ID A0A369VV16_9SPHN Unreviewed; 1153 AA.
AC A0A369VV16;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
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 ECO:0000313|EMBL:RDE06224.1};
GN ORFNames=DVW87_00325 {ECO:0000313|EMBL:RDE06224.1};
OS Sphingomonas aracearum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=2283317 {ECO:0000313|EMBL:RDE06224.1, ECO:0000313|Proteomes:UP000253918};
RN [1] {ECO:0000313|EMBL:RDE06224.1, ECO:0000313|Proteomes:UP000253918}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WZY 27 {ECO:0000313|EMBL:RDE06224.1,
RC ECO:0000313|Proteomes:UP000253918};
RA Zhiyong W., Qinglan Z., Zhiwei F., Ding X., Gejiao W., Shixue Z.;
RT "a novel species of Sphingomonas isolated from the rhizosphere soil of
RT Araceae plant.";
RL Submitted (JUL-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:RDE06224.1}.
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DR EMBL; QQNB01000001; RDE06224.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A369VV16; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000253918; 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:UP000253918}.
FT DOMAIN 622..783
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 804..958
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1153 AA; 126103 MW; 520FCA2D9D694F58 CRC64;
MPDLKTILSA AAPLTLSGVP SGFQPWLLAD LARAAPTRAV FVAADEAAMR AIAATAPAFA
PELEVLTFPA WDCLPYDRAS PTLRVMAERM ATLHALQRKP NGPQLLLTTV NAVAQRTLTP
FRIRQLVARL APGERIGRDR LAELLSANGY VRTETVHDAG EFAVRGGLVD LFPSGEEQAL
RLDFFGDEIE SVRSFDPADQ RTTGKLDGFT LLPASEALLD EESIKRFRSR YREKFGATAT
GDPLYQAVSD GRRLAGMEHW LPLFEEKLAT LFEHLGDGAV VVREAGVAGS AERRLEAIAD
YYENRMRAQT GQPGSYRPLG TTALYLGEKE LNQAFDAAPA HRTSPFHEPE SASVLDFAVD
GPRDFAPERT AGTNIYEAVV DHLAALGRQK RKRVLASYSV GARDRLAGLL ADHDLAGARK
VDSWHEALGV GETQVALLVL PLDHGFTTPD VALLTEQDML GDRLVRRAKR KKSADAFLAE
IASLTPGDLV VHVDHGIGRY EGLTQIPVSK APHDCVAVSY AGGDKLFVPV ENLEVLSRYG
SDSDAVASLD RLGGEAWQRR KSKMKERIRE IAGELIKTAA ARALRPAEVV EPDEGAYASF
VDRFPYEETD DQDRAIGDVL EDLSAGKPMD RLVVGDVGFG KTEVALRGAF AAAISGHQVA
VVCPTTLLAR QHYNNFAQRF EGFPLKVGRL SRLVGTAEAK ATKDGLAEGT VDVVVGTHAI
LAKGVEFKRL GLVVVDEEQR FGVTHKERLK ALKTDVHQLT LTATPIPRTL QMAMSGLREL
SVIQTPPVDR LAVRTYVMPW DPVVLREALL REHYRGGQSF FVVPRINDLP DVEQFLREHV
PEVRYVVAHG QMAAGEVEER MSAFYDKKFE VLVSTTIVES GLDIPSANTM VVHRADRFGL
AQLYQLRGRV GRSKTRAYCY LTTPEGRILT ETAEKRLKVL SDLDSLGAGF QLASHDLDQR
GAGNLLGDEQ SGHIKEVGYE LYQSMLEEAI LDAKAGGMRQ ERPRDFSPQI TVDAPILIPE
DYVPDLDLRM GLYRRLNELE DRAAVDGFAA ELIDRFGPLP APTDNLVKLI EAKLNARKAC
IAKLDVGPRG AVVSFHEDTP PNIPGLIAYV DRLGGVAKLR PDNKLVVNRN WGDPQARLNG
ALQLSKGLAK AAG
//
