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Database: UniProt
Entry: V4N5E4_9CAUL
LinkDB: V4N5E4_9CAUL
Original site: V4N5E4_9CAUL 
ID   V4N5E4_9CAUL            Unreviewed;      1130 AA.
AC   V4N5E4;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 44.
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=AEYBE204_18445 {ECO:0000313|EMBL:ESQ77062.1};
OS   Asticcacaulis sp. YBE204.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Asticcacaulis.
OX   NCBI_TaxID=1282363 {ECO:0000313|EMBL:ESQ77062.1, ECO:0000313|Proteomes:UP000017808};
RN   [1] {ECO:0000313|EMBL:ESQ77062.1, ECO:0000313|Proteomes:UP000017808}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YBE204 {ECO:0000313|EMBL:ESQ77062.1,
RC   ECO:0000313|Proteomes:UP000017808};
RX   PubMed=24463524; DOI=10.1038/nature12900;
RA   Jiang C., Brown P.J., Ducret A., Brun Y.V.;
RT   "Sequential evolution of bacterial morphology by co-option of a
RT   developmental regulator.";
RL   Nature 506:489-493(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:ESQ77062.1}.
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DR   EMBL; AWGF01000020; ESQ77062.1; -; Genomic_DNA.
DR   AlphaFoldDB; V4N5E4; -.
DR   STRING; 1282363.AEYBE204_18445; -.
DR   PATRIC; fig|1282363.3.peg.3582; -.
DR   Proteomes; UP000017808; 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}; Reference proteome {ECO:0000313|Proteomes:UP000017808}.
FT   DOMAIN          598..759
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          780..934
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1130 AA;  125296 MW;  F013A177B5AEBA5F CRC64;
     MFVARDYARM NGVAEELGFY APDLGIIRFP AWDCLPYDRV SPTAGLIAQR MHGLTRLQAL
     SGAKPAKPVL ILTTASALSQ KVPPREAMKD SFLSLRPGQS VDTNELEAYF TRNGYNRVST
     VSERGEFAVR GGIVDVFSPS QSEPVRLDFF GDTLETIRSF DPETQRSLKQ VTQIDFMAVS
     EILLDEKSIS RFRQGYLENF GAPGDDPLYA AVSSGIRRQG VETLLPLFYN HLDSVFDYLP
     EGTLILLDAL ADAAFDERQA TIIDAYESRK GSIDARVMAK GAVKLDSGYR ALPPERLYLK
     DNQWREGLTR GRVRQFESFQ RDDAGHVDLG ARTGRSFAPE RLQDSVNLFS AVAEHARAKS
     KMGKRVLFAS WTEGSSDRLG AMLADHGLDK TRLAKDYADA VAFGVAGTKA KPIQRAVLPL
     DQGYETEGLV VISETDILGD RLARPRKRRR ANNFLAEASS LSMGDLVVHI EHGIGRYEGL
     KTLSVNDAPH DCLELQYAAD AKLYLPVENI DLLTRYGADS DSAQLDKLGS ASWQARKSKA
     KEKLREMADG LIQLAAARAL KVGQQIDPPS GLYDEFCAQF PYEETEDQLN AIHDVLEDLA
     KGQPMDRLIC GDVGFGKTEV ALRAAFVVAM SGQQVAIICP TTLLARQHFK TISQRFQGWP
     IRVRHLSRMV TKKEADETRD GLKNGEVEVV IGTHALLAEQ VSFKDLGLVI VDEEQHFGVK
     HKEKLKSFRA DVHMLTLSAT PIPRTLQMAL SGIREMSIIA TPPVDRLAVR TYVLPFDGVS
     IREALLREKY RGGQAYYVVP RLKDLPDVER FLREQVPEVR FIVGHGQMTP TQLEEVMTAF
     YDGQYDVLLA TTIVESGLDV PTANTLIVHR ADMFGLSQLY QIRGRVGRSK TRAFAYLTTQ
     PHHILSDASE KRLKVLQSLD NLGAGFQLAS HDLDIRGGGN LLGNEQSGHI REIGVELYQQ
     MLEDAVAELR SRNDQVVDDR SWSPQINAGA AIMIPEDYIP DLNTRLSLYR RVSEAEKRED
     REALAAELID RFGPIPEAAE QLLKVVGIKG LCREANVAKI DVGPKGAVIT FRNDTFANPM
     GLIGLIQARP NDWKLRPDQK LLVRGEWPEA AARLVAAEKI MTQLAGVATG
//
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