ID Q2NU25_SODGM Unreviewed; 1150 AA.
AC Q2NU25;
DT 07-FEB-2006, integrated into UniProtKB/TrEMBL.
DT 07-FEB-2006, sequence version 1.
DT 27-MAR-2024, entry version 124.
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 OrderedLocusNames=SG1075 {ECO:0000313|EMBL:BAE74350.1};
OS Sodalis glossinidius (strain morsitans).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Bruguierivoracaceae; Sodalis.
OX NCBI_TaxID=343509 {ECO:0000313|EMBL:BAE74350.1, ECO:0000313|Proteomes:UP000001932};
RN [1] {ECO:0000313|EMBL:BAE74350.1, ECO:0000313|Proteomes:UP000001932}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=morsitans {ECO:0000313|Proteomes:UP000001932};
RX PubMed=16365377; DOI=10.1101/gr.4106106;
RA Toh H., Weiss B.L., Perkin S.A.H., Yamashita A., Oshima K., Hattori M.,
RA Aksoy S.;
RT "Massive genome erosion and functional adaptations provide insights into
RT the symbiotic lifestyle of Sodalis glossinidius in the tsetse host.";
RL Genome Res. 16:149-156(2006).
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; AP008232; BAE74350.1; -; Genomic_DNA.
DR RefSeq; WP_011410935.1; NC_007712.1.
DR AlphaFoldDB; Q2NU25; -.
DR STRING; 343509.SG1075; -.
DR KEGG; sgl:SG1075; -.
DR eggNOG; COG1197; Bacteria.
DR HOGENOM; CLU_005122_0_2_6; -.
DR OrthoDB; 9804325at2; -.
DR BioCyc; SGLO343509:SGP1_RS09240-MONOMER; -.
DR Proteomes; UP000001932; 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 790..952
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1150 AA; 130027 MW; 32AC8BAAFD9F58A6 CRC64;
MSERDRYTLP TQAGKKLILG QLTGAAVAVE CAAIVDRYSG PVLLITTDMQ SALRLHDEIL
QFTHHPVLTL PDWETLPYDS FSPHQEIISD RIATLYRLPS LARGVIILPV NTLMQRVCPH
TFLHRHTLLM TKGQRLSRDT LRAQLEQAGY RSVDQVLEHG EFATRGALLD LYPMGSEEPY
RIDFFDDEID SLRIFDVDTQ RTLQEMASIN LLPAHEFPTD KAAIELFRSQ WREQFDVRRD
AEHIYQQVSK GTLPAGIEYW QPLFFSEPLV PLFSYLPADT LVVNTGDLEA GAGRFWDDAC
ARFDNRRVDP MRPLLPPETL WLRVDNLFAE LKRWPRVQLS TQTLPEKAGH YNMDYRPLPD
LAVEAQSKAP MDKLRRFCEQ FDGPVIFSVE SEGRRETLSE LLARVKILPT LINRLEDAAA
PGAYYLIIGA SERGFIDAPR ARALICEGDL LGERVSCRRQ DNRRIINAYT LIRNLAELHE
GQPVVHLEHG VGRYAGMTTL EAGSIKAEYL ILTYACNDKL YVPVSSLHLI SRYAGGADEN
APLHKLGGDA WTRARQKAAE RVRDVAAELL DIYAQRAAKS GFAFRHNREN YQLFCEGFPF
EPTVDQSQAI NAVLSDMCQP LSMDRLICGD VGFGKTEVAM RAAFLAIENH KQVAVLVPTT
LLAQQHFDNF RDRFANWPVR IEMISRFRSA RDQAQVLEQT AEGKVDILIG THKLLQSDVK
WHDLGLLIVD EEHRFGVRHK ERIKAMRAGV DILTLTATPI PRTLNMAMSG MRDLSIIATP
PARRLTVKTF VRQYDALVVR EAILREVLRG GQVYYLYNDV ENIEKAARCL ETLVPEARIA
IGHGQLRERE LERVMNDFHH QRFNVLVCTT IIETGIDIAN ANTIIIERAD HFGLAQLHQL
RGRVGRSHHQ AYAYLLTPPP KALSQDAHKR LEAIASLEDL GAGFALATHD LEIRGAGELL
GEDQSGQMET IGFSLYMDLL ESAVDALKAG REPSLEDLTR QLTEVELRMP ALLPEEYIPD
VNTRLSLYKR IAIAADDREI EDLKVELIDR FGLLPDPARY LLAIAGLRQR AQSLGIRRIE
GNDKGGFIEF SATNRVDTVY LIGLLTSEPG TYRLDGPTRL KFICDLADRT TRLQYVDGLL
RELQQHTLST
//
