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Database: UniProt
Entry: J7Q5B2_METSZ
LinkDB: J7Q5B2_METSZ
Original site: J7Q5B2_METSZ 
ID   J7Q5B2_METSZ            Unreviewed;      1178 AA.
AC   J7Q5B2;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 61.
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=BN69_3348 {ECO:0000313|EMBL:CCJ08799.1};
OS   Methylocystis sp. (strain SC2).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Methylocystaceae; Methylocystis.
OX   NCBI_TaxID=187303 {ECO:0000313|EMBL:CCJ08799.1, ECO:0000313|Proteomes:UP000005263};
RN   [1] {ECO:0000313|EMBL:CCJ08799.1, ECO:0000313|Proteomes:UP000005263}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC2 {ECO:0000313|EMBL:CCJ08799.1,
RC   ECO:0000313|Proteomes:UP000005263};
RX   PubMed=23045511; DOI=10.1128/JB.01446-12;
RA   Dam B., Dam S., Kube M., Reinhardt R., Liesack W.;
RT   "Complete Genome Sequence of Methylocystis sp. Strain SC2, an Aerobic
RT   Methanotroph with High-Affinity Methane Oxidation Potential.";
RL   J. Bacteriol. 194:6008-6009(2012).
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; HE956757; CCJ08799.1; -; Genomic_DNA.
DR   RefSeq; WP_014892825.1; NC_018485.1.
DR   AlphaFoldDB; J7Q5B2; -.
DR   STRING; 187303.BN69_3348; -.
DR   KEGG; msc:BN69_3348; -.
DR   PATRIC; fig|187303.17.peg.3617; -.
DR   eggNOG; COG1197; Bacteria.
DR   HOGENOM; CLU_005122_1_3_5; -.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000005263; 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; 3.40.50.11180; -; 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; 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; 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          644..805
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          826..980
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1178 AA;  129610 MW;  3110174B934DC8B6 CRC64;
     MSAAATKLKK AAAGLEAARS GLVKGERLIF AHAPDGFDAF VSADLARALA REAEGQAAVF
     VHVARDGARS AAFRNALRFA NPDVEILDIP GWDCQPYDRV SPHAGVVARR MTALSRLTRA
     KSSSERPRVV TTTVDCLLQR VPPQKMVSAE SFAAAPGNVV KLDELALWLE SNGYLRASTV
     RETGEYAQRG GIVDLYPPGL PAPIRLDFFG ETLESIRSFD PDTQRATGQL RSLDLTPMSE
     VRLTSDTMRR FRQSYAARFG GQTRGDALYE AVSEGRRFHG MEHWLPLFYE RMDTLFDYLG
     EAPVVLDPLV EDAAAERVKQ IEDYYDARKY AHDLDPAASN YKPLEPRALY LSLEDWRAAI
     EGRAAAQFTP FAAHEGQKAI DCGARPGRDF APERNTPDVN VFQAAADHIE ALRDAGGTVV
     VTGWSEGSCE RLGHVLAEHG APDLPRVASL PQALSKAVSI AVLGIEHGFE TDAYAVVGEQ
     DILGDRFVRR RRKRKPNENL LGEVAALSAG DLVVHVDHGI GRFVGLETIS AAGAPHDCLE
     LHYAGGDKLY LPVENIELLT RYGGEDAEAQ LDRLGGAGWQ SRKSRMKNRI REMAKGLIEI
     AAQRQLREAP KLIAPEGLYD EFCARFPYDE TEDQLAAIDA TLDDLAAGRP MDRLVCGDVG
     FGKTEVALRA AFCAAINGKQ VAVVAPTTLL ARQHYKTFTE RFAGLPVRIG RLSRMVGAAE
     ARETKKDLAE GRIEILIGTH AVLGKTVSFK DLGLVIIDEE QHFGVGHKER LKELRAEVHV
     LTLSATPIPR TLQLAMTGVR ELSIIATPPI DRLAVRSFVS PFDSLIVREA LLRERYRGGQ
     AFFVCPRIED LEEAAAFLRE NAPESKFVTA HGQMSASELE DKMSAFCDGK FDILLSTTIV
     ESGLDIPRAN TLIVWRADMF GLAQLYQLRG RVGRAKLRAY ALFTTPANRT ITPQAQKRLD
     VLQSLDTLGA GFQLASHDLD IRGAGNLLGE EQSGHIREVG YELYQQMLAD AITLLKAGVE
     EPQEEAWSPT IAIGAPVTIP EDYVADLTLR LQLYRRLSTL ETDQDIEAFA AEMIDRFGPI
     PPEVEQLLEI VAIKALCRRA HVEKIDAGPK GVIVAFREDK FANPAGLVRY VAEQRTSAKV
     RPDMRVVFIR EFENTKQRLA GTRRILRALV EIAEKKAA
//
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