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Database: UniProt
Entry: S7HVA9_VIBFL
LinkDB: S7HVA9_VIBFL
Original site: S7HVA9_VIBFL 
ID   S7HVA9_VIBFL            Unreviewed;      1153 AA.
AC   S7HVA9;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 48.
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=L910_2835 {ECO:0000313|EMBL:EPP19608.1};
OS   Vibrio fluvialis PG41.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=1336752 {ECO:0000313|EMBL:EPP19608.1, ECO:0000313|Proteomes:UP000014854};
RN   [1] {ECO:0000313|EMBL:EPP19608.1, ECO:0000313|Proteomes:UP000014854}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PG41 {ECO:0000313|EMBL:EPP19608.1,
RC   ECO:0000313|Proteomes:UP000014854};
RX   PubMed=23895343; DOI=10.1186/1757-4749-5-20;
RA   Khatri I., Mahajan S., Dureja C., Subramanian S., Raychaudhuri S.;
RT   "Evidence of a new metabolic capacity in an emerging diarrheal pathogen:
RT   lessons from the draft genomes of Vibrio fluvialis strains PG41 and
RT   I21563.";
RL   Gut Pathog. 5:20-20(2013).
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:EPP19608.1}.
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DR   EMBL; ASXS01000029; EPP19608.1; -; Genomic_DNA.
DR   RefSeq; WP_020332321.1; NZ_ASXS01000029.1.
DR   AlphaFoldDB; S7HVA9; -.
DR   PATRIC; fig|1336752.4.peg.4511; -.
DR   Proteomes; UP000014854; 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   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; 2.
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          620..780
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          797..954
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1153 AA;  129970 MW;  9AC972BF4098DF6E CRC64;
     MSNTGCSELK NIQNVCKKGI GGLCGSSVSL AISEIFSDLV KSSIIVCKDN NEASEILSQL
     RFFSAVNEDQ IIHIPEIEVL PYDTESPNAS VSALRISAFN KLASMNGDKR LVVTTAAAAT
     QYIMDFDYWI NTQINLKVNE QVSIQQVEEK LIAVGYEKAN LEVTKPGEFT VINNILDIYP
     LSHDKPARIA VSDSDHITSI KTFDSITQKS IATLESIQIL QAREVPLDKP SSILFRKNFR
     KEFSSATGDV TYSQISAGET PEGIEFYTYL YDQHTTLMEK LSERQFNVFL TSGFSSHYSQ
     VISTAKERYE ELKDDKKRKI LPPQKVWLNS ESLINCISRT NSIFLSEDKK GFDTVYDTEN
     TGFSKKHSLS DIMSMLSPYV KKAEKVVFVL HSEARSDQIV AISRLLRMKS LFAKKWDEAK
     NAPEKAVIVY SNVNTGYFDN THKILVVTEK EIFGMPIQAK IEDESEVVDE DNNHQFIKDL
     EIDDLVVHTH YGIGKYKGLK QLSLETDGNE YFTIEYQDSA LAFVQISDLH LVNKYNGLNP
     ESVKIDRLDE KGSSWKDEIA KVVDDIEGTA LTLIEAQIQR EKMVGIQIPE PKADYYRFCR
     EFPYQATNDQ LKAVEDIKND LVSARPMDRL VAGDVGFGKT EVALRASMIV ASAGAQVVLV
     APSTILAQQH YRSFKARFES FGINVVELTS GTQKIEKEII QQIENGEAHI IIGTHKAIKR
     AIDYHNLALV IIDEEHRFGV NDKENIRSRF SGINILAMTA TPIPRTLNMS LSGIKDTSTL
     RQPPANRLNI RTIVSEFNDQ LIVEAIKREM LRNGQLFFLH NNTTSIYARA EYLKNLFPDL
     RIGIAHGKMH ALEVEAVMSA FYKHEFDMLI ATTIIENGID VPNANTILIE NANAFGLAAL
     HQLRGRVGRS TRQGYAYLLT SGNNITEEGM KRLNAMEKTS KIGEGYKLAN HDLEIRGAGE
     ILGESQSGHI SKMGYSLYHF ILNKCIEILK SNNFESLSDF QLQSLKEGDE SINIDVGVKY
     SIPENYIPHP NLRLYYYRRI SMAEKVSEVN DVFQEMEDRF GKSPYLVGNL IFITKLKMAA
     KRLKIVGIHA NEDGGKIIFS RSVKDRDSIL NIFVKDPENM QISVVHGEKA MIHFNKKLPN
     TKDRVGYIRQ ILL
//
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