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Database: UniProt
Entry: A0A1Y2QIY9_9BURK
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ID   A0A1Y2QIY9_9BURK        Unreviewed;      1160 AA.
AC   A0A1Y2QIY9;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
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=CAP38_03930 {ECO:0000313|EMBL:OSZ67904.1};
OS   Hydrogenophaga sp. IBVHS2.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Hydrogenophaga.
OX   NCBI_TaxID=1985170 {ECO:0000313|EMBL:OSZ67904.1, ECO:0000313|Proteomes:UP000243193};
RN   [1] {ECO:0000313|EMBL:OSZ67904.1, ECO:0000313|Proteomes:UP000243193}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBVHS2 {ECO:0000313|EMBL:OSZ67904.1,
RC   ECO:0000313|Proteomes:UP000243193};
RA   Orr R.J.;
RT   "Draft genome sequences of novel bacteria, isolated from environmental
RT   samples.";
RL   Submitted (MAY-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}.
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:OSZ67904.1}.
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DR   EMBL; NFUT01000001; OSZ67904.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2QIY9; -.
DR   STRING; 1985170.CAP38_03930; -.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000243193; 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:UP000243193}.
FT   DOMAIN          624..785
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          806..960
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1160 AA;  129143 MW;  2A32ABF2FC1E68DB CRC64;
     MDLPKLSPGK RHTLPHPGGS ADALLLAQLA LRERAASRLT AIVTADANDA QRLIDELAFF
     APDLRVTLFP DWETLPYDTF SPHQDLISER LATLWRISQR DHEAGADVVL VPATTALYRL
     APPSFLAGYT FEFKVRQKLD EARLKAQLTL AGYNHVTQVV SPGEYAVRGG LIDLFPMGSL
     VPYRVDLFDD EIDSIRTFDP DSQRSLYPVP EVRLLPGREF PMDDAARALF RSRWRELLEG
     DPTKSRIYKD IGNGVATAGI EYYLPLFFEE TATVFDYLGE QATVVLHGDL EPAFQRFWQD
     TRDRHRLLHG DPDRPVLPPE SLFLQAEQFY TLANRHAQLA LRPGVGDVTH SAFVQTLPTL
     SVVRGAEDPL AHLQAHLRAS PHRLLLLAES DGRRESLLDF IRASGLSPPV FDSLAEFQAS
     DEKVGMATAA LNAGFAWIEG GIDFVTETEL FSAGPTTRRR RKQEQVSDVE ALIKDLSELN
     VGDPVVHTQH GIGRYRGLVN LDMGEKNADG TPALQEFLHL EYADKAVLYV PVSQLQLIGR
     YTGVSADEAP LHKLGSGQWE KARRKAAEQV RDAAAELLNI YARRAARQGH PFRYSPQDYE
     TFANDFGFDE TADQRAAIHA VIQDMISPRP MDRLVCGDVG FGKTEVALRA AFVAVTGGKQ
     VAFLAPTTLL AEQHYQTLVD RFSKWPVKVA EMSRFRTQKE ITAAMKGIAD GSVDIVVGTH
     KLLSEKTQFK NLGLLIIDEE HRFGVRHKEA VKALRAEVDV LTLTATPIPR TLGMALEGLR
     DLSVIATAPQ RRLAIKTFVR NEDKGVIREA VLRELKRGGQ VYFLHNEVET IENRRARLEG
     LLPEARIGVA HGQMPERQLE AVMRDFVAQR TNLLLCSTII ETGIDVPSAN TIVISRADKF
     GLAQLHQLRG RVGRSHHQAY AYLLVPEIES LTKQAQQRLD AIQQMEELGS GFYLAMHDLE
     IRGAGEVLGE NQSGNMLEVG FQLYNEMLSE AVRSLKAGKE PDLLSPLSVT TDINLHAPAL
     LPNDYCGDVH LRLSFYKKLA TAKSTDQVDA LLEEIVDRFG KLPPQAQTLI DVHRLRVLST
     PYGVVKVDAA PGVTNITFRP NPPVEPMRII ELIQKNKHIK LAGNEKLRIE KALPEVKDRV
     QLVRDVLRSL GQPVQSAETI
//
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