ID A0A0R0C6U6_9GAMM Unreviewed; 1191 AA.
AC A0A0R0C6U6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 50.
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=ABB27_15505 {ECO:0000313|EMBL:KRG65407.1};
OS Stenotrophomonas terrae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas.
OX NCBI_TaxID=405446 {ECO:0000313|EMBL:KRG65407.1, ECO:0000313|Proteomes:UP000051863};
RN [1] {ECO:0000313|EMBL:KRG65407.1, ECO:0000313|Proteomes:UP000051863}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18941 {ECO:0000313|EMBL:KRG65407.1,
RC ECO:0000313|Proteomes:UP000051863};
RA Patil P.P., Midha S., Patil P.B.;
RT "Genome sequencing and analysis of members of genus Stenotrophomonas.";
RL Submitted (MAY-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}.
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:KRG65407.1}.
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DR EMBL; LDJJ01000055; KRG65407.1; -; Genomic_DNA.
DR RefSeq; WP_057629683.1; NZ_LDJJ01000055.1.
DR AlphaFoldDB; A0A0R0C6U6; -.
DR PATRIC; fig|405446.3.peg.2856; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000051863; 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; 5.
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 658..819
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 840..994
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 429..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1191 AA; 131836 MW; C7E7DF58425471B3 CRC64;
MSPITYPNPP LPRSGQLRAW WRAPASSSAL AWHVACAAQA HDKPLLLVTR DNQSAHQLVA
DLQTLLGADS PLPVVPFPDW ETLPYDQFSP HPDIISQRLA ALHRLPALKQ GIVVLPVQTL
LQRLAPLSYI VGGSFDLKVG QRLDMDAEKR RLESAGYRNV AQVMDPGDFA VRGGLLDVYP
MGADAPLRIE LLDEDIDSIR EFDPESQRSL EKVTAVKMLP GREVPMDEAS LNKVLATLRE
RFDVDTRRSP LYQDLKAGLL PSGIEYMLPL FFNQTATLFD YLPAGFMTVL GSGVGEASDA
FWLQTNSRYE QRRHDIERPL LPPEEIYQSP DKLREQFNKL PRVEVCAADH PRAAEAQPLG
DQPLPPLPVA AKDAPAAQAL KSFIEHYPGR VLIAADSPGR REALLEVLQA AELRPEVVAS
FNDFLPSPIG GRWPEGSDGS KAAGKSSSKN ALSPAPLPKG EGLSRFAITV APLDDGFALS
EPALAVLTER QLFPERAGQA RRTRRAGREP EAIIRDLGEL TEGAPIVHED HGVGRYRGLI
AMDVGGMPGE FLEIEYAKGD RLYVPVAQLH LISRYSGASP ETAPLHSLGG EQWAKAKRKA
AEKVRDVAAE LLEIQARRRA RAGLALEIDR SMYEPFAAGF PFEETADQQA AIEATLRDLQ
SSQPMDRVVC GDVGFGKTEV ALRAAFAAAS GGKQVAVLVP TTLLAEQHYR NFRDRFADYP
LRVEVLSRFK STKEIKAELD KVAEGTIDVI IGTHRLLQPD VKFKDLGLVI VDEEQRFGVR
QKEALKAMRA NVHLLTLTAT PIPRTLNMAM AGLRDLSIIA TPPPNRLAVK TFITAWDNAQ
LREAFQRELS RGGQLYFLHN DVESMGRMQR ELSELVPEAR IGMAHGQMPE RELERVMLDF
QKQRFNVLLA STIIESGIDI PNANTIIINR ADRFGLAQLH QLRGRVGRSH HRAYAYLLVP
DKRSITPDAQ KRLDAIASMD ELGAGFTLAT HDLEIRGAGE LLGEDQSGQM AEIGFSLYTE
LLERAVRSIR SGKLPDLDAG EEPRGADVEL HVPALIPEDY LPDVHTRLTL YKRISSARDS
ERLRELQVEM IDRFGLLPDP VKHLFAIAEL KLQANELGIR KLELGENGGR IVFDSKPNID
PMVVIQLIQK QPKLYQMDGP DKLRIKHPLP ESADRFNAAR ALLTTLHPAN A
//
