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
//