ID A0A0U1Q019_9BURK Unreviewed; 1164 AA.
AC A0A0U1Q019;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 38.
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=AAV94_06295 {ECO:0000313|EMBL:KKW68097.1};
OS Lampropedia cohaerens.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Lampropedia.
OX NCBI_TaxID=1610491 {ECO:0000313|EMBL:KKW68097.1, ECO:0000313|Proteomes:UP000050580};
RN [1] {ECO:0000313|EMBL:KKW68097.1, ECO:0000313|Proteomes:UP000050580}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT6 {ECO:0000313|EMBL:KKW68097.1,
RC ECO:0000313|Proteomes:UP000050580};
RA Tripathi C., Rani P., Mahato N.K., Lal R.;
RT "Draft genome sequence of Lampropedia sp. CT6, isolated from the microbial
RT mat of a hot water spring, located at Manikaran, India.";
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:KKW68097.1}.
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DR EMBL; LBNQ01000022; KKW68097.1; -; Genomic_DNA.
DR RefSeq; WP_046741495.1; NZ_LBNQ01000022.1.
DR AlphaFoldDB; A0A0U1Q019; -.
DR STRING; 1610491.AAV94_06295; -.
DR PATRIC; fig|1610491.3.peg.1337; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000050580; 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:UP000050580}.
FT DOMAIN 627..788
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 809..963
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1164 AA; 129937 MW; 80EC594AA51E386E CRC64;
MNLPKLTPGQ RYTMPMPVGS ADALLLAQMA TREKAAGKRL AVVTADARDA LRLLREMVFF
EPALKAVLFP DWETLPYDSF SPHQDLISER LATLWSILQG EADVLLIPAT TALYRLAPPS
FLAAYTFHFK TGQKLDEARL KAQLTMAGYQ HVGQVVSPGE YAVRGSLIDL FPSGAALPYR
IDLFDDEIDS IRTFDPDSQR SQYPVPEVRL LPGREFPMDE PARKRFRSRW RELLEGDPTK
SRIYKDIGNG VATAGIEYYL PLFFEETATV FDYLGEATTL VLHGPLDAAL QRFWDDTQER
YRLIAGDEER PALPPPALFL SSEQFFALCK PLAQLSLRPA ASEEAARSEA RHSSAEFAAL
PDISAVRGSD DPLSRLQAYL RNTPQRVLIL AESEGRRESL GDFLRASSLS TPGFDSLAEF
QASPEKIGIA TSALQRGFGW LEGGIDFVTE TELFNTEPTA RKRRRHEHAS NVEHMVRDLA
ELKVGDPVVH AQHGIGRYRG LVHMDMGQKN PDGSPALQEF LHLEYAGEAV LYVPVSQLQQ
ISRYSGVAAD EAPLHRLGSG QWEKAKRKAA EQVRDTAAEL LNIYARRAAR QGHAFRFNAA
EYEAFAKDFG FEETPDQRAA IHAVIQDMIS PQPMDRLVCG DVGFGKTEVA LRAAFVAVLA
GKQVAFLAPT TLLAEQHYLT LTDRFSKWPV KVEQMSRFRT TKEINAAIKG LADGSVDIVV
GTHKLLSSSI DFKNLGLLII DEEHRFGVRH KEAMKALRAE VDVLTLTATP IPRTLGMALE
GLRDLSVIAT APQKRLAIKT FVRSESQGVI REAVLRELKR GGQVYFLHNE VETIENRREK
LQEILPEARI AVAHGQMPER ELERVMRDFV AQRYNLLLCS TIIETGIDVP TANTIVISRA
DKFGLAQLHQ LRGRVGRSHH QAYAYLLVPD VESLSRQAQQ RLDAIQDMEE LGSGFYLAMH
DLEIRGAGEV LGENQSGNMM EIGFQLYNEM LADAVKALKA GKEPDLLSPM QAVTEINLHT
PALLPNDYCG DVHLRLSFYK RLATADSIEQ VDLLLEEIVD RFGKPPEPVQ ALIDTHRLRI
LCEPYGVQKV DAAPGAITIA FRPNPPVEPL RIIEMIQKNR HIKLAGNDKL RIERELPAMK
DRVQMVRDVL RNLGQPRTEA AAVE
//
