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Database: UniProt
Entry: A0A2U2N202_9GAMM
LinkDB: A0A2U2N202_9GAMM
Original site: A0A2U2N202_9GAMM 
ID   A0A2U2N202_9GAMM        Unreviewed;      1158 AA.
AC   A0A2U2N202;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 24.
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=DEM34_09060 {ECO:0000313|EMBL:PWG63216.1};
OS   Spiribacter halobius.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Spiribacter.
OX   NCBI_TaxID=2182432 {ECO:0000313|EMBL:PWG63216.1, ECO:0000313|Proteomes:UP000245474};
RN   [1] {ECO:0000313|EMBL:PWG63216.1, ECO:0000313|Proteomes:UP000245474}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E85 {ECO:0000313|EMBL:PWG63216.1,
RC   ECO:0000313|Proteomes:UP000245474};
RA   Zheng W.-S., Lu D.-C., Du Z.-J.;
RT   "Spiribacter halobius sp. nov., a moderately halophilic bacterium isolated
RT   from marine solar saltern.";
RL   Submitted (MAY-2018) 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}.
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:PWG63216.1}.
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DR   EMBL; QFFI01000012; PWG63216.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2U2N202; -.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000245474; 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:UP000245474}.
FT   DOMAIN          625..786
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          799..966
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1158 AA;  129672 MW;  A911EE72CC3875AC CRC64;
     MADQSASPLR PPIPRSPGER RDWYGLPEPA QALALASAAE AHTGLVLAVA ASSQQALHLE
     AELGFFLDGR LPVEVMPDWE TLPYDVFSPH QDIISQRLRT LHDLPGLTRG VLIVPAGTLM
     QRIAPRSFLE GTVLRVAVGD HLALEPMRER LERAGYRCVS EVMEHGEFAV RGSLLDLYPM
     GSETPYRIDL FDDEVDSIRL FDPETQRSAQ KVDRIELLPA REFPTGEEGI TRFRRQYRAA
     FEGDPTASTV YRDVSDGRMP NGIEYYLPLF FEQTGTLFDY LPEGALAVRT GPVDEQLGAD
     WEQIAERYEQ RRHDRERPLL PPERLYLSPD EVRSALNRLP QVRIPAEDAE PTGQAREVTF
     TTSTLPDLRS EPGAARPLGR LEAFAAEAPE RLLFLAETAG RRETLRERLQ QAGLRPEDVS
     GWAAFAAGDP ALGLTVGPLE AGFRLPDDGI AVVPDTALFA ERAKQRRRRQ STAERDPDAI
     IRDLTDLHPG APVVHENHGV GRYRGLQTLD VGNVRTEFLT LEYAGGDKLY VPVASLHLIT
     RYTGTDSDAA PLHRLGGEQW EKARRKAAER ARDVAAELLD IYARREAQSG HAHRFPREEY
     ERFAAQFPFE ETPDQETAIH AVIRDLEQER PMDRVVCGDV GFGKTEVAMR AAFVGVQAGG
     QVAVLVPTTL LAQQHYQNFS DRFADWPVRI ELLSRFRSQK EQNAVLRDLA AGKVDIVIGT
     HKLLQGSVKF DNLGLLIIDE EHRFGVRQKE ALKRLRANVD VLTLTATPIP RTLNMSLAGM
     RDLSIIATPP ARRLAVKTFV NQWNDALIRE ACLRELHRGG QVYFLHNDVE TIERVARELE
     ALVPEARVRI AHGQMREREL ERVMLDFYHQ RFNVLVCTTI VESGIDVPSA NTIVINRADR
     LGLAQLHQLR GRVGRSHHRA YAYLVAPPKR QLTPDAAKRL EAIASLEDLG IGFALASHDL
     EIRGAGELLG EGQSGQIQEV GFSMYSELLE RAVRDLRAGR EPALDRPLHH GTEVDLRIPA
     LLPEEYLPDV HTRLVLYKRI ASAPDENALR ELQVEMIDRF GLLPEPARNL FRLAELRLRA
     ERLGLERIEA GPGGGVLTFS DTPRVDPAAL VQLVQEKPAV YRLEGQERLR FRLETEAADE
     RIGVVSQLMD ALEQKEAA
//
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