ID B5CPD5_9FIRM Unreviewed; 1117 AA.
AC B5CPD5;
DT 14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2008, sequence version 1.
DT 24-JAN-2024, entry version 79.
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:EDY33041.1};
GN ORFNames=RUMLAC_01327 {ECO:0000313|EMBL:EDY33041.1};
OS [Ruminococcus] lactaris ATCC 29176.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Mediterraneibacter.
OX NCBI_TaxID=471875 {ECO:0000313|EMBL:EDY33041.1, ECO:0000313|Proteomes:UP000003254};
RN [1] {ECO:0000313|EMBL:EDY33041.1, ECO:0000313|Proteomes:UP000003254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29176 {ECO:0000313|EMBL:EDY33041.1,
RC ECO:0000313|Proteomes:UP000003254};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Ruminococcus lactaris ATCC 29176.";
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDY33041.1, ECO:0000313|Proteomes:UP000003254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29176 {ECO:0000313|EMBL:EDY33041.1,
RC ECO:0000313|Proteomes:UP000003254};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (AUG-2008) 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:EDY33041.1}.
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; ABOU02000032; EDY33041.1; -; Genomic_DNA.
DR RefSeq; WP_005610951.1; NZ_DS990191.1.
DR AlphaFoldDB; B5CPD5; -.
DR GeneID; 77334325; -.
DR eggNOG; COG1197; Bacteria.
DR HOGENOM; CLU_005122_1_3_9; -.
DR Proteomes; UP000003254; 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; 3.40.50.300; 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; 3.
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:UP000003254}.
FT DOMAIN 582..743
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 752..918
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1117 AA; 128265 MW; 7D79411BDED51B67 CRC64;
MLAFLEPLEE LADYQEIVQK RGKAEGILQI AGCVSSQKTH LMYALSDGFE YRVIVFSSEE
KAKQAYEEYK MLEENTFLYP AKDLLFYHAD IKGAALTGKR MEVLKKLTEK KNREPVTVIT
TADAFLDGLP SKEKLWESRI EIEAGAVIDF QKLQEELVHL GYERESQIEG PGQFAVRGGI
LDVYPLTEEI PVRIELWGDE IDSIRSFDVE SQRSVENMEK VVIYPATENV EKKEQAVSFS
EYFPKEESLF FFDEPVRLQE TLEAVEKEYF HSFESRKNAG MTEEADEIRV FQTKEIIEKF
NTRYGIGLTT LETRCGGFKV RDVYSIQAAG VNPYNNSFEM LTQDLKKLKR QGYRVILVSG
SRTRAKRLAE DLRDYDLSSF YSEDMVRTVR PGEIMVVYGC VAEGYEYPML KFMVISESDI
FGKRKKKRRR KVYEGQKIQE FAELKPGDYV VHENHGLGVY QGIEKVEVDK VTRDYMKISY
ADGGILYILA TQMDLIQKYA GADAKPPKLN KLGTPQWNKT KSQVKKAVQV IAQDLVELYA
VRQQTEGFVY SPDTVWQKEF EEMFPFEETE DQLRAIEDTK KDMESTKVMD RLICGDVGYG
KTEVAIRAAF KAVQDGKQVV YLVPTTILAQ QHYNTFIQRL KDFPVRIDLL CRFRTPAQQK
KTIEDLKKGL VDIVIGTHRV LSKDVTYKDL GLLIIDEEQR FGVTHKEKIK KMRENIDVLT
LTATPIPRTL HMSLIGIRDM SVLEEAPMDR MPIQTYVMEF NDEMIREAIE RELSRGGQVY
YVYNRVEDIA DVAGRVQKLV PGASVSFAHG QMSERELEDI MYDFINGEID VLVSTTIIET
GLDIANANTM IIQDADRFGL SQLYQLRGRV GRSSRMAYAF LLYRRDKLLK EVAEKRLAAI
REFTDLGSGI KIAMRDLEIR GAGNLLGEAQ SGHMAAVGYD LYCKMLNEAV KELKGEKEED
QFTTTMDLNI DAFIPESYIK NEYQKLDIYK RIAAITTEEE MDDMTEELID RFGDIPKKVQ
QLLHIAALKS LAHAAYVTAV EQKGSDFKFT LYEKAKLDPQ KIPGLLQRYG NKLVFRAEEP
PYFFYQKKGR SGKETGEDTI QLLRKILEDI RELRIVP
//