ID   MFD_MYXXA               Reviewed;        1201 AA.
AC   O52236;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Transcription-repair-coupling factor {ECO:0000255|HAMAP-Rule:MF_00969};
DE            Short=TRCF {ECO:0000255|HAMAP-Rule:MF_00969};
DE            EC=3.6.4.- {ECO:0000255|HAMAP-Rule:MF_00969};
GN   Name=mfd {ECO:0000255|HAMAP-Rule:MF_00969}; Synonyms=trcF;
OS   Myxococcus xanthus.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Myxococcaceae; Myxococcus.
OX   NCBI_TaxID=34;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DK101;
RA   Garza A.G., Pollack J.S., Harris B.Z., Lee A., Keseler I., Licking E.F.,
RA   Singer M.H.;
RL   Submitted (OCT-1997) 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:0000255|HAMAP-Rule:MF_00969}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00969}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the UvrB family.
CC       {ECO:0000255|HAMAP-Rule:MF_00969}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the helicase family.
CC       RecG subfamily. {ECO:0000255|HAMAP-Rule:MF_00969}.
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DR   EMBL; AF031084; AAB94134.1; -; Genomic_DNA.
DR   PIR; T31114; T31114.
DR   AlphaFoldDB; O52236; -.
DR   SMR; O52236; -.
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 transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR   GO; GO:0000716; P:transcription-coupled nucleotide-excision repair, DNA damage recognition; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.300; -; 2.
DR   Gene3D; 3.90.1150.50; -; 1.
DR   HAMAP; MF_00969; TRCF; 1.
DR   InterPro; IPR036101; CarD-like/TRCF_dom_sf.
DR   InterPro; IPR003711; CarD-like/TRCF_domain.
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; IPR037235; TRCF-like_C_D7.
DR   InterPro; IPR005118; TRCF_C.
DR   InterPro; IPR041471; UvrB_inter.
DR   Pfam; PF02559; CarD_CdnL_TRCF; 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; SSF141259; 1.
DR   SUPFAM; SSF143517; SSF143517; 1.
DR   SUPFAM; SSF52540; SSF52540; 4.
DR   TIGRFAMs; TIGR00580; mfd; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; DNA damage; DNA repair; DNA-binding; Helicase;
KW   Hydrolase; Nucleotide-binding.
FT   CHAIN           1..1201
FT                   /note="Transcription-repair-coupling factor"
FT                   /id="PRO_0000102172"
FT   DOMAIN          670..831
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00969"
FT   DOMAIN          852..1006
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00969"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           784..787
FT                   /note="DEEQ box"
FT   BINDING         683..690
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00969"
SQ   SEQUENCE   1201 AA;  132665 MW;  CF8FD1A021A748C5 CRC64;
     MRLLITLGPS GSTHGHSLHT DAGRRRGGRP FAQVVDELRA GQRVRTQGLK GAARGHVLAR
     LHGALRAPLV CVAVDEEAAD ALAADLSFFL GGQGSLLAPR VLRLPADEVL PYDEVSPDAA
     AVTERLGALF HLGQGTRFPA LVLSVRALHR KVLPLAVMRA LAARVAVGQD FDRDSLARRL
     VRMGYQNSPL VEDVGTFSVR GDLLDVFSPL YDKPVRLEFF GDTIESIRAF DPQSQRTVDA
     LKEVDLVPAR EVLLTDETRP RAESAARAVA DRINLPTIKL REQLDALREG LPGFGMEGLL
     PGFFEDGLST VFDFLRDWSP EAPVIYLDDP LGQDRAADTL WEELERSHGA AEARQELICP
     PLEHFLSRED VNQRMQSFRV LEGGGLSLAQ TERPPVHFSF GGTQDLREAI LAHHGEEGAL
     SPLVERLERW RELRVACVVA CGTLSQADRL KRLLMDRNVM VKVHTEPLED AVALYEPSIR
     AHLFTGEVSH GFVDGPGGLA VLADEEIFGA RARRRPKRSK KLDAFGSGFG DLKEGDLIVH
     TDFGIGRYAG LTKMEVNGVP GDFLVLEYAG RDKIYLPVGR MRLIQKFSGG DPTQVQLDKL
     GTTSWEKTKK RVKEQLLKMA AELLQIAAAR KAHPGHAFSA PDRYFAQFEA DFEFEETPDQ
     AKAIEDVLAD MQKPEPMDRL VCGDVGYGKT EVAMRAAFKA ALDRKQVAVL VPTTVLAQQH
     FLSFKKRFAD YPVTVEVISG LKKAPEVREI LKRAKEGKVD ILIGTHKLLG GEVAFKELGL
     MIVDEEQRFG VKQKESLKKW RSQIDVLTLT ATPIPRTLHM SMSGVRDMSI IATPPQDRRA
     IRTFVMKYED TVVKEAIERE VARGGQVFFV HNRVESLPSI ETQLRALVPQ VSIGVAHGQM
     GEGQLEKVML AFTEKKYQVL LCTSIIESGI DISSANTMIV NRADQFGLAQ LYQLRGRVGR
     SKERAYAYLL VPSRRAVTKD AQRRLEVLQN FTELGAGFSI ASHDLEIRGA GNLLGDKQSG
     AIAEIGFDMY AQLLEEAVAE MQGQPPKVQI EPDVTLPMPA LIPDDYVSDV HQRLVFYKRF
     SQASHPDEVT DLRAELVDRY GEAPDEVDHL SELTLLKIDM RDLRLRGLEV GTTRLVVTLG
     ADALLDGPKV AGLVQRSKGV YRLTPDMKLI ARAPQGASGQ DLISEAKKVL RDLSHCALPQ
     A