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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//