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Database: UniProt
Entry: A0A1Y4N415_9FIRM
LinkDB: A0A1Y4N415_9FIRM
Original site: A0A1Y4N415_9FIRM 
ID   A0A1Y4N415_9FIRM        Unreviewed;      1143 AA.
AC   A0A1Y4N415;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
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=B5F09_09120 {ECO:0000313|EMBL:OUP75638.1};
OS   Erysipelatoclostridium sp. An173.
OC   Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC   Coprobacillaceae; Thomasclavelia.
OX   NCBI_TaxID=1965571 {ECO:0000313|EMBL:OUP75638.1, ECO:0000313|Proteomes:UP000196550};
RN   [1] {ECO:0000313|Proteomes:UP000196550}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An173 {ECO:0000313|Proteomes:UP000196550};
RA   Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA   Rychlik I.;
RT   "Function of individual gut microbiota members based on whole genome
RT   sequencing of pure cultures obtained from chicken caecum.";
RL   Submitted (APR-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:OUP75638.1}.
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DR   EMBL; NFKR01000019; OUP75638.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y4N415; -.
DR   Proteomes; UP000196550; 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:UP000196550}.
FT   DOMAIN          617..778
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          799..953
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1143 AA;  131396 MW;  A57F9F24B81DAD88 CRC64;
     MKKIDEILKK NLAFKTLLNG QGSIVVNNVN DEALLIAGAF LHLKKDIVVI KPNQYEANLL
     YQQLALINEQ DCLFFPVDES YRIETLASSP ELLGQRIDAL YQLSQNKPKI LITHGQALVR
     YLPTKQLFCD NCLDIKVGDH IDIYQLQTKL INAGYQNAMR VDQPFYFSKR GGVIDVFSIQ
     YENPVRIEFF DDEIDNIRFY DQNSQRTIEH VNQITIIPAS DILYEEKEVR AVLGKINDLR
     DQQFEELEEM YQDEYLNKVA IDQENLRNHD TSFNMYSYYN LFNQTANLLE YVNDPLIIQV
     NRHDIEIAYK NYLEENFYYY QELASIGKSV KGLNLFSDLY QILDQDAVFF NPFAKDDKDV
     FFNARGIMLD NNDENLLIKE IRDYLKVSKV LIALDDEHQI KLMCELFDRH EMLYTLVGIK
     DELYPGLNIG IYRLNAGIEL VDEKLVIISA NELFKTRNLN KPKYLKYKNA KIIKDYQELN
     VGDYVVHDNY GIGQYLGIKT LEVQGFHKDY LYVAYANNDT LYIPVEQFKL IRKYSSSEGK
     IPKVNKLGSS NWQKTKAKAR NKVDDIADKL IEIYSARINQ PGFAFPPDDQ IQLEFEQAFG
     YELTPDQQRS VDEIKADMEK PTPMDRLLCG DVGFGKTEVA LRAAFKAILA NKQVAFLCPT
     TILSMQHYKT MEARFKDFPV RIALLNRFTS SKNKKQILSD LKQGNIDLLV GTHRILSKDV
     IFKDIGLLCI DEEQRFGVRQ KERIKEYRKT IDVLTLTATP IPRTLQMSLM GIRGLSQIET
     PPKNRQPVQT YVVGKSNVLI KQIIERELAR DGQVFYLYNR TNQIANVAYN ISLAVPQAKV
     AIGHGQMDKN ELEDVMMRFV NKEFNVLVCT TIIETGIDIP NANTIIVEDA DRFGLSQLYQ
     IKGRVGRSNR GAYAYLLYNP GKILNEEASK RLKAIKEFTE LGSGYKIAMR DLAIRGAGDI
     LGGTQSGFID SIGFDMYMKI LQEAVNEKMG KVNEEKEIKS VNVNVDGYIP HDYVSSDIEK
     LELYQRLDQA KTIVAIDHLK SEFIDYYGKL PKEVAVLIEK RKLDILANSE IIEDIVEVKG
     KMQVTFTKQY SKELKGDQLF ELVNRLFTRP GFKQSGGQVM LLLPKSDQWL ERINQLISTL
     SAS
//
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