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Database: UniProt
Entry: B3DY76_METI4
LinkDB: B3DY76_METI4
Original site: B3DY76_METI4 
ID   B3DY76_METI4            Unreviewed;      1060 AA.
AC   B3DY76;
DT   22-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2008, sequence version 1.
DT   24-JAN-2024, entry version 96.
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:ACD82353.1};
GN   OrderedLocusNames=Minf_0293 {ECO:0000313|EMBL:ACD82353.1};
OS   Methylacidiphilum infernorum (isolate V4) (Methylokorus infernorum (strain
OS   V4)).
OC   Bacteria; Verrucomicrobiota; Methylacidiphilae; Methylacidiphilales;
OC   Methylacidiphilaceae; Methylacidiphilum (ex Ratnadevi et al. 2023).
OX   NCBI_TaxID=481448 {ECO:0000313|EMBL:ACD82353.1, ECO:0000313|Proteomes:UP000009149};
RN   [1] {ECO:0000313|EMBL:ACD82353.1, ECO:0000313|Proteomes:UP000009149}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate V4 {ECO:0000313|Proteomes:UP000009149};
RX   PubMed=18593465; DOI=10.1186/1745-6150-3-26;
RA   Hou S., Makarova K.S., Saw J.H., Senin P., Ly B.V., Zhou Z., Ren Y.,
RA   Wang J., Galperin M.Y., Omelchenko M.V., Wolf Y.I., Yutin N., Koonin E.V.,
RA   Stott M.B., Mountain B.W., Crowe M.A., Smirnova A.V., Dunfield P.F.,
RA   Feng L., Wang L., Alam M.;
RT   "Complete genome sequence of the extremely acidophilic methanotroph isolate
RT   V4, Methylacidiphilum infernorum, a representative of the bacterial phylum
RT   Verrucomicrobia.";
RL   Biol. Direct 3:26-26(2008).
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; CP000975; ACD82353.1; -; Genomic_DNA.
DR   AlphaFoldDB; B3DY76; -.
DR   STRING; 481448.Minf_0293; -.
DR   KEGG; min:Minf_0293; -.
DR   eggNOG; COG1197; Bacteria.
DR   HOGENOM; CLU_005122_1_3_0; -.
DR   Proteomes; UP000009149; 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; 3.40.50.300; 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};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:ACD82353.1};
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          546..707
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          728..882
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1060 AA;  121479 MW;  EB825A1F7BD66941 CRC64;
     MTANMATLNL NLQNNKEGSC PSQASKEMTF SYEKWLDHPL LKNLHHRIIE QRNCAIDSLP
     LSGQSFFLAS FLRVYRGPLL VIAENIKKTN EIALGLECWG SPYLILPEVE PVPAESLPDP
     TFLAERLSTA YSLLDFPSGI IITTEQAMEE ALPSPELLKE KRLPLAVENS FDRKAVIEKL
     VTAGYERVDS VDCRGQFAVR GAIIDTFCWD SCYPLRMEWE GNRLISLRQF DPITQRSFKP
     LAQAHLCFFN LEDMLKSGAS LHDYLPQAIP TFWSKSPEIP IPDVGIHFES HLFLDTPKGD
     WFYQERRWQL FLEALGRWIE KQWEVVIFVN NEGEESRLKE ILNNQGISTE KILFSKSPLL
     RGFCWPEAKL SILTDAEIFG RYQNQKILLR SQQKNDYFRA PLGSDIFEQW KEGDIVVHLQ
     KGICKFKGIK TIEGTNTEMV ELEFDQQAKL YVPIDQAHLI ARYIGGTKKL PKLDSLGGNR
     WIKAKRAAQK AVTDLAEKLL KINAEREVLE GFAFPQDDQW QKEFEEAFIY EETPDQLKAI
     EETKKDMESK RPMDRLICGD VGFGKTEVAI RAIFKAVMGG KQAVLLTPTT VLAKQHFNTL
     RERFADYPIH TALLCRFVKN SEEKEILAGL KEGTVDVVVG THRLLSADVE FKDLGLIVID
     EEQRFGVLQK EKWKEKFRFI DVLLLSATPI PRTLYLAMAG ARDMSLIETP PPNRFPIETI
     VGPYDERVIR QAIERELNRG GQVYFLHNRI RTIEKVASRL KSLLPSIKID IGHGRMKKHE
     LEEVMERFVE GKIDVLLATS IIENGLDIPN ANTIIIDRAD LFGLADLYQL RGRVGRSNQK
     AYAYLLLPRD LFIQSDAKKR IKAMQEHSQL GTGFQIALRD LEIRGAGNLL GTSQSGHIAS
     IGFELYCKLL KKAIQKIQGK ETEPLIDCRL SLDFLLPEPG GGRHALAYIP FSYMERRQER
     LHAYRQLAEA SQPEELEEIK KSWKDRYGPW PEPVEHLFSL VEIRIIAARK GIERVETERD
     KLKLIKNNDY LFTKQGKFPR LIEAEPKDKI LQIKKWLESF
//
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