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Database: UniProt
Entry: A0A1G9IHU4_9ACTN
LinkDB: A0A1G9IHU4_9ACTN
Original site: A0A1G9IHU4_9ACTN 
ID   A0A1G9IHU4_9ACTN        Unreviewed;       989 AA.
AC   A0A1G9IHU4;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, 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=SAMN05216298_3255 {ECO:0000313|EMBL:SDL24662.1};
OS   Glycomyces sambucus.
OC   Bacteria; Actinomycetota; Actinomycetes; Glycomycetales; Glycomycetaceae;
OC   Glycomyces.
OX   NCBI_TaxID=380244 {ECO:0000313|EMBL:SDL24662.1, ECO:0000313|Proteomes:UP000198662};
RN   [1] {ECO:0000313|EMBL:SDL24662.1, ECO:0000313|Proteomes:UP000198662}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.3147 {ECO:0000313|EMBL:SDL24662.1,
RC   ECO:0000313|Proteomes:UP000198662};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00205}.
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DR   EMBL; FNGF01000004; SDL24662.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G9IHU4; -.
DR   STRING; 380244.SAMN05216298_3255; -.
DR   Proteomes; UP000198662; 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; 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; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
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   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          623..961
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   ZN_FING         764..790
FT                   /note="C4-type"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          969..989
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         51..58
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
FT   BINDING         665..672
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
SQ   SEQUENCE   989 AA;  107885 MW;  48E6BCB55A7170C4 CRC64;
     MANEYSSTDP NPQPAPARHP SGTIVVRGAR EHNLKDVDLD LPRDSLIVFT GLSGSGKSSL
     AFDTIFAEGQ RRYVESLSAY ARQFLGQMDK PDVDFIEGLS PAVSIDQKST SRNPRSTVGT
     ITEIYDYMRL LYARVGVPHC PQCGEEIGRQ SPQQITDQIM ALPEGTRFQV LAPVVRKRKG
     EFVDLFGDLQ QQGYARARVD GEVYALTDVP KLKKQEKHDI DVVIDRLVVK PSSIQRVTDS
     VESALGLADG VVELDFVDVA EGDPGRTRRF SEKLACPNDH PLQLDELEPR TFSFNAPFGA
     CPVCHGLGMR KEVDPELVIR DQEATIRAGA LAPWSSVGMG DYFLYQIEAL GEAVGFDVDT
     PWADLPSRAQ KAVLYGYDET LQVAYRNKRG QRRSYETRFE GVVPWVERRH TETDSEWTRE
     KYEQFMREIP CSTCEGTRLK PEILAVTVDG LSIHEVCTLS INECSKFFDA LKLSDRDTMI
     AAPIVKEVTA RLQFLLDVGL DYLTLARAAG SLSGGEAQRI RLATQIGAGL VGVLYVLDEP
     SIGLHQRDNN RLIATLERLR DLGNTLIVVE HDEDTIRVAD HIVDIGPGAG EHGGHVIYSG
     PVAGLTDAEG SITGDYVSGR RHIPVPEVRR KPDPGRELVV KGARENNLKG IDVAFPMGCM
     VSVTGVSGSG KSTLVNEILY NTLASEINGA KLVAGRHRTI TGLDGVDKVV GVDQSPIGRT
     PRSNPATYTG VFDKVRKLFA GTPEAKVRGW GPGRFSFNVK GGRCEACGGD GTLKIEMNFL
     PDVYVPCEEC GGARYNRDTL KVHYRGKTIS DVLDMPIEEG AEFFEPIQTI HRHLKTLVDV
     GLGYVRLGQP APTLSGGEAQ RVKLASELQK RSTGKTVYIL DEPTTGLHFE DVRKLLGVLD
     GLVEKGNTVI TIEHNLEVIK SSDWVIDLGP EGGDKGGTLV ATGTPEEIAA IAASHTGEYL
     RPLLGLEGKG NGTGAAARRA KTGNGRTRK
//
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