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Database: UniProt
Entry: A0A1Q5Q129_9ACTO
LinkDB: A0A1Q5Q129_9ACTO
Original site: A0A1Q5Q129_9ACTO 
ID   A0A1Q5Q129_9ACTO        Unreviewed;      1176 AA.
AC   A0A1Q5Q129;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
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=BSZ39_08870 {ECO:0000313|EMBL:OKL53573.1};
OS   Bowdeniella nasicola.
OC   Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC   Bowdeniella.
OX   NCBI_TaxID=208480 {ECO:0000313|EMBL:OKL53573.1, ECO:0000313|Proteomes:UP000185628};
RN   [1] {ECO:0000313|Proteomes:UP000185628}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19116 {ECO:0000313|Proteomes:UP000185628};
RA   Meng X.;
RL   Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
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:OKL53573.1}.
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DR   EMBL; MQVR01000053; OKL53573.1; -; Genomic_DNA.
DR   RefSeq; WP_073716984.1; NZ_MQVR01000053.1.
DR   AlphaFoldDB; A0A1Q5Q129; -.
DR   STRING; 208480.SAMN02910418_01350; -.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000185628; Unassembled WGS sequence.
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   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:UP000185628}.
FT   DOMAIN          639..800
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          818..975
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1176 AA;  128634 MW;  2A00031809AC49BB CRC64;
     MDLRPLLPLL AHDASFADAV AAVPDRGLKT LVAPAGIRPA LLAAAAEARP LAIVTPTGRQ
     ADELAAALRG YLPDADVAVL PAWETLPHEK LSPRPDTVAR RLAVLRRLAH PDPHTPGAGP
     LRVVIIPVRS LIQPVVAGAA ELEPVRLAVG EEIDMQEVVA RLADAAYTRV DMVERRGEFA
     VRGGLLDIFP PTESHPLRVE FFGDEVDEIR SFSVADQRSI EASEFLWAPP AREILLTDRV
     RARAREAIAD FPGARDMLER LSEGIAVEGM ESLAGVLVED MHSVVANLDP EMLLVALDPE
     RIARRVDDLL ATTEEFLSAA WTSAAAGGEA PLVLRKASFL TLDQTREAAL ERRLGWWELT
     ELPSGAEGEH VLDAEAASRY RGRIDELATD LAAWLHEGRH VVITTDGPGP GRRVAEQLAD
     AGIAAAYAPD APAGLPTGTV HVTLGTLAEG YLAPGARVVH LAHSDLTGRR RDTAAAGQKM
     PTKRRKTVDP LALKPGDYVV HDTHGVGQFV ELITRSVGAG AKKGMREYVV IEYAASRRGG
     PPDRLFVPTD SLDQVTKYTG GEAPSVNRLG GSDWAKTKSR ARKAIREIAA ELIRLYAART
     SAKGHAFSPD TPWQRELEEA FPYMETPDQL ATIEDVKADM ERPVPMDRLI CGDVGYGKTE
     IAVRAAFKAV QDGKQVAVLC PTTLLAQQHF ETFSERYGGF PVRVAALSRF QSAKEAREIK
     DGLKAGTIDV VIGTHRLVTG EVHFKDLGLV IVDEEQRFGV EHKEALKQLR TDVDVLAMSA
     TPIPRTLEMA VTGIREMSTL ATPPEERHPV LTYVGRYEEK QIAAAIRREL LRDGQVFFVH
     NRVESIDRVA ARLHELVPEA RIGVGHGKMN ETQLEKVIVD FWNREYDVLV CTTIVETGLD
     ISNANTLIVD RADAFGLSQL HQLRGRVGRG RDRAYAYFLY HPEKTLTETA YERLRTIAAN
     TDLGAGMQVA MKDLEIRGAG NLLGGEQSGH IAGVGFDLYV RMVAEAVAAF KGEYSGSKDM
     KLELPVDAHV PEDYIGHERL RLEAYSKIAA ARTREDLDAI AAELTDRYGP IPRVVERLFT
     VAELRESARA IGLEEAIVQG QMLRVGPLQL KDSQQVRLKR LHPGTHIRLA TRQLLIPLPK
     PKGFGNVALS DDEILGWVRD LFALLSAIVS ARRVPE
//
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