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Database: UniProt
Entry: W2BYY0_9FIRM
LinkDB: W2BYY0_9FIRM
Original site: W2BYY0_9FIRM 
ID   W2BYY0_9FIRM            Unreviewed;      1106 AA.
AC   W2BYY0;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 48.
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   ECO:0000313|EMBL:ETJ99405.1};
GN   ORFNames=HMPREF0378_0198 {ECO:0000313|EMBL:ETJ99405.1};
OS   Eubacterium nodatum ATCC 33099.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales;
OC   Eubacteriales Family XIII. Incertae Sedis.
OX   NCBI_TaxID=1161902 {ECO:0000313|EMBL:ETJ99405.1, ECO:0000313|Proteomes:UP000018868};
RN   [1] {ECO:0000313|EMBL:ETJ99405.1, ECO:0000313|Proteomes:UP000018868}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33099 {ECO:0000313|EMBL:ETJ99405.1,
RC   ECO:0000313|Proteomes:UP000018868};
RA   Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M., Haft D.H.,
RA   Methe B., Sutton G., Nelson K.E.;
RL   Submitted (DEC-2013) 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:ETJ99405.1}.
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DR   EMBL; AZKM01000020; ETJ99405.1; -; Genomic_DNA.
DR   AlphaFoldDB; W2BYY0; -.
DR   STRING; 1161902.HMPREF0378_0198; -.
DR   PATRIC; fig|1161902.3.peg.1097; -.
DR   eggNOG; COG1197; Bacteria.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000018868; 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:UP000018868}.
FT   DOMAIN          576..737
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          758..912
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1106 AA;  127685 MW;  647B8BC5EAC0B9ED CRC64;
     MATEPRAKRL ADDLYFFTGQ NPIVMPSEEQ VFLRFEAKNH DMTMERLNGM KALTGDSDCI
     VIAPVTAAIK KVLPHNVIKD KKLLLKRGDE HFLTDIKEML VELGYERMSM VESRGEFSIR
     GGILDIFTPD ADNPYRVEFF DTEVDSIRSF DIDTQRSIEN LSFVEINPAE QMVLDKSRFS
     KAADRLYKAY TNQAKKLLKK GEQYAETVRS LEQRRDELCE YIRNQRNVQL LENYLHYFYD
     RTEYLWDYLD RGNVYVDDPN RIYELLDARE KELAQDFEVM LRRGDIVPED LELLTGKKDF
     MKCYNHRPIA FLSPFPKTIK GIEEYDSLET VQSSQMMRFS GHMELLESEL KSYVNKNYKI
     YLTASTDERR KNLIEYCDRI GVISFVNFLK GNLSSGFDFP KKKLCYISDN DIFGERINRR
     KKRRKMPGGQ RIESFSDLAK GDFVVHESHG VGKFIGIEQL DIQGDKKDYL KIKYAGNDFL
     YVPVEQFGIV QKYIGSDGIL PRLNKLSGAE WKLTKARAKQ AIAEMTDELI KLYAEREIEG
     GFAFSKDTPW QKEFEDSFPY VETDDQLRCI EEIKRDMELP KSMDRLLCGD VGFGKTEVAA
     RAIFKCIADG KQAAVLVPTT VLANQHYYNL KDRFEKFPVD IEMLSRFRSD AQQKKIIERL
     KTGDIDLIIG THRLLSKDIE YKELGLLVID EEHRFGVAHK EALKKIRKSV DVLTLSATPI
     PRTLNMSLSG IKDMSLIEEP PEERYPIQTY VMEQDDMMIR DVIKRELDRD GQIFIICNRV
     KGINKLAKKI SDLVPEARIS VGHGQMNENA LENVMLDFVN HETDILIATT IVESGIDIPN
     ANTMIVIDAE TYGLAQLYQL RGRVGRSNRM AYAYLMYRKD KVLTEVAEKR LRAIREFTEF
     GSGFKVAMRD LEIRGAGNLL GSQQSGQMMN IGYELYCKLV DEQIRRIKGE YVPEESDEIS
     VELPLPANIP NWYIENESLK LAIYKKISGV NSENKEDEMV DELLDRFGDV PKETMNLIRI
     SRVQALCQEV SVLRIYAQNN RIFFSFGEKN CLTPFAIVNI NDKFKGRAFI HGGKEPYIRI
     PQVKGLILKD CLELLNIIKE NMKDAI
//
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