ID A0A068QT57_9GAMM Unreviewed; 1150 AA.
AC A0A068QT57;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 47.
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:CDG18187.1};
GN ORFNames=XDD1_2488 {ECO:0000313|EMBL:CDG18187.1};
OS Xenorhabdus doucetiae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=351671 {ECO:0000313|EMBL:CDG18187.1, ECO:0000313|Proteomes:UP000032721};
RN [1] {ECO:0000313|EMBL:CDG18187.1, ECO:0000313|Proteomes:UP000032721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FRM16 / DSM 17909 {ECO:0000313|Proteomes:UP000032721};
RA Genoscope - CEA;
RL Submitted (JUL-2013) 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}.
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DR EMBL; FO704550; CDG18187.1; -; Genomic_DNA.
DR RefSeq; WP_045971281.1; NZ_VNHN01000016.1.
DR AlphaFoldDB; A0A068QT57; -.
DR STRING; 351671.XDD1_2488; -.
DR KEGG; xdo:XDD1_2488; -.
DR HOGENOM; CLU_005122_0_2_6; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000032721; Chromosome.
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 CDD; cd18810; SF2_C_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 616..777
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 799..952
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1150 AA; 131061 MW; B7C2A5C8509ABB25 CRC64;
MSAKYRYQLP ERRGDSRSLG HLTGAACAVE CAAIIERHSG PILLVTKDMQ NALRLRDEIQ
QFTHAPINTM SDWETLPYDS FSPHQEIISN RLSTLYHLPF MTKGALILPV NTLMQRVCPH
DYLKGHALVM HKGQRLSRDK LRAELEQAGY RRVEQVLEHG EFATRGALFD LFPMGSEHPY
RIDFFDDEID SLRTFDVDSQ RTLAEVEKIS LLPAHEFPTD QEAIELFRSQ WREQFEVRRD
AEHVYQQVSK KMLPAGIEYW QPLFFEQPLP AIFDYLPENT LLITQNLTHA AERFWQDAKQ
RFESRKVDPM RPLLAPEQLW LPVNKLFSEL KNWPRIEVDN DPLPQKAKNT NLAYHPLPDL
SVAAQQKAPL DKLRRFMEQF SDGGKIVFSV ESEGRRESVQ ELLSRIKINP IKINQLTDAD
SPGHYLMVGA AEHGFVDEDH HLALICESDM LGERVSRRRQ DNRRTINTDT LIRNLAELRH
GQPVVHLEHG VGRYQGLITL EAGGIKAEYL ILTYAGEDKL YVPVSSLHLI SRYAGGAEES
APLHKLGGEA WSKARQKAAE KVRDVAAELL DVYAQRAVKP GFAFANDREQ YQLFCQSFPF
DTTPDQEQAI NAVLDDMCEP IAMDRLVCGD VGFGKTEVAM RAAFLSIINN KQVAVLVPTT
LLAQQHYDNF RDRFANWPVH IEVMSRFRSA KEQQQVIDMA AEGKVDIIIG THKLLQSDLR
WKDLGLLIVD EEHRFGVRHK ERIKSIRADV DVLTLTATPI PRTLNMAMSG MRDLSIIATP
PARRLAVKTF VREYDSLVVR ESILREILRG GQVYYLYNDV ENIEKAKARL EELVPEARIV
VGHGQMRERD LERVMTDFHH QRFNVLVCTT IIETGIDIPS ANTIIIERAD HFGLAQLHQL
RGRVGRSHHQ AYAYLLTPHP KAMTSDAKKR LEAIASLEDL GAGFALATHD LEIRGAGELL
GEDQSGQMAS IGFTLYMELL ESAVDALKEG REPSLEDLTN NQTEIELRMP VLLPDDYIPD
VNMRLSFYKR IASAQDNSEL DELKVELIDR FGALPDPGRQ LLQSAAIRLI AQQLGIKRIE
AYEKGGFIEF GSHNKVDPNY LISLLQTQPN VYRLDGPFKL KFMTELTERA SRLSFIQQLL
ENFVQHKSDT
//
