ID M6Y957_9LEPT Unreviewed; 1181 AA.
AC M6Y957;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 48.
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:EMO90275.1};
GN ORFNames=LEP1GSC024_0166 {ECO:0000313|EMBL:EMO90275.1};
OS Leptospira noguchii str. 2001034031.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=1193053 {ECO:0000313|EMBL:EMO90275.1, ECO:0000313|Proteomes:UP000012138};
RN [1] {ECO:0000313|EMBL:EMO90275.1, ECO:0000313|Proteomes:UP000012138}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2001034031 {ECO:0000313|EMBL:EMO90275.1,
RC ECO:0000313|Proteomes:UP000012138};
RA Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA Sanka R., DePew J., Purushe J., Whelen A.C., Vinetz J.M., Sutton G.G.,
RA Nierman W.C., Fouts D.E.;
RL Submitted (JAN-2013) 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:EMO90275.1}.
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; AKXB02000057; EMO90275.1; -; Genomic_DNA.
DR RefSeq; WP_004444528.1; NZ_AKXB02000057.1.
DR AlphaFoldDB; M6Y957; -.
DR Proteomes; UP000012138; 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}; 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}.
FT DOMAIN 652..813
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 822..988
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1181 AA; 134483 MW; 5A8DD31F9A49B47F CRC64;
MKDLLNMIGE EIFSKFESSP KKKNSTSKVK SSFAEASKAQ SNFILKKYTS EKNLSVNTEV
VGSVYSVTTG SHSILASSLF QKLNKTILVV SENNTSAEFL FREALSFLSS NDLIYLPGQE
VLPYEYMRYP SEMKRERIKA IAKILSGEPS LIFTSVSGFL KTLPPIQTMQ GRAIVLEKGK
EIDLESLLIQ LIDLGYKRVQ VCETFGEFSL KGGILDIFSS YSTEPVRIDL FGEEIESIRT
FDPDSQRSMA DLNQAILLPA DEYILSEEQK KEYQNILKSS DSSLHLPEIP EGSYGIYYEE
LIPLVRENHG ILSYFSEPPV LIFPSVNSVK ERLFHLEKEY VSLFEKRSRE VLCAPPEKLL
SFGEEFKVLS ESIGLSFVGL PPKNENDLIS FLKEAPSFKG KIREVREKIS KLREEGGWKI
VLTSSFEAQT KRLQGLFEKE GVVLLNEDST EPLPFHLENH KSDAFLVLSE LRNGFIFENQ
KILILSENDI FGREYKRKTR FKKQSSKALQ SFIDLKEGDY VVHIHHGVGK FLKIERTSAN
GKERDFLKLE YSGGDSLFVP LDQISLVQRY IGGTESPRLD SLGKSTWKKT KDRVQKTVEA
LAEDLVQMYS NRLKLQGYAF PPDTIYQEEF EAEFEYEETP DQIEAIEAVK KDLESPRPMD
RLVCGDVGYG KTEVAIRAAF KVAMAGRQIM MLAPTTILAL QHYNTFKSRF ENYPVRVELV
SRFKTPAEIR DILADFSAGK VDMVVGTHAI LSSKLKPKNL GLLVIDEEQR FGVNHKEAIK
KFKNLVDVLT LTATPIPRTL HMALTGIREL SIIATPPKNR QSVETYVLEE EDDLIADAIR
NEVQRDGQVF YLYNRVETID QETSYLNKLV PEVSIGILHG QMTEDEIEET LLDFYNRKYD
ILVTTTIIES GIDMPNVNTL FVKRADLFGL SQLYQIRGRV GRSDRKAFAY MLLPKDRVVT
EQAEKRLNTI FEYQELGSGF KVAMRDLEIR GAGNLLGKEQ SGDIMEVGFD LYVRMLEDAI
ARIKGEEIVV EVRTSVTLNT NFFIPETYIS DTRQKIEFYK KFEGARDLDE IEEIYSEMLD
RFGEPPEDAK TFILLEKIRT LASSLGFESV TEMKDEIKMK SGSYFKGDHT KIIQLISART
GLTLNPREPN VLIFQTGKKL EKEKLDTLIF LLSEMLPSKK V
//
