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Database: UniProt
Entry: W6TP34_9SPHI
LinkDB: W6TP34_9SPHI
Original site: W6TP34_9SPHI 
ID   W6TP34_9SPHI            Unreviewed;      1140 AA.
AC   W6TP34;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 45.
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=N824_11320 {ECO:0000313|EMBL:ETZ19324.1};
OS   Pedobacter sp. V48.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=509635 {ECO:0000313|EMBL:ETZ19324.1, ECO:0000313|Proteomes:UP000019145};
RN   [1] {ECO:0000313|EMBL:ETZ19324.1, ECO:0000313|Proteomes:UP000019145}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=V48 {ECO:0000313|EMBL:ETZ19324.1,
RC   ECO:0000313|Proteomes:UP000019145};
RX   PubMed=24578271;
RA   Bitzer A.S., Garbeva P., Silby M.W.;
RT   "Draft Genome Sequence of Pedobacter sp. Strain V48, Isolated from a
RT   Coastal Sand Dune in the Netherlands.";
RL   Genome Announc. 2:e00094-e00014(2014).
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:ETZ19324.1}.
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DR   EMBL; AWRU01000034; ETZ19324.1; -; Genomic_DNA.
DR   AlphaFoldDB; W6TP34; -.
DR   STRING; 509635.N824_11320; -.
DR   PATRIC; fig|509635.5.peg.5720; -.
DR   eggNOG; COG1197; Bacteria.
DR   Proteomes; UP000019145; 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}.
FT   DOMAIN          602..763
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          783..938
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1140 AA;  129973 MW;  C64313C51216CDED CRC64;
     MLSSFYLRLI NRDFVTSKAN HKSYICIVNI RDLINRYKTD ERIVALAKAL NAGKGNKLQL
     KGLVGSADAT IATATYFLLH KPILFVLPDR EEASYFLADL ESILDKEVLL FPSSFRKAFE
     FTQVDTANVL ARAEVLNELN HHSEYGKIVV TYPEALAEKV INRSLLEKNT LEISLGAKLG
     IDFINEFLID YDFNRTDFVY EPGQFSIRGG IVDIFSFSHD LPYRIEFFGD EIESIRTFEI
     ESQLSVEDVK TFTIIPNVQS KYLTESNISL LDYIEKDTQL WFRDVEFTLD IVKSGYKKAV
     ELWKALPVKE KAENQDWIDP KFAFTDEKMI ADMLQDFLLV EFGKQFFYKT DQVFQFETKP
     QPSFNKDFNL LIHNIKENEK QGIHNFIFSS STKQTERLYA ILDDIDKTAK FTPVNIPLRE
     GFVDAQQHVA FYTDHQIFDR FYKYKLKRGY QRSQAITLKE LRDLKPGDFV THIDHGIGKY
     AGLEKVEVNG KTQEMIRLVY ADNDLLYVNI NSLNRIAKYS GKDGTAPKMN KLGTEAWDKL
     KKTTKKKVKD IARDLIKLYA LRKSQVGTAF DPDGYLETEL EASFIYEDTP DQEKATNDVK
     KDMEAPHPMD RLVCGDVGFG KTEIAIRAAF KAVANGKQAA VLVPTTILAL QHFKTFSGRL
     KGFPCNVDYI NRFKTNKQIK DTLAAVVDGK VDIIIGTHRL LSKDVKFKDL GIMIIDEEQK
     FGVASKEKLK ALRVNVDTLT LTATPIPRTL HFSLMGARDL SIMSTPPPNR QAVNTELHVF
     NDKLIQEAVQ FELDRGGQVF FIHNRVNDLP QLGGLIQRLV PKARIGIAHG QLDGDALEDV
     MLDFINGEKD VLVATTIIEA GLDIPNANTI IINHAHMFGL SDLHQMRGRV GRSNKKAFCY
     LLSPPLSTLT SEARKRLSAI EEFSDLGSGF NIAMRDLDIR GSGNLLGAEQ SGFIAEIGFE
     MYHKILDEAI QELKADEFKG LFKDEPERPF VTFTQIDTDL ELYIPDDYVT NITERYNLYT
     ELSKIENETQ LKAFELSLKD RFGPVPRPVK TMLNVLRLQW VAKKLAFEKI TFKKGTLRGY
     FITDKQSSFF DSTMFNKILH FAQIHPRLCN LKEVKDSLRI AFDNLNTVDE AVEMLEMVVN
//
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