ID E3FW23_STIAD Unreviewed; 1194 AA.
AC E3FW23;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 75.
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 OrderedLocusNames=STAUR_6988 {ECO:0000313|EMBL:ADO74744.1};
OS Stigmatella aurantiaca (strain DW4/3-1).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Archangiaceae; Stigmatella.
OX NCBI_TaxID=378806 {ECO:0000313|EMBL:ADO74744.1, ECO:0000313|Proteomes:UP000001351};
RN [1] {ECO:0000313|EMBL:ADO74744.1, ECO:0000313|Proteomes:UP000001351}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DW4/3-1 {ECO:0000313|EMBL:ADO74744.1,
RC ECO:0000313|Proteomes:UP000001351};
RX PubMed=21037205; DOI=10.1093/molbev/msq292;
RA Huntley S., Hamann N., Wegener-Feldbrugge S., Treuner-Lange A., Kube M.,
RA Reinhardt R., Klages S., Muller R., Ronning C.M., Nierman W.C.,
RA Sogaard-Andersen L.;
RT "Comparative genomic analysis of fruiting body formation in Myxococcales.";
RL Mol. Biol. Evol. 28:1083-1097(2011).
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}.
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DR EMBL; CP002271; ADO74744.1; -; Genomic_DNA.
DR RefSeq; WP_013377597.1; NC_014623.1.
DR AlphaFoldDB; E3FW23; -.
DR STRING; 378806.STAUR_6988; -.
DR KEGG; sur:STAUR_6988; -.
DR eggNOG; COG1197; Bacteria.
DR HOGENOM; CLU_005122_1_3_7; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000001351; 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}.
FT DOMAIN 663..824
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 844..999
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1194 AA; 132052 MW; 3758DCB161C9D551 CRC64;
MDTPFSQTAG SEALRGAVPP TGDPFARLLE RLQPGHRART QGLHGAARGH VLARLSRTLK
APLVCVAVDE EAADALAGDL AFFLGGNGTL LAPRVLRLPA DEVLPYDELS PEPHIVSERL
GTLFHLSQGT RFPALVLSLR ALLRRVLPVS TMTGLAQLLT TGQDIDRDTL ARQLVLMGYQ
SSPLVEDPGT FSVRGGILDV FSPLYERPVR LEFFGDTIES IRLFEPDNQR TVDSLKEVSL
VPARELLLTD QTRAKAEATA RAVADHINLP TIKLRERLDA LREGLPGFGL EGLLPGFFEG
GLATVFDYLR LWAREPVFYF DDPVGLERAA TDLWEELERS HQEADARQDL TLPPSEHFLT
REQADAQLAG WRGVEGGGLA LTPGEQPPVL FSFGGTQDLR EAILAHHGEE GALTPLVERL
QRWRDMHVAC AIACGTLSQA DRLKRLLLDR HLMVRIHEEP LTDASKLYEP SVYAHLYTGE
VSHGFVDGTG GLAVLADEEI FGVRARRRVR RSKKSEAFGA GFKDLKEGDL IVHTDFGIGR
YAGLTKMQVN GVPGDFLVLE YAGRDKIYLP VGRMRLIQKF TGGDPSQVQL DKLGTPGWEK
TKRRVKEQLL KMAAELLQLA AARKAHPGHA FSAPDRYFAQ FEADFEFEET PDQAKAIEDV
LADMQKPTPM DRLVCGDVGY GKTEVAMRAA FKAALDRKQV AVLVPTTVLA QQHFLSFKKR
FKDYPITVEV ISGLKKPPEV RELLKRAKEG RVDILIGTHK LLGGDVAFKD LGLLIVDEEQ
RFGVKQKEQL KRLRTQVDVL TLTATPIPRT LHMSMSGVRD MSIIATPPQD RRAIRTFVMK
FDPQVIQEAI QREVARGGQV FFVHNRVQSI ASMEKLLREL VPKVSIGVAH GQMGEGQLER
VMLAFTEKQH QVLLCTSIIE SGIDISSANT MIINRADAFG LAQLYQLRGR VGRSKERAYA
YLLVPARRAV TRDAQRRLEV LQNFTELGAG FSIASHDLEI RGAGNLLGDK QSGAIAEIGF
DMYAQLLEEA VAEMQGQPPR MQIEPDITLP MPALIPDDYV PDVHQRLVFY KRFSQASHPD
EVTDLRAELV DRYGEAPDEV DCLSEVTLLK IDMRDLRLRA LEGAAGRLVV TLGADALLDG
PKVAALVQRS KGLYRLTPDM KLVTRVPEGV KGLALITEAK KVLRDLSACA LPQA
//