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Database: UniProt
Entry: A0A0R0D4B9_9GAMM
LinkDB: A0A0R0D4B9_9GAMM
Original site: A0A0R0D4B9_9GAMM 
ID   A0A0R0D4B9_9GAMM        Unreviewed;      1154 AA.
AC   A0A0R0D4B9;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 40.
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=ABB28_03610 {ECO:0000313|EMBL:KRG76347.1};
OS   Stenotrophomonas chelatiphaga.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas.
OX   NCBI_TaxID=517011 {ECO:0000313|EMBL:KRG76347.1, ECO:0000313|Proteomes:UP000051386};
RN   [1] {ECO:0000313|EMBL:KRG76347.1, ECO:0000313|Proteomes:UP000051386}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21508 {ECO:0000313|EMBL:KRG76347.1,
RC   ECO:0000313|Proteomes:UP000051386};
RA   Patil P.P., Midha S., Patil P.B.;
RT   "Genome sequencing and analysis of members of genus Stenotrophomonas.";
RL   Submitted (MAY-2015) 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:KRG76347.1}.
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DR   EMBL; LDJK01000009; KRG76347.1; -; Genomic_DNA.
DR   RefSeq; WP_057507311.1; NZ_LDJK01000009.1.
DR   AlphaFoldDB; A0A0R0D4B9; -.
DR   PATRIC; fig|517011.3.peg.3474; -.
DR   Proteomes; UP000051386; 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   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:UP000051386}.
FT   DOMAIN          623..784
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          797..959
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1154 AA;  127954 MW;  25967837DF91C2BC CRC64;
     MSRSPYPLPP LPRPGQLRAW WRAPSSPTAL AWYLARAAQA HDGPVLVVAP DNHGANQIES
     DLRTLLGDDP SLPVVAFPDW ETLPYDRFSP HPDIISQRLS ALHRLPGLKR GLVVVPVQTL
     MQQLAPKQYV IGGSFDLEVG QRLDLDAEKR RLESAGYRNV PQVMDPGDFA VRGGLLDVYP
     MGASEPLRVE LLDQDIDTIR AFDPETQRSL EKVQAVHMLP GREVPMDDAS ISRVMDALRE
     RFDVDTRRSS LYQDLKSRLA PAGIEYYLPL FFDHTATLFD YFSADVLPVM AAGVGEAAAA
     FWAQTGQRYE QRRHDVERPL LPPGQLYLSP ELLRERLNDL PRVEVWPPGH ARIEQAHALG
     DTALPPLPVA ARDAAAGQAL ATFIEQYPGR VLIAADTAGR REALLEVLQA ASLRPPVVAD
     LPTFLAGSER FAITVAPLED GFALDDPRIA VLTERQLFPE RAAHQRRSRR AGREPEAIIR
     DLGELTEGAP IVHEDHGVGR YRGLIAMDVG GMPGEFLEIE YAKGDRLYVP VAQLHLISRY
     SGASAETAPL HSLGGEQWTK AKRKAAEKVR DVAAELLEIQ ARRRARAGLA LDVDRAMYEP
     FAAGFPFEET QDQLAAIDAT LRDLASSQPM DRVVCGDVGF GKTEVAVRAA FAAASAGKQV
     AVLVPTTLLA EQHYRNFRDR FADYPMKVEV LSRFKSTKEI KAELEKVADG TIDVIIGTHR
     LLQPDVKFKD LGLVVVDEEQ RFGVRQKEAL KAMRANVHLL TLTATPIPRT LNMAMAGLRD
     LSIIATPPPN RLAVQTFISQ WDDALLREAF QRELARGGQL YFLHNDVESI GRMQRELSEL
     VPEARIGIAH GQMPERELER VMLEFQKQRF NVLLSTTIIE SGIDIPNANT IIINRADRFG
     LAQLHQLRGR VGRSHHRAYA YLVVPDRRSI TPDAEKRLEA IASMDELGAG FTLATHDLEI
     RGAGELLGED QSGQMAEVGF SLYTELLERA VRSIRLGKLP DLDAGEEARG AEVELHVPSL
     IPNDYLPDVH TRLTLYKRIS SARDSASLRE LQVEMIDRFG LLPDAAKHLF AIAELKLQAN
     ELGIRKVDLG EAGGRIVFEA KPNIDPMSVI QLIQKQSNLY SMDGPDKLRI KHPLPLPEDR
     FNAARALLTT LAPG
//
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