ID A0A1F1UVS0_9CORY Unreviewed; 1209 AA.
AC A0A1F1UVS0;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
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=HMPREF3171_04465 {ECO:0000313|EMBL:OFT30199.1};
OS Corynebacterium sp. HMSC08F01.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1581139 {ECO:0000313|EMBL:OFT30199.1, ECO:0000313|Proteomes:UP000176366};
RN [1] {ECO:0000313|EMBL:OFT30199.1, ECO:0000313|Proteomes:UP000176366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMSC08F01 {ECO:0000313|EMBL:OFT30199.1,
RC ECO:0000313|Proteomes:UP000176366};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-2016) 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:OFT30199.1}.
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DR EMBL; LWNT01000047; OFT30199.1; -; Genomic_DNA.
DR RefSeq; WP_070483234.1; NZ_KV789298.1.
DR AlphaFoldDB; A0A1F1UVS0; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000176366; 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; 3.40.50.11180; -; 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 644..805
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 823..980
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1209 AA; 132083 MW; 07C82A7A29CCB6D2 CRC64;
MTDNTPPVLG GLLTQALTDP KLKGLVTHVG EDSLHITGID QARSWTAGAI ARETPVLLVT
ATGHEAEDLT AELKAMLGDD KVAQFPAYET LPHERLSPAA DIVGRRAKVL WDMPRVIVAA
ARAVCQPVLP AIEPIRVAVD QEADFEDLTQ QLVHFAYNHV DMVAGRGEFA TRGGIIDVFP
TTAQNPVRIE FWGDEVTDIR SFAVADQRTI EEVGAVELFP ARQLLIDDTV AAKADDLARK
FPSNPTLSSL LARISEKQPA DGMEAIIPAL TDKTYSVLPE LMPAGSVVLV TNPEKVRTRI
ADLEATDREF LEAGWEAAAM GAEGPVAVEG LDVSASSYRS FESLEVSASK AGNAWWTFAP
PGMFAADDAS TLPLEFEAAP APKGDPKQIE QLYATLKLHV TQNHGKAAYV APAKGAIDRM
AERLREHGVS ARVATPGLEP VDGAVTLYQA LSHAGLVFGG PNLVVITETD LTGNRVGDIA
GAKRRAPRRR NRVDPLALQP GDFVVHDTHG IGKFVKMAER TIKAGDEASR REYIVLEYQP
AKRGQPGDQL WVPMESLDLL SKYTGGEKPS LSKMGGSDWK STKRKARAAV REIAGELVEL
YAKRQAAPGH AFAPDTPWQL EMEDAFPFVE TEDQLNAIEA VKEDMEKPTP MDRVIVGDVG
FGKTEVAVRA AFKAVQDGKQ VAVLVPTTLL AQQHYSTFTQ RMDGFGVEVR ELSRFTSTTD
SKKILAGLAD GSVDIVIGTH RLLQTGVQWK NLGLIIVDEE QRFGVEHKEH IKALKSHVDV
LTMTATPIPR TLEMSLTGIR EMTSITTAPE DRHPVLTYVG PQEDKQVAAA IRRELLRDGQ
VFYIHNKVSD IEKTARQLRE LVPEARVVVA HGQMSEQVLE QTVQGFWNRE YDVMVCTTIV
ETGLDIANAN TLIVENAQNM GLSQLHQLRG RVGRSRERAY AYFLYPKDKT LTETSYDRLA
TIAQNNDLGA GMAVAQKDLE MRGAGNVLGA EQSGHIAGVG FDMYVRLVSE AVETFKGLMS
GKPIDATDKG PKEIRVDLPV DAHIPETYIN SERLRLEVYR KLAEARDDDA LTAAADDMID
RFGTLPIEVE RLMAVARLRN QARAVGVSEI LTQGTRIKLH PVELPDSKQV RLKRLYPGAN
FRAAAKALQV PMPKEGGAKR ALNAPNLRDM ELLQWVADFM TDVLDAPKIA VAGPGAEEAP
KKKVFSVSE
//
