ID A0A1B3LSM2_9PROT Unreviewed; 1149 AA.
AC A0A1B3LSM2;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-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:AOF83852.1};
GN ORFNames=BSY238_3465 {ECO:0000313|EMBL:AOF83852.1};
OS Methyloversatilis sp. RAC08.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Sterolibacteriaceae; Methyloversatilis.
OX NCBI_TaxID=1842540 {ECO:0000313|EMBL:AOF83852.1, ECO:0000313|Proteomes:UP000094168};
RN [1] {ECO:0000313|Proteomes:UP000094168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RAC08 {ECO:0000313|Proteomes:UP000094168};
RA Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL Submitted (JUL-2016) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP016448; AOF83852.1; -; Genomic_DNA.
DR RefSeq; WP_069040777.1; NZ_CP016448.1.
DR AlphaFoldDB; A0A1B3LSM2; -.
DR STRING; 1842540.BSY238_3465; -.
DR KEGG; metr:BSY238_3465; -.
DR PATRIC; fig|1842540.3.peg.3509; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000094168; 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 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:UP000094168}.
FT DOMAIN 617..782
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 803..957
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1149 AA; 127653 MW; 1F376856449563CA CRC64;
MTSSPSLLNS LLRPLPRPRP ASRIDWPPLP GGAQALALAG LAKDTGAPLV VVAARPMDAQ
RLLDELRWFA PSLRSFQLPD WETLPYDQFS PHNDLVSERL ETLYALMRGE LDVLVVPAST
ALYRLAPREY LAAHTFFVKQ GEKLDVERLR LQLTVAGYGP VTQVVAPGEY SVRGGLVDLY
PMGAALPYRI DLFDDEVESI RTFDVDTQRT VFPTKEIRLL PAREFPMDDK ARTAFRSRFR
EAFEGDPSKS VIYKDVSNGV PTAGIEYYIP LFFEHTDTLF DYLPANALVA LDAEVNDAIA
DFWRDTKSRF DLMKGERARP ILPPSELFLS EEQFHVSLAN RAIVRLGRGA PDVSAGAAAL
PELGIERKAA DPLHRLRAAV AAQRVVVIAE SAGRRETLID YFAEYGLASA PVDGFDAAIA
ADTALTVAIG PLIEGFALSS PAIALVTESE LYPTQARSRG KRDGRKVTAE NFLRDLTELK
IGDPVVHLQH GIGRYIGLTH MDLGEGETEF LHLEYADGDK LYVPVSQLHQ ISRYSGAPGD
QVHLHKLGSG QWDKAKKRAA AQVRDTAAEL LALYAQRSAR KGHTFGFKQH DMDAFAEGFG
FEETPDQMGA ITAVIGDMTS GRPMDRLVCG DVGFGKTEVA LRAAFVAVAD GKQVAILAPT
TLLAEQHYQT FSDRFAQVAH EWPARIAEIS RFKSAKEQTQ ALKEAAEGKI DVLIGTHRLL
QKDVKFARLG LVIIDEEHRF GVRQKEALKS LRAEVDVLTL TATPIPRTLA MSLEGIRDFS
VIATAPQKRL AIKTFVSPWS RGLIREAVLR EFKRGGQVYF LHNEVDTIEE MGTRLADLLP
EARIVIGHGQ LPERELERVM REFTQRKHNL LLCTTIIETG IDNPNANTII INRADRFGLA
QLHQLRGRVG RSHHQAYAYL LTDAHAKPTE QGRRRLEAIT MMEELGSGFY LAMHDLEIRG
AGEVLGESQS GEMQEIGFNL YTDMLKSAVK SLQKGEDADL TQPLDIVSEI NLHTPALLPT
AYCPDVHERL TLYKRLANCD TTDEVSALRE ELVDRFGQMP DQTRALLETH RLRIAAKPLG
ITKIDAHDTQ ILVTFVPNPP IEPIRIIQLV QKDRNFKLAG QDRLSWKRSS VDLDARVAGV
RELMKKLTG
//
