ID A0A2A7MB40_9CLOT Unreviewed; 1167 AA.
AC A0A2A7MB40;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
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:PEG28944.1};
GN ORFNames=CQ394_20050 {ECO:0000313|EMBL:PEG28944.1};
OS Clostridium neonatale.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=137838 {ECO:0000313|EMBL:PEG28944.1, ECO:0000313|Proteomes:UP000220840};
RN [1] {ECO:0000313|EMBL:PEG28944.1, ECO:0000313|Proteomes:UP000220840}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LCDC99A005 {ECO:0000313|EMBL:PEG28944.1,
RC ECO:0000313|Proteomes:UP000220840};
RA Bernard K., Burdz T., Wiebe D., Balcewich B., Alfa M., Bernier A.-M.;
RT "Effective Description of Clostridium neonatale sp. nov. linked to
RT necrotizing enterocolitis in neonates and a clarification of species
RT assignable to the genus Clostridium (Prazmowski 1880) emend. Lawson and
RT Rainey 2016.";
RL Submitted (OCT-2017) 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:PEG28944.1}.
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DR EMBL; PDCJ01000006; PEG28944.1; -; Genomic_DNA.
DR RefSeq; WP_058293129.1; NZ_PDCJ01000006.1.
DR AlphaFoldDB; A0A2A7MB40; -.
DR STRING; 137838.GCA_001458595_00118; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000220840; 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}; Coiled coil {ECO:0000256|SAM:Coils};
KW 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:UP000220840}.
FT DOMAIN 641..802
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 811..977
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT COILED 250..277
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1167 AA; 134603 MW; C7B8EC86DAB9A491 CRC64;
MRLKGLLEPL EESSEFKNLE DSIKGKKYPI GIYGISESGR GYIIDGIFEN IDKSIVVVTQ
NDIEAKNLYE DLILYTNEVY YFPAKEVVFY NIDAVSGDLR WARLKVINEI LNNNKKIIVT
SVDAFASKYT PHKLFTEYNI KLKENDDVDV KEIGKKLIQS GYERVEMVEG KGQFSLRGGI
LDVFPTCSSY PYRIELFGDE IESIRTFNIE SQRSIEKVKS VNIFPAKEIV LTDEALEYGR
EKLKSEFEEI EDKDKDKDRV EKLRKILNKN LESLEETCSF ETIDSYLNYF SKKTESLFDY
FNDYYFIMDN VQRCEGKLNS TYIEFEENFT AFSQRGDIFP GQGGLLLNKE EILGSFSEQK
IIFLESLSQN NNWLRPITKI DISQSTLTNY QGQLDLLIDD ISRKKSEEYK TLILSGTRAR
GERLVDTLRD RGIESSYKDS VDKINFGEVV ITFGNQLKGF EYPNYKICVI SDKEVFGEAK
RKLKTKNKSK QKGIAKIKSF AELKPGDYVV HANHGIGVYK GIKQIDVAGH KRDYLDIVYD
KGDKLYVPVE QLDLIQKYVG SEGKFPKINK LGGTEWQKAK AKARKSINEI AEDLVKLYAT
RATVRGYKFS KDTQWQKQFE DEFPYEETPD QLTSLEEIKS DMESDKPMDR LLCGDVGYGK
TEVAVRAAFK CVMDGKQVAF LVPTTILAEQ HYKNMKNRFS DFPIKVDMVS RFRTTKQQKE
TLQRLKEGNV DILIGTHRIV SKDIQFKDLG LLIIDEEQRF GVKQKEKIKN LKKNVDVLTL
SATPIPRTLH MSLTGVRDIS VIETPPEERY PVQTYVVEQN DQLIRDAILR EVGRDGQVYF
VYNRVEDIDR MAKYVQELVP EAKVGIAHGQ MAERELEKEM MDFMSGEHNV LVCTTIIETG
MDIQNVNTII IYDSDKMGLS QLYQLRGRVG RSNRIAYAYL LYTKDKVLTE VAEKRLKALR
DFTELGSGFK IAMRDLEIRG AGNMMGSSQH GHMATIGYDL YCRMLEDTIK IIKGEISKEP
IETTVDIKVD AFISEHYIED EIQKIEVYKK IAAIENIDDY NDIEEELNDR YSKMPESVRN
LMDIAYIKNK AKTVFIEEIK EMPKVIIFKF AQGESDYSNI YVNLIKKYKD IVVLKFGLEP
YFAFKIKGIK KENKLEFLKE VVDDIIL
//
