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Database: UniProt
Entry: A0A2I9CS21_9DEIO
LinkDB: A0A2I9CS21_9DEIO
Original site: A0A2I9CS21_9DEIO 
ID   A0A2I9CS21_9DEIO        Unreviewed;      1003 AA.
AC   A0A2I9CS21;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=UvrABC system protein A {ECO:0000256|ARBA:ARBA00039316, ECO:0000256|HAMAP-Rule:MF_00205};
DE            Short=UvrA protein {ECO:0000256|HAMAP-Rule:MF_00205};
DE   AltName: Full=Excinuclease ABC subunit A {ECO:0000256|ARBA:ARBA00042156, ECO:0000256|HAMAP-Rule:MF_00205};
GN   Name=uvrA {ECO:0000256|HAMAP-Rule:MF_00205};
GN   ORFNames=DAERI_010551 {ECO:0000313|EMBL:GBF04379.1};
OS   Deinococcus aerius.
OC   Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=200253 {ECO:0000313|EMBL:GBF04379.1, ECO:0000313|Proteomes:UP000236569};
RN   [1] {ECO:0000313|Proteomes:UP000236569}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TR0125 {ECO:0000313|Proteomes:UP000236569};
RA   Satoh K., Arai H., Sanzen T., Kawaguchi Y., Hayashi H., Yokobori S.,
RA   Yamagishi A., Oono Y., Narumi I.;
RT   "Draft Genome Sequence of the Radioresistant Bacterium Deinococcus aerius
RT   TR0125, Isolated from the Higher Atmosphere above Japan.";
RL   Submitted (JAN-2018) 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}.
CC   -!- SUBUNIT: Forms a heterotetramer with UvrB during the search for
CC       lesions. {ECO:0000256|HAMAP-Rule:MF_00205}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_00205}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. UvrA family.
CC       {ECO:0000256|ARBA:ARBA00038000, ECO:0000256|HAMAP-Rule:MF_00205}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GBF04379.1}.
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DR   EMBL; BFAG01000001; GBF04379.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2I9CS21; -.
DR   OrthoDB; 9809851at2; -.
DR   Proteomes; UP000236569; Unassembled WGS sequence.
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:ATP hydrolysis 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   CDD; cd03270; ABC_UvrA_I; 1.
DR   CDD; cd03271; ABC_UvrA_II; 1.
DR   Gene3D; 3.30.190.20; -; 1.
DR   Gene3D; 1.10.8.280; ABC transporter ATPase domain-like; 1.
DR   Gene3D; 1.20.1580.10; ABC transporter ATPase like domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR   HAMAP; MF_00205; UvrA; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR004602; UvrA.
DR   InterPro; IPR041552; UvrA_DNA-bd.
DR   InterPro; IPR041102; UvrA_inter.
DR   NCBIfam; TIGR00630; uvra; 1.
DR   PANTHER; PTHR43152; UVRABC SYSTEM PROTEIN A; 1.
DR   PANTHER; PTHR43152:SF3; UVRABC SYSTEM PROTEIN A; 1.
DR   Pfam; PF17755; UvrA_DNA-bind; 1.
DR   Pfam; PF17760; UvrA_inter; 1.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00205};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00205};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW   Rule:MF_00205};
KW   DNA excision {ECO:0000256|ARBA:ARBA00022769, ECO:0000256|HAMAP-
KW   Rule:MF_00205};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW   Rule:MF_00205};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_00205};
KW   Excision nuclease {ECO:0000256|ARBA:ARBA00022881, ECO:0000256|HAMAP-
KW   Rule:MF_00205};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00205};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00205};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|HAMAP-Rule:MF_00205};
KW   SOS response {ECO:0000256|HAMAP-Rule:MF_00205};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00205};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|HAMAP-
KW   Rule:MF_00205}.
FT   DOMAIN          634..971
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   ZN_FING         255..282
FT                   /note="C4-type"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
FT   ZN_FING         774..800
FT                   /note="C4-type"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
FT   BINDING         33..40
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
FT   BINDING         675..682
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
SQ   SEQUENCE   1003 AA;  110573 MW;  B02EB9E00C4A2273 CRC64;
     MQNQNLVVRG AREHNLKNVT VELPRDKFVV ITGVSGSGKS TLAFDTIYAE GQRRYVESLS
     AYARQFLGLM EKPDVESIEG LSPAISIDQK TTSHNPRSTV GTVTEIHDYL RLLYARIGTP
     YCPICGRKIE KQSPSEITDR LLSQFADARA ILLAPVVRGR KGEYRKLLGD LRREGFARVR
     VDGTLYELEE AEKLKLEKFE KHDVDVVVDR VTLRESDRSR IAESVELGLR RGEGLLRVLM
     PDTGAEELYS EKFACPEHGS VLEELEPRSF SFNSPYGACG DCAGLGHKNE FAPELVVDEK
     LSIAEGAILP WSKKGTGGGV YYWDKLKALA EHMEFDLKTP WRDLPEKAKK AILEGPGEPF
     EVVYRRGGKE TMRFMTEFEG VIPNLERRYA DTESEFMREK LEELMELRPC PTCGGTRYKP
     EILAVRVGGL NISQASGMSV LESDAFFRGL QDGTLNHEAI EPHLEGHLGG TAKAAPPRRY
     EYALNEFGAA VGAPILKAIR TRLKFLVDVG LDYLSLDRTA NTLSGGEAQR IRLATQVGSG
     LTGVLYVLDE PSIGLHPKDN GRLIGTLKNL RDLGNTLIVV EHDEDTMLEA DYLVDMGPGA
     GVHGGEIVAV GTPEEVRENP DSLTGKYLRG DLKIEVPATR RRGNGKKLKV FGAREHNLRD
     VDIEIPLGTM TVVTGPSGSG KSTLIHDIVH ATLARELNGA KTNPGRYDRI EGMEYLDKVI
     EIDQSPIGRT PRSNPATYTG VFTEIRDLFT RTPEARRRGY QAGRFSFNVK GGRCEHCKGD
     GVMKIEMNFL PDIYVPCEVC KGARYNRETL EVKYNGKTIS EVLDLTVEDA RTFFENIPGI
     EKKMSLLCDV GLGYMRIGQP STTLSGGEAQ RIKLASELSK RATGKTIYIL DEPTTGLHFE
     DVRKLMEVLN RLAEGGNTLV VIEHNLDVMK CADHIIDLGP EGGVRGGTVV ATGTPEQLAA
     HPTSYTGEYL RRVPGIVPAG AEDREMVGAA ATKKTRTKKA VGA
//
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