ID   MFD_BUCAI               Reviewed;         812 AA.
AC   P57381; Q9F456;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Transcription-repair-coupling factor;
DE            Short=TRCF;
DE            EC=3.6.4.-;
GN   Name=mfd; OrderedLocusNames=BU294;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS   pisum symbiotic bacterium).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=107806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APS;
RX   PubMed=10993077; DOI=10.1038/35024074;
RA   Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT   "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT   sp. APS.";
RL   Nature 407:81-86(2000).
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 site
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the UvrB family.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the helicase family.
CC       RecG subfamily. {ECO:0000305}.
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DR   EMBL; BA000003; BAB13004.1; -; Genomic_DNA.
DR   RefSeq; NP_240118.1; NC_002528.1.
DR   RefSeq; WP_010896053.1; NC_002528.1.
DR   AlphaFoldDB; P57381; -.
DR   SMR; P57381; -.
DR   STRING; 107806.10038969; -.
DR   PRIDE; P57381; -.
DR   EnsemblBacteria; BAB13004; BAB13004; BAB13004.
DR   KEGG; buc:BU294; -.
DR   PATRIC; fig|107806.10.peg.304; -.
DR   eggNOG; COG1197; Bacteria.
DR   HOGENOM; CLU_005122_8_2_6; -.
DR   OMA; CYAVIPA; -.
DR   Proteomes; UP000001806; 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 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   Pfam; PF02559; CarD_CdnL_TRCF; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF03461; TRCF; 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; 3.
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; Reference proteome.
FT   CHAIN           1..812
FT                   /note="Transcription-repair-coupling factor"
FT                   /id="PRO_0000102164"
FT   DOMAIN          280..441
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          462..621
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   MOTIF           394..397
FT                   /note="DEEH box"
FT   BINDING         293..300
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   812 AA;  93881 MW;  BB5C9F54D9EF2C35 CRC64;
     MKITKNKILK NKKIINFKYQ KLLDLFYNVN NQKKNNQLLS YLYSFSGKII FSLTEEKSLK
     KILRFLMRHK IHPQYIKRII DIKKEIDYFY MIEEIKNGFI DKKNNILFLC TKDLLPILID
     DKYIGNIKKN TNNINKFNLS QLILNHPVMH IEHGIGRYKG LTTIETASIQ SEYLVISYAE
     GDKLYVPVSN LHLVSPYTGT SIENAPLHKL GGDDWNKEKH KISKTVYDHA AQLLHIYAKR
     ESKTGFAFKK NIEKYDLFCN DCSFKTTSDQ NEVMKFVLKD MSKPIPMDRL ICGDVGFGKT
     EIAMRASFLA VSNKKQVAIL VPTTLLAQQH YKNFKIRFSN WPVNINILSR FQTQKEQDLI
     FKHTKNGRIN IIIGTHKLLF KNIEWCSLGL LIIDEEHRFG VSHKEIIKKI YSNIDILTLT
     ATPIPRTLNM AMTGIKDLSI IAKPPAQRLA IKTFIQEYSP ILIRKTILRE ISRGGQVYYI
     YNKVQNIMNI AERLSILIPE ASIKIGHGQM KNIDLKKVMN EFYNNKFNVL ICTTIIESGV
     DIARANTIII ENSDHFGLSQ LHQLRGRIGR SNNQAYALLL VNNFNKITSD AKKRLEAISS
     VDNFGGGFSL SNQDLEIRGV GEILGKEQSG HIKNIGFSLY MDLLKNAIDL LKNGKIFSVE
     KSLKKPLEID LHVSSLLPSS YILDINTRLF FYKKLANAIH EKQIEEIKYE LIDQFGKLPD
     FSKNLILIAK IRLIADKIGI KYIKSNNNIG IIEFNDYGSI NTEYLLKMFQ KEPKIWKMET
     STRIKFILHL KNDYLRLKWI INLLRNLFKK NI