ID A0A3G8YJ05_9DEIO Unreviewed; 1043 AA.
AC A0A3G8YJ05;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 20.
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=EHF33_00460 {ECO:0000313|EMBL:AZI41411.1};
OS Deinococcus psychrotolerans.
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=2489213 {ECO:0000313|EMBL:AZI41411.1, ECO:0000313|Proteomes:UP000276417};
RN [1] {ECO:0000313|EMBL:AZI41411.1, ECO:0000313|Proteomes:UP000276417}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S14-83T {ECO:0000313|EMBL:AZI41411.1,
RC ECO:0000313|Proteomes:UP000276417};
RA Tian J.;
RT "Deinococcus shelandsis sp. nov., isolated from South Shetland Islands soil
RT of Antarctica.";
RL Submitted (NOV-2018) 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}.
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DR EMBL; CP034183; AZI41411.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3G8YJ05; -.
DR KEGG; dph:EHF33_00460; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000276417; Chromosome 1.
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; 3.40.50.300; 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 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; 3.
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};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:AZI41411.1};
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 506..684
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 705..862
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1043 AA; 115559 MW; 92CB22121B9F94CB CRC64;
MTLAVPSLSK LLPTVPVGNL ILLPQVARAA LFAAHAGPAV LLTTPDRLPL YEGAGKLGAP
ISVNPGLREW DDKKEHVVLD IQTAMDLFPA KPEDHALMFK VGRQYPREEL LSRLEKLGYE
RLIDGRLDEI GFVLRGDTLD LYLTADPQED QIVALRAEFF GDELDTLREL SQDGFPSEKM
PQFTLAPTTE YLSEVKWDAT RLELLAGRIF LDAPEFYAST LGPMTDVLWA HLLTREVSSF
GRAPLILEDF TLDLVTLPYY RARLGELARD VDEWRAAGYR VLLLVRHDRT ATYLAEKLLG
NKEPKWLNLP RLEAGELGFL RSSGEGGFVL EQARMVVLTE DLIYGFQGGS ALRGKKLSGK
PVTDALGLAV GDYLIHPEHG IGQFQGLQTR TVLGVTRDYL NISYKNEASL AVPIELLPTL
RRHPGTTDDP PALSSLDKSA WAKAKERARK NAEEVASKLL VQYAARQVTP GNSFAPNPEW
ESQIEKNFEF ELTADQKTAL KETLKDLEAP NPADRLISGD VGFGKTEVAL RAAHRVVGAG
MQVAVLVPTT LLAEQHTSVF VERFKDLPVR VEGLSRFTGD KQAKSILGDL AQGKVDIIIG
THRLLSSDIV FKNLGLIIVD EEHRFGVSQK EKLRAMRGLP EINKEGKIEI PEGVKAIDTL
ALSATPIPRT LYMSMVGLRD MSSIQTPPKG RKPIQTILAP FDPVTVRDAI VSEIERGGKV
FYIHDRIASI GARSLYLRNL VPEARIGVAH GRMNEEELEE IMLGFEEGAF DVLVSTTIVE
TGLDIPEANT ILIERADRLG LAQLYQLRGR VGRRSTDAYA YLFFPPRMTE NASRRLWAIA
DLQDLGSGHL LAEKDMEIRG VGNILGEEQH GHVQAVSIDV YTEMLAEAVA KLKGEPLKAA
PTVSVDLPIS ARLNAEYFGN DEEARISTYG RLSEARTLQA ISRVERDLRK KFGPPSPEVQ
NFIDLAKLRL TSLARRVLSI GETMTDLQIT FAYKALDYDA GGLKKFPHKT EVTTFPPSLK
IQKRGIRVDD YARTLIDVLG YFG
//
