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Database: UniProt
Entry: A0A1H2PTN9_9BURK
LinkDB: A0A1H2PTN9_9BURK
Original site: A0A1H2PTN9_9BURK 
ID   A0A1H2PTN9_9BURK        Unreviewed;      1201 AA.
AC   A0A1H2PTN9;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 23.
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=SAMN05216551_11224 {ECO:0000313|EMBL:SDV50488.1};
OS   Chitinasiproducens palmae.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Chitinasiproducens.
OX   NCBI_TaxID=1770053 {ECO:0000313|EMBL:SDV50488.1, ECO:0000313|Proteomes:UP000243719};
RN   [1] {ECO:0000313|Proteomes:UP000243719}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JS23 {ECO:0000313|Proteomes:UP000243719};
RA   Varghese N., Submissions S.;
RL   Submitted (SEP-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}.
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DR   EMBL; FNLO01000012; SDV50488.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H2PTN9; -.
DR   STRING; 1770053.SAMN05216551_11224; -.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000243719; 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; 3.40.50.11140; -; 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:UP000243719}.
FT   DOMAIN          665..826
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          847..1001
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          357..398
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        357..372
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1201 AA;  132282 MW;  9FDF0158890A2E56 CRC64;
     MSDKKPSSSA TVSLVKEGHR HVVDGIAGSA DALVIARYLQ SHRAQLAMLA VVCANASDAQ
     RLLAEIAYFA PQARVRVLPD WETLPYDTFS PHQDLVSERL ATLHDLSAGR CDVLLVPAST
     ALYRMPPAAF MAAYTFEFAQ NQKLDEAKLR AQLTLASYEH VNQVVRPGEY CVRGSLIDLF
     PMGSALPYRI DLFDDQVDSI RAFDPDSQRS LYPVKDIRLL PGREFPFDEA ARTAFRKRWR
     ETFEGDPSRA TIYRDAGNGV PSGGIEYYLP LFFDETATLF DYLPAGSQLV TVGDLDEAMS
     RFMRDTEQRY GFLSHDSERP ILDPSRLFLS SEAFFARARG LARLVLRRDV PATDATNATD
     AANATGGTDD SAASATAAGA AHADRPSGEA ASARAPRKHA PVALPLPSLS VDRRSDDPLA
     ALRGFTHGAY RVLLAAESAG RRETIAQLLI DNRMPAAPVD DFASFLASDV AFGLGVAPLA
     TGFVLPDARV AVVTETELYG ALARRTQRRR QEQTSSVDEM VRDLSELKIG DPIVHSQHGI
     GRYLGLATMD LGEGDTEFLH LEYAGPSKLY VPVAHLHLIS RYSGADPDTA PLHALGSGQW
     DKARRRAAKH IRDTAAELLN LYARRAARTG HAFELSPRDY ETFAESFGFE ETPDQAAAIN
     AVINDMTSGQ PMDRLVCGDV GFGKTEVALR AAFIAVLGGK QVALLCPTTL LAEQHFQTFT
     DRFSQWPVRI AELSRFKSGK ETTQAVKALA SGDVDIVIGT HKLLSQDVVF KRLGLVIIDE
     EHRFGVRQKE TLKALRAEVD ILTLTATPIP RTLGMALEGL REFSVIATAP QKRLAIKTFV
     RREDDSVIRE AMLRELKRGG QVYFLHNEVE TIENRRTMLE ALVPEARIVV AHGQMNEREL
     ERVMRDFIGR RANVLLCTTI IETGIDVPNA NTILIHRSDR FGLAQLHQLR GRVGRSHHQA
     YAYLLVRDPE TLTSQATRRL EAIQQMEELG AGFYLAMHDL EIRGAGEVLG DKQSGEIHEI
     GFQLYTDMLA DAVDALRAGR EPDLTAPLAA TTEINLHVPA ILPADYCGDV QERLTLYKRL
     ASCTTFDAVD AVHEELIDRF GKLPPQAVAL VETHRLRLMA KPLGVAKIDA SEVAVGIQFV
     PDPPIDAMRI IEMVQKNRHV KLAGQDRLRL EIPTPDLPAR IALLKDTLRQ LGRAETAGAA
     R
//
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