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Database: UniProt
Entry: A0A2A9D176_9MICO
LinkDB: A0A2A9D176_9MICO
Original site: A0A2A9D176_9MICO 
ID   A0A2A9D176_9MICO        Unreviewed;      1235 AA.
AC   A0A2A9D176;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
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=ATL40_2058 {ECO:0000313|EMBL:PFG20458.1};
OS   Serinibacter salmoneus.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Beutenbergiaceae;
OC   Serinibacter.
OX   NCBI_TaxID=556530 {ECO:0000313|EMBL:PFG20458.1, ECO:0000313|Proteomes:UP000224915};
RN   [1] {ECO:0000313|EMBL:PFG20458.1, ECO:0000313|Proteomes:UP000224915}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21801 {ECO:0000313|EMBL:PFG20458.1,
RC   ECO:0000313|Proteomes:UP000224915};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (OCT-2017) 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:PFG20458.1}.
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DR   EMBL; PDJD01000001; PFG20458.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A9D176; -.
DR   Proteomes; UP000224915; 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:UP000224915}.
FT   DOMAIN          692..853
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          878..1028
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1235 AA;  134150 MW;  C1C5311851B60EB3 CRC64;
     MGFGRPSGTP RLGGREAATL GPAAQNTPMK LTGLLSALAH DPSIDPTLRA LAQRRACEVI
     APVGARPALI AQLALAPQAP QIVVLTATGR EAESLVAALG AYLPAESLAA LPAWETLPHE
     RLSPRADTVA TRLAVMRRLT HPDPEGTGGS HTGRIRVLVV PVRAAMQPVV TGLGDLEPVA
     AHAGQTRPME EIVEALAAAA YTRTDMVTAR GEFAVRGGIL DVFPPTQDHP MRLDFWGDEI
     EEIRWFSAAD QRSLEVAPEG LWAPPCRELL LTDEVRERAL RLRDALPGAA EMLEKMAQGI
     AVEGMESLTP ALVDEMSQVL DLVEDDALLM AWDPERIRSR AADLQATTEE FLAAAWTSAA
     AGGSVPLDLS AASFVALAQV YERAQARGLL RWSLTVLPSD ADLVGADDTA GDEENLRLAA
     RDVEGYRGDL ERAVSDLRDL VRQEWRLVLA TDAAGQARRM VEQLRAAQVP ARLESDLETA
     PEPGVVHVTT ATIGRGFVAP DLRLALFTEA DLTGRATAGA RDAKRLASRR RNVVDPLALR
     PGDYVVHEQH GVGRFVELVQ RTVGGAAGAR GKPATREYLV IEYASPKQGK NAGSQDLLYV
     PTDALDQVTK YTGGEAPTLS RMGGSDWKNT KARARKAVRE IAGELIRLYS ARMATQGHAF
     APDTPWQREL EDAFAYVETP DQLVTIEEVK ADMEKSVPMD RLICGDVGYG KTEVAVRAAF
     KAVQDGKQVA VLVPTTLLVQ QHLQTFTDRF TGFPVTVAAL SRFQTDAEAA RVREDVRAGK
     VDVVIGTHRL LTGEVRFKDL GLVIVDEEQR FGVEHKETLK QLRTNVDVLA MSATPIPRTL
     EMAVTGIREM STLATPPEER HPVLTFVGPY EEKQIAAAIR RELLREGQVF YVHNRVESIE
     RAAAHLAELV PEARIAVAHG KMNEHQLERV IMDFWEKRFD VLVCTTIVET GLDISNANTL
     ILERADVMGL SQLHQLRGRV GRGRERAYSY FLYPPEKPLT ETAHDRLATI AANTDLGAGM
     QVALKDLEIR GAGNLLGGEQ SGHIAGVGFD LYVRMVSEAV QRFRGEEVEE LQDVTIELPI
     DAHIPHEYVP HERLRLEAYQ KIASARGSED VAAVREELVD RYGAVPASTE LLFAVAEMRT
     LARSLGVTAI TIQGQYIRFA PVELSDSATV RLKRLYPRSV IKAAVRTILV PAPTTARVGG
     EVLRDLALVE WVMGLLRSVV GSSVAAAAAV AGPGS
//
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