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Database: UniProt
Entry: R7XUH2_9ACTN
LinkDB: R7XUH2_9ACTN
Original site: R7XUH2_9ACTN 
ID   R7XUH2_9ACTN            Unreviewed;      1195 AA.
AC   R7XUH2;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   RecName: Full=Transcription-repair-coupling factor {ECO:0000256|HAMAP-Rule:MF_00969};
DE            Short=TRCF {ECO:0000256|HAMAP-Rule:MF_00969};
DE            EC=3.6.4.- {ECO:0000256|HAMAP-Rule:MF_00969};
GN   Name=mfd {ECO:0000256|HAMAP-Rule:MF_00969};
GN   ORFNames=CF8_3169 {ECO:0000313|EMBL:EON22931.1};
OS   Nocardioides sp. CF8.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Nocardioides.
OX   NCBI_TaxID=110319 {ECO:0000313|EMBL:EON22931.1, ECO:0000313|Proteomes:UP000015971};
RN   [1] {ECO:0000313|EMBL:EON22931.1, ECO:0000313|Proteomes:UP000015971}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF8 {ECO:0000313|EMBL:EON22931.1,
RC   ECO:0000313|Proteomes:UP000015971};
RX   PubMed=23833136;
RA   Kimbrel J.A., Chang J., Arp D.J., Sayavedra-Soto L.A.;
RT   "The Draft Genome Sequence of Nocardioides sp. Strain CF8 Reveals the Scope
RT   of Its Metabolic Capabilities.";
RL   Genome Announc. 1:e00439-e00439(2013).
CC   -!- FUNCTION: Couples transcription and DNA repair by recognizing RNA
CC       polymerase (RNAP) stalled at DNA lesions. Mediates ATP-dependent
CC       release of RNAP and its truncated transcript from the DNA, and
CC       recruitment of nucleotide excision repair machinery to the damaged
CC       site. {ECO:0000256|HAMAP-Rule:MF_00969}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00969}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the helicase family.
CC       RecG subfamily. {ECO:0000256|HAMAP-Rule:MF_00969}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the UvrB family.
CC       {ECO:0000256|HAMAP-Rule:MF_00969}.
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:EON22931.1}.
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DR   EMBL; ASEP01000097; EON22931.1; -; Genomic_DNA.
DR   AlphaFoldDB; R7XUH2; -.
DR   STRING; 110319.CF8_3169; -.
DR   PATRIC; fig|110319.3.peg.3830; -.
DR   eggNOG; COG1197; Bacteria.
DR   HOGENOM; CLU_005122_2_2_11; -.
DR   Proteomes; UP000015971; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:UniProtKB-UniRule.
DR   GO; GO:0000716; P:transcription-coupled nucleotide-excision repair, DNA damage recognition; IEA:UniProtKB-UniRule.
DR   CDD; cd17991; DEXHc_TRCF; 1.
DR   CDD; cd18810; SF2_C_TRCF; 1.
DR   Gene3D; 2.40.10.170; -; 1.
DR   Gene3D; 3.40.50.11180; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 3.30.2060.10; Penicillin-binding protein 1b domain; 1.
DR   Gene3D; 3.90.1150.50; Transcription-repair-coupling factor, D7 domain; 1.
DR   HAMAP; MF_00969; TRCF; 1.
DR   InterPro; IPR003711; CarD-like/TRCF_RID.
DR   InterPro; IPR036101; CarD-like/TRCF_RID_sf.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR004576; Mfd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR047112; RecG/Mfd.
DR   InterPro; IPR037235; TRCF-like_C_D7.
DR   InterPro; IPR005118; TRCF_C.
DR   InterPro; IPR041471; UvrB_inter.
DR   NCBIfam; TIGR00580; mfd; 1.
DR   PANTHER; PTHR47964; ATP-DEPENDENT DNA HELICASE HOMOLOG RECG, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR47964:SF1; ATP-DEPENDENT DNA HELICASE HOMOLOG RECG, CHLOROPLASTIC; 1.
DR   Pfam; PF02559; CarD_TRCF_RID; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF03461; TRCF; 1.
DR   Pfam; PF17757; UvrB_inter; 1.
DR   SMART; SM01058; CarD_TRCF; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00982; TRCF; 1.
DR   SUPFAM; SSF141259; CarD-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 4.
DR   SUPFAM; SSF143517; TRCF domain-like; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00969}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00969};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW   Rule:MF_00969};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW   Rule:MF_00969};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_00969}; Helicase {ECO:0000256|ARBA:ARBA00022806};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00969};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00969}; Reference proteome {ECO:0000313|Proteomes:UP000015971}.
FT   DOMAIN          661..822
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          840..997
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1195 AA;  130942 MW;  C31D964B8095737D CRC64;
     MHADVDAVME VVVQDHKTPL TAVADAVLAG PVLAEAMAEA SQVRALDLTG PAAVRPLVVK
     GLADAGRTVL AVTATAREAE DLVVELADLL DPATIAYYPS WETLPHERLS PRSDTVGRRL
     AVLRRLKHPG TDASNGPLRV IVAPVRSILQ PQVKGLADLE PVELTKGSTA ALDDVVRGLA
     DAAYSRVDMV EKRGEFAVRG GIVDVFPPTE EHPLRVEFWG DEVEEIRSFS VADQRTVETL
     DRLWAPPCRE LLLTEDVRRR AAALGQAHPQ LLELTDKIAA GIAVEGMESL APVLVDEMEL
     LVDLLPDTTT VLVLDPERAR TRAHDLVATS EEFLGASWAA AASGGQSPID LGAASYREVA
     DVRGSVIERS LGWWTVSPFG IDSQELDVEV IAGAVPSRAL SVQGAEAYRG DLEKAIADIR
     GWLAQGYRVT VVHQGHGPAE RMVEVLGEHD VPAALIDGAV SPDASVVTVT TGCLVSGFID
     PETKVAVLTG EDISGQKGST RDMRKMPARR KKQIDPLELK AGDYVVHEQH GVGRFVAMQQ
     REMQGATREY LVLEYGSSKR GAPADRLFVP ADTLDQITRY VGGEQPSLDR LGGGDWTKRK
     NRARKAVREI AAELIKLYAA RQATKGHAFG PDTPWQRELE DAFPFHETPD QLTTVDEVKA
     DMRRTVPMDR LVCGDVGYGK TEIAVRAAFK AVQDGKQVAV LVPTTLLVTQ HLSTFTERMS
     GFPVVLKGLS RFQTDKEARE VVAGLEDGSI DIVVGTHRLL SPNIKMKDLG LIIVDEEQRF
     GVEHKEQMKR LRTSVDVLSM SATPIPRTLE MAVTGIREMS TITTPPEERH PVLTYVGAYE
     DRQVIAAVRR ELLREGQVFF IHNRVNSIEK AAAHIRELVP EARVATAHGQ MGEHQLEQVM
     LDFWEKRFDV LVCTTIVESG LDVSNANTMI IERADTLGLS QLHQLRGRVG RSRERAYAYF
     LYPAEKPLTE TAHERLATLA QHSDLGGGMA IAMKDLEIRG AGNLLGGEQS GHIADVGFDL
     YVRLVGEAVN DFKGEGAEEL GEVRIELPVD AHLPHDYISS ERLRLEMYKR LAEVRADEDV
     DQLREEMVDR YGQPPIEVES LLIVARFRAR ARQAGVKEIT LAGKFVRFAP VDLPDSRVVR
     LGRVYPKSIV KAPTQTILVP RPQTAVIGGK PIDGIALLEW ARHVIDDIID PPTTS
//
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