ID A0A0W0Y4Q6_9GAMM Unreviewed; 1148 AA.
AC A0A0W0Y4Q6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 36.
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:KTD51712.1};
GN ORFNames=Lqui_0556 {ECO:0000313|EMBL:KTD51712.1};
OS Legionella quinlivanii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=45073 {ECO:0000313|EMBL:KTD51712.1, ECO:0000313|Proteomes:UP000054618};
RN [1] {ECO:0000313|EMBL:KTD51712.1, ECO:0000313|Proteomes:UP000054618}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC#1442-AUS-E {ECO:0000313|EMBL:KTD51712.1,
RC ECO:0000313|Proteomes:UP000054618};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
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:KTD51712.1}.
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DR EMBL; LNYS01000006; KTD51712.1; -; Genomic_DNA.
DR RefSeq; WP_058506670.1; NZ_UGOX01000001.1.
DR AlphaFoldDB; A0A0W0Y4Q6; -.
DR STRING; 45073.Lqui_0556; -.
DR PATRIC; fig|45073.5.peg.586; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000054618; 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:UP000054618}.
FT DOMAIN 617..778
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 799..953
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1148 AA; 130846 MW; ABE1630CA4B9A0EC CRC64;
MQNAILQYPS VDRKQNWGSL HGCSLSLALS EYCLNEPGVK LLITPDTLTA NQLMSELRFF
LGQSSCELLY FPDWETLPYD LFSPHQDIIS ERLLTLNRLQ QASKTIVIAS ASTLMHRLCP
PAFLHQYAFA LKQGQTLDLG HFRNQLQNGG YHSVNKVLEH GEYAVRGSII DMYPMGSNCP
FRIELFDDEI ESLRQFDTES QRTIAKVDQI EILPAREFPL NEASITLFRR NFREQFSGNP
SQCPVYESVS NSQYPSGIEY YLPLFFENTA TFFDYLPENA SICLIQNIPE EAERFWQELK
LRYEQRRYDI SRPVLTPEQM FISPTDLLTR VNTHQQLRLW HQAIDRKGAV FNFRVKEAPA
LPVERQSPQP LHHLRDYLSQ PDRRHLIVVE SAGRREVLLD LLRQTGISAN QLNDWQSFLS
SDDLISITTG PLIEGAELLD SQIAIIVEAQ LFGEQAIPQR RSSQKTVDPD LIIRDLSELR
LHAPVVHIQF GVGRYQGLKT LETNDSINEF LVLSYAGDDK IYVPVTSLHL ISRYTGMDSE
HAPLHKLGSD QWQKEKKKAA EKIHDVAIEL LDIYAKREAQ PGFVYEFDSL EYQRFASGFP
FTETVDQLNA INEIIKDMKS PRPMDRLICG DVGFGKTEVA MRAAFLAVQN NKQVCVLVPT
TLLAGQHFEN FRDRFADFPV NLELLSRFRS TKESNQVIDG LKSGKIDIVI GTHKLFSKDI
SFKNLGLLII DEEHRFGVKQ KEHIKSLRTH IDILSMTATP IPRTLNMAMG GIRDISLIAT
PPAKRLAIKT FWQEKQTTVL REAILREILR GGQVYFLHNN VQTIDKTAEE LQEMIPEAKI
RTAHGQMRER ELEKIMSDFY HHRFNVLVCT TIIETGIDIP TANTIIIDRA DKFGLAQLHQ
LRGRVGRSHH QAYAYLFTPN EKLLTPDAVK RLEAIVSLED LGAGFTLATH DLEIRGAGEL
LGEEQSGNMH AVGFHLFMEM LDKAVSDLKS GKTPELGGPM QQGPEIDLRL SAILPEEYIA
DIHTRLIMYK RIANAGDKEQ LRDLQIEMID RFGLLPPQAK YLLWVTELKL IAAQLGINKI
YAAQQQGKIE FGENPRINTG VLINLIQVHA KRYQLEGPSR LKFTLDSESH EERILEIKNL
LLKLSNEG
//
