ID A0A0S7XZP9_9COXI Unreviewed; 1147 AA.
AC A0A0S7XZP9;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 35.
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 ORFNames=AMJ43_02935 {ECO:0000313|EMBL:KPJ67934.1};
OS Coxiella sp. DG_40.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Coxiella.
OX NCBI_TaxID=1703354 {ECO:0000313|EMBL:KPJ67934.1, ECO:0000313|Proteomes:UP000051153};
RN [1] {ECO:0000313|EMBL:KPJ67934.1, ECO:0000313|Proteomes:UP000051153}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DG_40 {ECO:0000313|EMBL:KPJ67934.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPJ67934.1}.
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; LIZW01000011; KPJ67934.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S7XZP9; -.
DR PATRIC; fig|1703354.3.peg.1720; -.
DR Proteomes; UP000051153; 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; 3.40.50.11140; -; 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; IPR048635; MFD_D3.
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; PF21132; MFD_D3; 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 612..773
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 782..948
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1147 AA; 131155 MW; 6FC5A783D0963DE8 CRC64;
MINNNLPLKK GEQTYWSGLY GSSSSLAIYT AAVNHNGPVI VLAPDMLHVN KLANDLHFFA
QQCNLDIMTL PDWETLPYDR FSPHQDIISQ RLLTFYKLLS FKTGILLVSV TTAMHRFVPH
DYIVNNSFVI NKHDQIDISK LRDDLQKRSY YCVNQVMEHG EFAIRGSIID VFPMGSLIPY
RIDLFDNEID SICEFDPETQ RSLKELESIN LLPAREISTS ESAINHFRHK WQALFPKNVE
NCPFYQSITD GNSVPGIEYY LPMFFTQTET LFDYLPHDGL LIRTSDLHKV AQTFWTEINE
RYEQLRYDIT HPILAPKDIF IPVDNLFGYF NNFSQIQITK ESRKTKTIDF KSKELPDLTL
DSKASQPLAK LQDFLNSTTA RILFCAESTG RQQALLQLLK HIDVEPMIYP SWDKFLQGTA
SLGISIAQLD QGLWLKNVII IPEAVIFGQQ VMQRRLREQQ QQDTEAVIRD LTELKIGDPV
VHIEHGIGRY LGLQTISTAG QEAEYLTIEY ANQAKLFVPI SALHSISRYM GANPENVPYN
DLGSKQWEKA KHKAQQKIYD VAAELLNIYA QRAAKIGFSF HKDDMQHQQF AGIFPFETTI
DQQNAIDQVI NDMASPRSMD RLICGDVGFG KTEVAMRAAF LAVENNKQVV ILTPTTLLAQ
QHYHNFQDRF ANWPVNIAML SRFNSPKQQK AIIDHLKKGK IDIIIGTHRL LQRDIEFKDL
GLLIVDEEHR FGVRQKEKIK SFRANVDILT LTATPIPRTL SMALSGIRDL SIIATPPAKR
LSIKTFIQDY NKQLIREAIL RETLRGGQVY FLHNDVATIE NKARELRELI PESRIEIAHG
QMPERQLEQI MGNFYHLRFN VLVCTTIIES GIDIPTANTI IINNADHFGL AQLHQLRGRV
GRSHHQAYAY LFVRSQKSIT RDAKKRLDAF ATMEGLGAGF TLAIHDLEIR GAGEILGKEQ
SGQIQAIGFN LYTELLNRAV KALKSGKQPE LTELFNYEGE IDLKIPALIP DNYVHNVNTR
LTLYKRIANA KDNAELHELQ VELVDRFGLL PQPVKNLFAI TKIKLKARLL GIYSIKADIA
HAVIEFDEKP NINSATIIEL IQKYPETYKF YGKNKLKFTL REDNAENRII KIEQLLKDIS
NLTKYRL
//
