(data stored in SCRATCH zone)

SWISSPROT: A0A0F6BIH6_GEOS0

ID   A0A0F6BIH6_GEOS0        Unreviewed;       954 AA.
AC   A0A0F6BIH6;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   11-DEC-2019, entry version 31.
DE   RecName: Full=UvrABC system protein A {ECO:0000256|HAMAP-Rule:MF_00205, ECO:0000256|SAAS:SAAS00088996};
DE            Short=UvrA protein {ECO:0000256|HAMAP-Rule:MF_00205};
DE   AltName: Full=Excinuclease ABC subunit A {ECO:0000256|HAMAP-Rule:MF_00205};
GN   Name=uvrA {ECO:0000256|HAMAP-Rule:MF_00205};
GN   OrderedLocusNames=GY4MC1_0385 {ECO:0000313|EMBL:ADP73227.1};
OS   Geobacillus sp. (strain Y4.1MC1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   unclassified Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP73227.1};
RN   [1] {ECO:0000313|EMBL:ADP73227.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP73227.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G., Brumm P.,
RA   Mead D., Woyke T.;
RT   "Complete sequence of chromosome of Geobacillus sp. Y4.1MC1.";
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The UvrABC repair system catalyzes the recognition and
CC       processing of DNA lesions. UvrA is an ATPase and a DNA-binding protein.
CC       A damage recognition complex composed of 2 UvrA and 2 UvrB subunits
CC       scans DNA for abnormalities. When the presence of a lesion has been
CC       verified by UvrB, the UvrA molecules dissociate. {ECO:0000256|HAMAP-
CC       Rule:MF_00205, ECO:0000256|SAAS:SAAS00571360}.
CC   -!- SUBUNIT: Forms a heterotetramer with UvrB during the search for
CC       lesions. {ECO:0000256|HAMAP-Rule:MF_00205,
CC       ECO:0000256|SAAS:SAAS00571359}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00205,
CC       ECO:0000256|SAAS:SAAS00089096}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. UvrA family.
CC       {ECO:0000256|HAMAP-Rule:MF_00205, ECO:0000256|SAAS:SAAS00571366}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00434}.
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DR   EMBL; CP002293; ADP73227.1; -; Genomic_DNA.
DR   RefSeq; WP_013399996.1; NC_014650.1.
DR   EnsemblBacteria; ADP73227; ADP73227; GY4MC1_0385.
DR   KEGG; gmc:GY4MC1_0385; -.
DR   KO; K03701; -.
DR   OMA; GAIKGWD; -.
DR   OrthoDB; 152379at2; -.
DR   BioCyc; GSP581103:G1GOQ-430-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0009380; C:excinuclease repair complex; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATPase activity; 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:0008270; F:zinc ion binding; 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   HAMAP; MF_00205; UvrA; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003439; ABC_transporter-like.
DR   InterPro; IPR017871; ABC_transporter_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR004602; UvrA.
DR   InterPro; IPR041552; UvrA_DNA-bd.
DR   InterPro; IPR041102; UvrA_inter.
DR   Pfam; PF00005; ABC_tran; 1.
DR   Pfam; PF17755; UvrA_DNA-bind; 1.
DR   Pfam; PF17760; UvrA_inter; 1.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   TIGRFAMs; TIGR00630; uvra; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   3: Inferred from homology;
DR   PRODOM; A0A0F6BIH6.
DR   SWISS-2DPAGE; A0A0F6BIH6.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00205, ECO:0000256|PROSITE-
KW   ProRule:PRU00434, ECO:0000256|SAAS:SAAS00461349};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00205, ECO:0000256|SAAS:SAAS00461486};
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_00205,
KW   ECO:0000256|SAAS:SAAS00461370};
KW   DNA excision {ECO:0000256|HAMAP-Rule:MF_00205,
KW   ECO:0000256|SAAS:SAAS00461384};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_00205,
KW   ECO:0000256|SAAS:SAAS00089139};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00205,
KW   ECO:0000256|SAAS:SAAS00461351};
KW   Excision nuclease {ECO:0000256|HAMAP-Rule:MF_00205,
KW   ECO:0000256|SAAS:SAAS00461435};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00205,
KW   ECO:0000256|SAAS:SAAS00461425};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00205, ECO:0000256|PROSITE-
KW   ProRule:PRU00434, ECO:0000256|SAAS:SAAS00461357};
KW   Repeat {ECO:0000256|HAMAP-Rule:MF_00205, ECO:0000256|SAAS:SAAS00461462};
KW   SOS response {ECO:0000256|HAMAP-Rule:MF_00205};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00205, ECO:0000256|SAAS:SAAS00461396};
KW   Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00205,
KW   ECO:0000256|SAAS:SAAS00461452}.
FT   DOMAIN          315..593
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   DOMAIN          604..935
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   NP_BIND         33..40
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
FT   ZN_FING         252..279
FT                   /note="C4-type"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
FT   NP_BIND         639..646
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00205,
FT                   ECO:0000256|PROSITE-ProRule:PRU00434"
FT   ZN_FING         738..764
FT                   /note="C4-type"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
SQ   SEQUENCE   954 AA;  106043 MW;  653997970B7CE910 CRC64;
     MATDKIIVKG ARAHNLKNID VEIPRDKLVV LTGLSGSGKS SLAFDTIYAE GQRRYVESLS
     AYARQFLGQM DKPDVDAIEG LSPAISIDQK TTSRNPRSTV GTVTEIYDYL RLLFARIGRP
     VCPEHGIEIT SQTIEQMVDR LLSYPERTKM QILAPIVSGR KGTHAKTLED IRKQGYVRVR
     VDGEMRELTE TIELEKNKKH SIEVVVDRII IKDGIATRLA DSLETALKLA DGKVLIDVIG
     QEELLFSEKH ACPYCGFSIG ELEPRLFSFN SPYGACPDCD GLGATLEVDP DLVIPNNELS
     LREHAIAPWE PQSSQYYPQL LEAVCNHYGI DMDVPVKDLP KEQLDKILYG SGGEKIYFRY
     QSDFGQIREQ YIVFEGVIPN VERRYRETSS DYVREQMEKY MAQQPCPTCK GNRLKKESLA
     VLVGGKHIGE VTALSVTEAL AFFENLQLSE KEQKIAHLIL REIRERLGFL KNVGLDYLTL
     NRSAGTLSGG EAQRIRLATQ IGSRLTGVLY VLDEPSIGLH QRDNDRLIAT LKSMRDIGNT
     LIVVEHDEDT MLAADYLIDI GPGAGIHGGR VVAAGTPQEV MNNPDSLTGQ YLSGKKFIPI
     PSERRKPDGR WIEVVGAKEN NLKNVSVKIP LGTFVAVTGV SGSGKSTLVN EILYKALAQK
     LQRAKAKPGE HKTIKGLEHL DKVIDIDQSP IGRTPRSNPA TYTGVFDDIR EVFAATNEAK
     VRGYKKGRFS FNVKGGRCEA CHGDGIIKIE MHFLPDVYVP CEVCHGKRYN RETLEVTYKG
     KNIAEVLEMT VEDALEFFGN IPKIKRKLQT LYDVGLGYMK LGQPATTLSG GEAQRVKLAA
     ELHRRSTGRT LYILDEPTTG LHVDDIARLL KVLQRLVDNG DTVLVIEHNL DVIKTADYII
     DLGPEGGEQG GQIVATGTPE EVAEAKHSHT GRYLKPILER DRERMRALYE TAKA
//

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