ID K8WTM1_9GAMM Unreviewed; 1147 AA.
AC K8WTM1;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 24-JAN-2024, entry version 53.
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=OOA_03979 {ECO:0000313|EMBL:EKT63989.1};
OS Providencia burhodogranariea DSM 19968.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Providencia.
OX NCBI_TaxID=1141662 {ECO:0000313|EMBL:EKT63989.1, ECO:0000313|Proteomes:UP000009336};
RN [1] {ECO:0000313|EMBL:EKT63989.1, ECO:0000313|Proteomes:UP000009336}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19968 {ECO:0000313|EMBL:EKT63989.1,
RC ECO:0000313|Proteomes:UP000009336};
RX PubMed=23145767; DOI=10.1186/1471-2164-13-612;
RA Galac M.R., Lazzaro B.P.;
RT "Comparative genomics of bacteria in the genus Providencia isolated from
RT wild Drosophila melanogaster.";
RL BMC Genomics 13:612-612(2012).
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:EKT63989.1}.
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DR EMBL; AKKL01000012; EKT63989.1; -; Genomic_DNA.
DR RefSeq; WP_008910835.1; NZ_KB233222.1.
DR AlphaFoldDB; K8WTM1; -.
DR STRING; 1141662.OOA_03979; -.
DR PATRIC; fig|1141662.3.peg.806; -.
DR eggNOG; COG1197; Bacteria.
DR HOGENOM; CLU_005122_1_3_6; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000009336; 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 CDD; cd18810; SF2_C_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 614..775
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 788..950
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1147 AA; 130695 MW; 0CCB2EE91CD6E1F1 CRC64;
MSSKFRYELP TRSGDVRHLG CLIGAAGALE CGEMIERHQG PVVIVTRDMQ NTLRLRDEIQ
QFTQLPIETL SDWETLPYDN FSPHQEIISQ RLSTLYRLPT MQKGALILPV NTLMQKVCPA
DFLTSHALVM AKGDKLSRDA LRDELDKAGY RHVEQVLEHG EYATRGALLD LFPMGSSVPY
RIDFFDDEID SLRTFDVDTQ RTLEEVSSIN LLPAHEFPTD KDAIERFRSQ WRERFEVRRD
PEHIYQQVSK KTLPTGIEYW QPLFFSQPLP SLFDYLPANT LFISQHYQES AERFQVDTQQ
RFESRGVDPM RPLLPPAELW LTVEQLNQSL KKWPRVQLSV EKLADKAANT NLDYLPLPDI
STQGQNKHPL EKLRQFVESF DGTVVFSVES EGRRETVTEL LGRLKIRPSN IEHYSSSSEN
RFAITVGAAE HGFIQSQLHR ALICESDLLG ERVVRRRSDN RRTINTDTLI RNLAELRQGQ
PVVHIEHGVG RYQGLTTLEA GGIQAEYLIL SYAGNDKLYV PVSSLHLISR YSGGADENAP
LHRLGSDSWG RARQKAAEKV RDVAAELLDI YALRAAKPGF KFKHDKEQYQ EFCQGFPYET
TPDQEVAINA VLSDMCQPIA MDRLVCGDVG FGKTEVAMRA AFLAISNNKQ VAVLVPTTLL
AQQHFDNFRD RFANWPIRIE MISRFKTAKE QQQIINDTAE GKVDILIGTH KLLQNSLVWH
DLGLLIVDEE HRFGVRHKER IKAMRADVDI LTLTATPIPR TLNMAMSGMR DLSIIATPPA
RRLAVKTFVR QYDDLVVREA ILRETLRGGQ VYYLYNDVEN IEKTKQRLEE LVPEARFVVG
HGQMRERELE RVMNDFHHQR FNVLICTTII ETGIDIPTAN TIIIERADHF GLAQLHQLRG
RVGRSHHQAY AYLLTPHPKA MTTDAQKRLE AISSLEDLGA GFALATHDLE IRGAGELLGE
DQSGQLTTIG FSLYMELLES AVEALKDGRE PSLEDLIKQQ TEVELRMPVL LPDDYIHDVN
IRLSFYKRIA SSTDEDELKE LRTELIDRFG MLPDAGKFLL ANAAIRLQAE KLGIKRIEAH
DQGGFIEFGE KNKVSPQFLI SLLQSQPQTF RLDGPVRLKF VIDLSDRLAR IEFIKQLLSD
FADNLLD
//
