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Entry: A0A2N8ZCS9_9VIBR
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ID   A0A2N8ZCS9_9VIBR        Unreviewed;      1152 AA.
AC   A0A2N8ZCS9;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-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   ECO:0000313|EMBL:SON49709.1};
GN   ORFNames=VTAP4600_A1730 {ECO:0000313|EMBL:SON49709.1};
OS   Vibrio tapetis subsp. tapetis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=1671868 {ECO:0000313|EMBL:SON49709.1, ECO:0000313|Proteomes:UP000235828};
RN   [1] {ECO:0000313|EMBL:SON49709.1, ECO:0000313|Proteomes:UP000235828}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Vibrio tapetis CECT4600 {ECO:0000313|EMBL:SON49709.1};
RA   Banno H., Chua N.-H.;
RL   Submitted (OCT-2017) 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; LT960611; SON49709.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N8ZCS9; -.
DR   KEGG; vta:A1730; -.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000235828; Chromosome a.
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:UP000235828}.
FT   DOMAIN          618..779
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          801..954
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1152 AA;  129827 MW;  61B068837CC8B1CF CRC64;
     MPKSSLLSLA LPTKAGDKKH VGNLTGASLS IAVAELADAH KGHTLLVVPD PQMALKLSGE
     VEQFTEQDVQ LFPDWETLPY DNFSPHQDII SDRIAHLYRL PSQKNGITVV PISTLLQKQS
     PRDFLLQHTL MVKAGDRYNI ETLRIQLDKS GYRNVDQVFG PGEYASRGSI IDLYPTGSTD
     PYRIDFFDDE IDSIRTFDAE SQRSIEDIGH IRLLPAHEFP TTETAIEAFR SRWRQRFEAR
     REPESVYMQV SKGTWPSGIE YWQPLFFDET ETLFDYIADN TLLISIGDLE PSIDHFLADV
     DHRFEQRKVD PLRPLLPPEE LWLKKDELFS QLKVMPQARL NVKKIEEKAG RSNPAIAPLP
     ALHAQHQNKE PLAALRQFIE QFEGKIVFSV ESEGRREALL ELLQGIKLKP TATDSLTKAS
     KGKARVSLIL GVAEHGFIHR DPNIALICES DLLGDRVIQR RKKDRKAVNS DTVIRHLAEL
     KPGQPVVHLD HGIGRYIGLQ TLEAGGLVTE YVTLEYQNEA KLYVPVASLN LISRYSGGAE
     DKAPIHKLGG ETWVKARRKA AEKVRDVAAE LLDVYAKREL KPGHKFKLDR GQYATFKSSF
     PFEETDDQAM AINAVMSDMC QAKAMDRLVC GDVGFGKTEV AMRAAFIATD NNKQVAVLVP
     TTLLAQQHFE NFRDRFANLP IRVEVLSRFK SAKEQKQILA DLSEGKVDII IGTHKLLQDD
     IKFRDLGLLV VDEEHRFGVR QKEKVKAMRA DVDILTLTAT PIPRTLNMAM SGMRDLSIIA
     TPPARRLAIK TFVRESEDSV VREAILREIM RGGQVYFLHN QVETIEKVAA DLEKLIPEAR
     VTVAHGQMRE RELERVMNDF YHQRFNLLVC TTIIETGIDV PTANTIIMDR ADNLGLAQLH
     QLRGRVGRSH HQAYAYLLTP HPKAMSKDAI KRLDAIASLE DLGAGFTLAT HDLEIRGAGE
     LLGDDQSGQI HSVGFTLYME MLEQAVEALK EGKEPSLDEL LRDQTEVELR LPALLPDDYI
     PDVNMRLSMY KRIASVSNLN ELAEMKVELI DRFGPLPDAT KNLLSVSEIK LQAGQLHVKK
     LEAHPKGGFV EFYPTADINP AYLVKLLQST PQKFGMEGPT KLKFTVPLTD RRERIRFIND
     LLEQFAQNRL PA
//
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