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Database: UniProt
Entry: A0A174ET16_9FIRM
LinkDB: A0A174ET16_9FIRM
Original site: A0A174ET16_9FIRM 
ID   A0A174ET16_9FIRM        Unreviewed;      1108 AA.
AC   A0A174ET16;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
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:CUO40437.1};
GN   ORFNames=ERS852394_02111 {ECO:0000313|EMBL:CUO40437.1};
OS   Blautia obeum.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Blautia.
OX   NCBI_TaxID=40520 {ECO:0000313|EMBL:CUO40437.1, ECO:0000313|Proteomes:UP000095409};
RN   [1] {ECO:0000313|EMBL:CUO40437.1, ECO:0000313|Proteomes:UP000095409}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2789STDY5608837 {ECO:0000313|EMBL:CUO40437.1,
RC   ECO:0000313|Proteomes:UP000095409};
RG   Pathogen Informatics;
RL   Submitted (SEP-2015) 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}.
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DR   EMBL; CYZD01000010; CUO40437.1; -; Genomic_DNA.
DR   RefSeq; WP_055066244.1; NZ_CYZD01000010.1.
DR   AlphaFoldDB; A0A174ET16; -.
DR   Proteomes; UP000095409; 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:UP000095409}.
FT   DOMAIN          580..741
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          750..916
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1108 AA;  127626 MW;  34BB36BB703C9094 CRC64;
     MKTFLQPLQN LAEMEEIQKQ AKKNRGILEI SGCMESQKAH LMYGLSGLFP CHLVIAADEK
     SAKELYEDYR FYDKRVYYYP AKDLLFFQAD IHGNLLIRQR MQVIRALLER EDEITVVTSI
     DGCMDYLAPL EKIEKQLIHF RNDSTLDMDK LTAALVHMGY ERVGQVEMPG QFSIRGGIID
     IYSLTEENPW RIELWGDEID SIRSFDAQSQ RSLENLDDVT IYPAAEQPME KNGVSFLDYF
     KETETLFFLD ELNHLEENAK AVQEEFQQSC ENRKEKGEIS LSGDWMCTWE ELCHKINDRN
     CVAMSLLDPK KSNWKISGQF NITVKSMSSY QSSFELLVKD LKQYKKEGYQ IVLLSGSRTR
     AERLAKDLQE EGLNAFYGQD SDRILQPGEI MVVYGHARRG FEYPLVKFAV ITETDIFGKE
     QKKRKKKKEY NGKRIQDFSE LSIGDYVVHE KHGLGIYKGI EKVAVDKVAK DYIKIEYRNG
     SNLYILATQL DALQKYSGAE TAKPPKLNRL GGQEWKKTKS RVRGAVQNIA RELVELYAVR
     QEKEGYVCGP DTVWQREFEE MFPYEETEDQ LAAIEDTKKD MESTKIMDRL VCGDVGYGKT
     EVALRAAFKA VQESRQVVYL VPTTILAQQV YNTFIQRMKE FPVRVDLLCR FRTAAQQKKT
     IADLKKGQVD IVVGTHRVLS KDVEYKNLGL LIIDEEQRFG VVHKEKIKQL KKDIDVLTLT
     ATPIPRTLHM SMIGIRDMSV LEEPPMDRVP IQTYVMEYDE ETVREAINRE LRRGGQVYYV
     YNRVNDIADV TARIAKLLPD ARVDFAHGQM SERELEAVMY AFINGDIDVL VSTTIIETGL
     DISNVNTMII HDSDRYGLSQ LYQLRGRIGR SNRTAYAFLM YRRNTMLKET AEKRLSAIRE
     YTDLGSGFKI AMRDLELRGA GNLLGAEQHG HMNAVGYDLY CKMLSEAVKE AKGIHTMEDF
     ETTIDLNMDA FIPDSYISNE YQKLDIYKRI AGIETQQDYD DMLEELLDRF GEMPKAVLNL
     LVIARMKAQA HRCYVVEIKQ IAGDMKITLY ERAKLNPAGI PVLMQKYRRG LQFKNEQEPK
     FIFTPEGARN TLTALTDFLT ELESLVEE
//
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