ID A0A1Q5PZ17_9ACTO Unreviewed; 1192 AA.
AC A0A1Q5PZ17;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=BSZ40_00935 {ECO:0000313|EMBL:OKL52702.1};
OS Buchananella hordeovulneris.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Buchananella.
OX NCBI_TaxID=52770 {ECO:0000313|EMBL:OKL52702.1, ECO:0000313|Proteomes:UP000185612};
RN [1] {ECO:0000313|Proteomes:UP000185612}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20732 {ECO:0000313|Proteomes:UP000185612};
RA Meng X.;
RL Submitted (DEC-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:OKL52702.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MQVS01000001; OKL52702.1; -; Genomic_DNA.
DR RefSeq; WP_073822315.1; NZ_MQVS01000001.1.
DR AlphaFoldDB; A0A1Q5PZ17; -.
DR STRING; 52770.BSZ40_00935; -.
DR InParanoid; A0A1Q5PZ17; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000185612; 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:UP000185612}.
FT DOMAIN 662..823
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 832..998
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 374..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1192 AA; 128761 MW; 07E2B9EFA43A8B60 CRC64;
MRLSGLTPLL ASDPAVAAPR AALHSPEDRT FSVPLALRGA LLAELAAPTD GAAGRPLVVL
TATSREAEDL AAVLADYLPA AWADQIALFP AWETLPHERL SPRSDTMARR SAVARRLAHP
QSGPLAGPIR VLLAPIRAAA APIVAGLGER EPLQLQVGQS CDLAAAVTQL AQTGYRRVDM
VERRGEFAVR GGILDVFVPT DAHPVRVEFF GDEVEEIRSF TVADQRTFAP APHGVWAPVC
REIPLDAAVR QRAAALAGQL PGAADLLAQI ADGLAPEGME SLLPVLVDKL DNLLDLVAPD
ALVLLHEPER IRTRLESLLA TSEEFLVAAW SSAAAGGSAP LDLRGGSFLP LPQIRARAQA
RALPCWQVTS LPSLPQADNP VGDAHPAAGG TDTPAAAQDL PPYRGNIPAL FADVKRWLAD
GQRVVVTTQG PGMARRVVEQ FTAAALPATL AEQLTAAPAP ASLTVTTAAQ LHGLTSPAAG
VVLIGEADIT GRAAREQARD RAVPARRKNA VDPLQLQAGD YVVHEVHGVG RFVELISRTV
GHGTKAGKRE YLVIEYAPSK RGQPGDRLFV PTDSLDQVTK YVGGDAPALS RMGGADWAKT
KNKARAAVKD IAKELLRIYA ARQATKGHAF SPDTPWQLEL EQSFAHVETP DQLATMDEIK
ADMEREVPMD RLLCGDVGYG KTELAVRAAF KAVQDGKQVA VLVPTTLLVS QHLETFTQRY
ANFPVTVKAL SRFQSDKEAQ AVKDGTRDGS VDVVIGTHRL LTGEVRFKDL GLVIIDEEQR
FGVEHKETLK ALRANVDVLA MSATPIPRTL EMAVTGIREM STLATPPEER HPVLTYVGAY
EERQVAAAIR RELLRDGQVF FIHNRVQSIM DTAAKLTRLV PEARIAVAHG QMSEQQLERV
IVDFWNHEFD VLVCTTIVET GLDISNANTL IVDQASKMGL SQLHQLRGRV GRSRERAYAY
FLYPASPALT ETAYERLRTI AAHTDLGAGM QVAMKDLEIR GAGNLLGGEQ SGHIAGVGFD
LYVRMVADAV AEYRGERERP EADVRIDLPV DAHVPESYVS HDRLRLEIYT KISAASDETA
LEAVREELVD RYGPVPVQVE RLLVLARLRA AARALGLAEL VVQAKHLRLA PLEVPDSLQL
RLRRLYPGSA VKPAIRAVNV PLPRPRALGT TAVDDDELLA WVGQVLADIQ QP
//
