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Database: UniProt
Entry: B5CPD5_9FIRM
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Original site: B5CPD5_9FIRM 
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}.
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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
//
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