ID A0A2T0S3V4_9ACTN Unreviewed; 1212 AA.
AC A0A2T0S3V4;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=CLV70_109246 {ECO:0000313|EMBL:PRY28089.1};
OS Pseudosporangium ferrugineum.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Pseudosporangium.
OX NCBI_TaxID=439699 {ECO:0000313|EMBL:PRY28089.1, ECO:0000313|Proteomes:UP000239209};
RN [1] {ECO:0000313|EMBL:PRY28089.1, ECO:0000313|Proteomes:UP000239209}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45348 {ECO:0000313|EMBL:PRY28089.1,
RC ECO:0000313|Proteomes:UP000239209};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (MAR-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}.
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:PRY28089.1}.
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DR EMBL; PVZG01000009; PRY28089.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T0S3V4; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000239209; 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; 3.40.50.11180; -; 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}; Reference proteome {ECO:0000313|Proteomes:UP000239209}.
FT DOMAIN 670..831
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 849..1006
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1212 AA; 132465 MW; 8F134103BCBF2ACA CRC64;
MQLSGLVPAA LRDRGLARAR DLARKGGVDS DALDLTAPAS LRPFVVAAVA GPAGIGGAGR
PVLAVTATSR EADDLADALG CLISADGVAV YPSWETLPHE RLSPRSDTVG RRLAVLRRLA
HPAEAGSAPL QVVVAPVRSL LQPQLKGLGD LEPVELRPGG AAELEQVARR LSDMAYARVD
LVTKRGEFAV RGGILDVFPP TDEHPSRVEF WGDEVEEIRT FAVADQRTID PAERLWAPPC
RELLLTPQVR ARAAELSEQH PELAEILDKL AEGIPVEGME SLAPALLQGT DSMELLIDCM
PAGTHVLLCD PERIRTRAHD LTRTSDEFLE AGWAAAAVGG QAPIDVGAAA FRTLGDVRAH
AATLHQPWWT VSPFGLADAD EQPDAGLPWL ETPSVEVSPD AGDAVSLKAQ PVPLYHGDTA
RLAADLRQWT GDRWAVALVF EGHGTAQRAT ELLRDAGLGV TPVDSIATAV EPGQLLVTCG
GLNHGFVDEV SRLAVITGND ISGGRGASTK DMRKMPSRRR NTIDPLELKP GDFVVHEQHG
IGRYVELVQR TVNGADREYL VIEYAPSKRG QPGDRLFVPT DQLDQLSRYV GGESPTLHKM
GGSDWQKSKA RARKAVREIA AQLIQLYAAR QASQGHAFGP DTPWQRELED AFPYTETPDQ
LAAIHEVKHD MELAVPMDRL ICGDVGYGKT EIAVRAAFKA VQDGKQVAIL VPTTLLVQQH
YNTFAERMSQ FPVNIKQLSR FQTPKEAALA LEQAADGTAD IVIGTHRLLA NSTRFKNLGL
IIVDEEQRFG VEHKEQLKAL RASVDVLTMS ATPIPRTLEM AITGIREMST IATPPEERHP
VLTFVGAQDD KQVAAAIHRE LLRDGQVFYL HNRVESIDRA ARKLRELVPE ARIAVAHGQM
SEEQLEKVMV GFWEKEFDVL VCTTIVESGI DIANANTLIV ERADLLGLSQ LHQIRGRVGR
GRERAYAYFL YPREKPLTEQ AHERLATIAQ HTELGAGMYV AMKDLEIRGA GNLLGGEQSG
HIEGVGFDLY VRMVGEAVQA FKGERPEEEP EVKVDLPIDA HLPTDYIAVE RLRLEMYRKL
AEARDGVRLD EVVAEMTDRY GEPPEQVVNL IAVARFRLVA RAYGLTDVSM QGKHLRFSPL
PLPDSKQLRL KRYHPDSVYK TTNDQVSVPR PATRRVGGEP LRDQALLQWC TQLLKDVLGD
IPAPVPGVAS GA
//
