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Database: UniProt
Entry: A0A0Q4RJ74_9BURK
LinkDB: A0A0Q4RJ74_9BURK
Original site: A0A0Q4RJ74_9BURK 
ID   A0A0Q4RJ74_9BURK        Unreviewed;      1159 AA.
AC   A0A0Q4RJ74;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 42.
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=ASF16_09925 {ECO:0000313|EMBL:KQO18950.1};
OS   Acidovorax sp. Leaf78.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax.
OX   NCBI_TaxID=1736237 {ECO:0000313|EMBL:KQO18950.1, ECO:0000313|Proteomes:UP000051234};
RN   [1] {ECO:0000313|Proteomes:UP000051234}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf78 {ECO:0000313|Proteomes:UP000051234};
RA   Garrido-Oter R., Mueller D.B.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000051234}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf78 {ECO:0000313|Proteomes:UP000051234};
RA   Vorholt J.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-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:KQO18950.1}.
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DR   EMBL; LMLZ01000021; KQO18950.1; -; Genomic_DNA.
DR   RefSeq; WP_056169423.1; NZ_LMLZ01000021.1.
DR   AlphaFoldDB; A0A0Q4RJ74; -.
DR   STRING; 1736237.ASF16_09925; -.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000051234; 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}.
FT   DOMAIN          625..786
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          807..961
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1159 AA;  129150 MW;  72BACA2DBC7E37CB CRC64;
     MELPKLSPGK RFTLPRPVGS ADSLLLARLA ERDKAAGRTT AIVTADATDA QRLIEEMAFF
     APGLRCALFP DWETLPYDTF SPHQDLISER LATLWRISQK DKDTGADVVL VPATTALYRL
     APPSFLAGYT FHFKVKQKLD EAKFKAQLTL AGYSHVSQVV SPGEYAVRGG LIDLFPMGSL
     VPYRVDLFDD EIDSIRTFDP DSQRSLYPVP EVRLLPGREF PMDDDARAKF RSRWREMLEG
     DPTKSRIYKD MGAGVATAGI EYYLPLFFDD TATVFDYLGS EATVVLHGDL EPAFQRFWQD
     TKDRFRLVQG DPERPVLPPE ELFLSADQFY TRAKEHAQLS IRPGVEDIAE NPHFQKLGDL
     SVLRGAEDPL ARLHAHIRNT QHRVLLLAES AGRRESLLDF LRASGVNPPA FDSLAEFQGT
     ADEKVGIATA GLTVGFSWIE DGIDFVTETE LFAAGPTTRR RKKQEQVSDV EALIKDLAEL
     NVGDPVVHSA HGIGRYRGLV NMDVGNKNPD GTPAMQEFLH LEYADKAVLY VPVSQLQLIS
     RYTGVSADEA PLHKLGSGQW EKAKRKAAEQ VRDSAAELLN IYARRAAREG HAFRYSPQDY
     ETFANDFGFE ETADQNAAIH AVIQDMISPR PMDRLVCGDV GFGKTEVALR AAFVAVTGGK
     QVAFLAPTTL LAEQHYQTLV DRFSKWPVKV AEVSRFRSGK EITAAIKGIG DGTVDIVVGT
     HKLLSESTKF HNLGLLIIDE EHRFGVRHKE QMKALRAEVD VLTLTATPIP RTLGMALEGL
     RDLSVIATAP QRRLAIKTFV RNEGTGVIRE AVLRELKRGG QVYFLHNEVE TIENRRQKLE
     EILPEARIAV AHGQMPEREL ERVMRDFVAQ RYNILLCSTI IETGIDVPTA NTIIMSRADK
     FGLAQLHQLR GRVGRSHHQA YAYLMVPDTE GLTKHAAQRL DAIQQMEELG SGFYLAMHDL
     EIRGAGEVLG ENQSGNMLEV GFQLYNEMLN EAVKALKAGK EPDLLSPLSV TTDINLHAPA
     LLPDDYCGDV HLRLSFYKKL ATAKTPDQID SLLEEIVDRF GKLPPQAQTL IDVHRLRVLS
     QPYGVVKVDA APGVINITFK PQPPIDPMRI IELIQKNKHI KLAGNEKLRI ERELKDPKDR
     AQMVRDILRS LGQPVAAPV
//
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