvrC_RNase_H_dom_sf.
DR   Pfam; PF01541; GIY-YIG; 1.
DR   Pfam; PF02151; UVR; 1.
DR   Pfam; PF08459; UvrC_HhH_N; 1.
DR   SMART; SM00465; GIYc; 1.
DR   SMART; SM00278; HhH1; 2.
DR   SUPFAM; SSF46600; SSF46600; 1.
DR   SUPFAM; SSF47781; SSF47781; 1.
DR   SUPFAM; SSF82771; SSF82771; 1.
DR   TIGRFAMs; TIGR00194; uvrC; 1.
DR   PROSITE; PS50164; GIY_YIG; 1.
DR   PROSITE; PS50151; UVR; 1.
DR   PROSITE; PS50165; UVRC; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; DNA damage; DNA excision; DNA repair; Excision nuclease;
KW   SOS response.
FT   CHAIN           1..740
FT                   /note="UvrABC system protein C"
FT                   /id="PRO_0000264880"
FT   DOMAIN          22..100
FT                   /note="GIY-YIG"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00203"
FT   DOMAIN          209..244
FT                   /note="UVR"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00203"
FT   REGION          308..398
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        349..381
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   740 AA;  80220 MW;  3AF220D11ACA06A3 CRC64;
     MTSPDASESR FEPKPILAQL PHLPGVYRYY DAQEAVLYVG KARDLKKRVS SYFTKTQLSP
     RIAMMVTRIA RIETTVTRSE AEALLLENNL IKALAPRYNI LFRDDKSYPY LKLTGHRFPR
     MAYYRGAVDK KNQYFGPFPS AWAVRESIQI LQRVFQLRTC EDSVFSNRTR PCLLHQIGRC
     SAPCVGAIGE EDYARDVDNA SRFLLGRQGE VMGELERKMH AFAAELKFEQ AAAVRNQMSS
     LAKVLHQQAI DVGGDSDVDI LAVVAQGGRV CVNLAMVRGG RHLGDKAYFP THVETALALA
     GGVDAHAGEG AGDDARDAAE SPAQARLAGD AAANGVANAA AAARADDRSA QPTRARAEGD
     VERSADASAG ARGEADAREA AAPSEPDSVT AASQDADADA APLETEVLEA FIAQHYLGNR
     VPPILVVSHA IANRELIDLL VEQAGHKVAL VRQPQGQKRA WLAMAEQNAR LALARLLSEQ
     GSQQARARSL ADVLGYESDD LAQLRIECFD ISHTMGEATQ ASCVVYHHHK MQSSEYRRYN
     IAGITPGDDY AAMRQVLTRR YEKMVEEAAA EASADEAAGI DGNAVHAAAS AGRLPNIVLI
     DGGRGQVEIA RQVFSELGLD ISMLVGVAKG EGRKVGLETL IFADGRAPLE LGKESAALML
     VAQIRDEAHR FAITGMRAKR AKTRQTSRLE ELEGVGAKRR QRLLARFGGL RGVVAASVDE
     LASVEGISRA LAEQIYRQLH
 
 
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