ID F7XQJ7_METZD Unreviewed; 945 AA.
AC F7XQJ7;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=UvrABC system protein A {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|HAMAP-Rule:MF_00205};
GN Name=uvrA {ECO:0000256|HAMAP-Rule:MF_00205};
GN OrderedLocusNames=Mzhil_0632 {ECO:0000313|EMBL:AEH60499.1};
OS Methanosalsum zhilinae (strain DSM 4017 / NBRC 107636 / OCM 62 / WeN5)
OS (Methanohalophilus zhilinae).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosalsum.
OX NCBI_TaxID=679901 {ECO:0000313|EMBL:AEH60499.1, ECO:0000313|Proteomes:UP000006622};
RN [1] {ECO:0000313|Proteomes:UP000006622}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4017 / NBRC 107636 / OCM 62 / WeN5
RC {ECO:0000313|Proteomes:UP000006622};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K.,
RA Ovchinnikova G., Daligault H., Detter J.C., Han C., Tapia R., Larimer F.,
RA Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T.,
RA Wu D., Spring S., Schueler E., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Methanosalsum zhilinae DSM 4017.";
RL Submitted (JUL-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}.
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|HAMAP-Rule:MF_00205}.
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DR EMBL; CP002101; AEH60499.1; -; Genomic_DNA.
DR AlphaFoldDB; F7XQJ7; -.
DR STRING; 679901.Mzhil_0632; -.
DR KEGG; mzh:Mzhil_0632; -.
DR HOGENOM; CLU_001370_0_2_2; -.
DR Proteomes; UP000006622; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0009380; C:excinuclease repair complex; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0009381; F:excinuclease ABC activity; IEA:UniProtKB-UniRule.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
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; 1.10.8.280; ABC transporter ATPase domain-like; 1.
DR Gene3D; 1.20.1580.10; ABC transporter ATPase like domain; 2.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
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; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR009056; Cyt_c-like_dom.
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; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
DR PROSITE; PS51007; CYTC; 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}; Heme {ECO:0000256|PROSITE-ProRule:PRU00433};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PROSITE-ProRule:PRU00433};
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}; Reference proteome {ECO:0000313|Proteomes:UP000006622};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|HAMAP-Rule:MF_00205};
KW SOS response {ECO:0000256|ARBA:ARBA00023236, ECO:0000256|HAMAP-
KW 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 268..411
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT DOMAIN 341..601
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 606..942
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT ZN_FING 260..287
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
FT ZN_FING 745..771
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
FT BINDING 39..46
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
FT BINDING 646..653
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
SQ SEQUENCE 945 AA; 104735 MW; 08D2BE4D143FF5A0 CRC64;
MILVQIMSLN NIIIKGAKEH NLKNIDLNLP RDKLIVITGL SGSGKSSLAF DTIYAEGQRR
YVESLSAYAR QFLGLMEKPD VEYIEGLSPA ISIEQKTTSK NPRSTVGTVT EIYDYLRLLY
SRIGIRHCPD CGEMIEPQSI DQIVDNIKKI PEGTKIHILS PLVRERKGEY KKLISDILTE
GFSRVRIDGE VIPIEEALDV ELGRYQKHNI EIVVDRLVIK EGIDERLADS VETAIEKSGG
TIIVHLLDDK ELVFSEKLAC PACGTGFEDL EPAAFSFNSP QGACQTCHGL GTSMEFDPEL
IVPDDSLSLR DGAIEPWSSR DGYHMQSLES LAKHYDFSMD VPYRELSKKV QNTIMYGTKK
KIPFLHVGRK GGLWKHTGRF KGVIANLSKI YDKTESESTK EKLNKYISTK PCSTCNGARL
KPTSLAVTLD SLNIIDVTKL SVQDCLHFFE HLELKLTSRE FTIGRLILKE IKSRLGFLID
VGLDYLTLDR ASATLSGGEA QRIRLATQIG SSLMGVLYIL DEPSIGLHQR DNLRLINTLK
NLRDIGNTVL VVEHDEETIL NADHVVDMGP GAGIHGGYIV AEGTPQQVID DENSLTGKYL
KGEVSISVPE IRRTGNGTLT LEKAEENNLK NIDVSFPLST MICITGVSGS GKSTLISETL
NKVLAQKLHG SREKPGKYGN IRGIENIDKV ITIDQSPIGR TPRSNPATYT NLFTPIRELF
SQTQLARARG YKQGRFSFNV RGGRCEACSG DGIITIEMHF LPDVYVPCEV CHGKRYNRET
LEVTYKNKSI ADVLDMTVEE ALEFFEHIPK IERKLRTLFD VGLGYIKLGQ ASTTLSGGEA
QRVKLATELS KKSTGKTLYI LDEPTTGLHF DDVKKLLQVL HRLVDSGNTV IVIEHNLDVI
KTADWIIDLG PEGGEKGGEV IAKGTPETIA VSEGSYTGEF LKRIL
//
