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Database: UniProt
Entry: A0A0B3BZ25_9PSED
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ID   A0A0B3BZ25_9PSED        Unreviewed;      1147 AA.
AC   A0A0B3BZ25;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   24-JAN-2024, entry version 43.
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=PT85_01720 {ECO:0000313|EMBL:KHO66316.1};
OS   Pseudomonas flexibilis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=706570 {ECO:0000313|EMBL:KHO66316.1, ECO:0000313|Proteomes:UP000030980};
RN   [1] {ECO:0000313|EMBL:KHO66316.1, ECO:0000313|Proteomes:UP000030980}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 14085 {ECO:0000313|EMBL:KHO66316.1,
RC   ECO:0000313|Proteomes:UP000030980};
RA   Shin S.-K., Yi H.;
RT   "Genome sequence of Pseudomonas tuomuerensis JCM 14085.";
RL   Submitted (NOV-2014) 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:KHO66316.1}.
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DR   EMBL; JTAK01000001; KHO66316.1; -; Genomic_DNA.
DR   RefSeq; WP_039605756.1; NZ_JTAK01000001.1.
DR   AlphaFoldDB; A0A0B3BZ25; -.
DR   STRING; 706570.PT85_01720; -.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000030980; 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; 3.40.50.11140; -; 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; 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:UP000030980}.
FT   DOMAIN          615..776
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          797..951
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1147 AA;  129031 MW;  9C889354A84A5C0B CRC64;
     MSVLRLPTLP SAAGKQHWGN LPGAALSLAI AEAASAAGRR LTLLLTPDSQ SAERLKEELA
     FFAPTLPVLH FPDWETLPYD QFSPHQDIIS QRIATLYRLP EIRHGILVVP VNTALHRLAP
     TRFLLGRSLV LDVGQRLDVE DMRGRLEAAG YRCVETVYEH GEFAVRGALL DLFPMGSDTP
     YRIDLFDDEI ETLRTFDPES QRSVDKVESI RLLPGREFPL DKKSVTDFRG RFREHFDVDF
     RRCPIYQDLS TGITPAGIEY YLPLFFEETS TLFDYLPEDT QVFSLPGIEQ AAEQFWLDVR
     NRHEDRRLDP ERPVLPPAEL FVPVEDCFAR LKRWPRVVVD SQDLQTGVGR ERFPARPLPD
     LALQAKAAEP LAALRRFLEE YSGRVLFSAE TAGRREALLE LLGRLKLKPR EVNGWVDFLA
     SGERLNICIA PLDEGLLLDD LALIPESPLF GQRVMQRRRR EKTRDHGDNV IKHLTELREG
     APVVHIDHGV GRYQGLVTLD YDGQSNEFLV LQYADDAKLY VPVTSLHLIA RYTGSDEALA
     PLHKLGSEQW QKAKRKAAEQ VRDVAAELLD IYARRAARKG YAFKDPAADY ETFSAAFPFE
     ETVDQEAAIE AVRHDMLASK PMDRLVCGDV GFGKTEVAMR AAFIAVHSGK QVAVLVPTTL
     LAEQHYNSFR DRFADWPVRV EVMSRFKSAK EIADAAALLA EGKVDIVIGT HRLLQNDIRF
     KNLGLLIIDE EHRFGVRQKE QLKALRSEVD ILTLTATPIP RTLNMAVAGM RDLSIIATPP
     ARRLSVRTFV MERQPAVIKE ALLRELLRGG QVYFLHNDVK TIEKCAAELA ALVPEARIAI
     GHGQMPERQL EQVMSDFYHK RFNVLVASTI IETGIDVPTA NTIIIERADK FGLAQLHQLR
     GRVGRSHHQA YAYLLTPPRR QMTEDAQMRL EAIANAQDLG AGFVLATHDL EIRGAGELLG
     EGQSGQIQAV GFTLYMEMLE RAVKAIQKGE QPNLDQPLAS GTEINLRVPA LIPDDYLPDV
     HGRLILYKRI ASAPDEDALQ ELQVEMIDRF GLLPEPAKHL IRQTLLKLQA EKLGIQKIDA
     GPQGGRLEFS ANTCVDPLTL IKLIQSQPNR YKFEGATLFK FQVPMERPEE RFNTLEALLE
     RLAPQPA
//
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