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MFD_HAEIN
ID   MFD_HAEIN               Reviewed;        1146 AA.
AC   P45128;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=Transcription-repair-coupling factor {ECO:0000255|HAMAP-Rule:MF_00969};
DE            Short=TRCF {ECO:0000255|HAMAP-Rule:MF_00969};
DE            EC=3.6.4.- {ECO:0000255|HAMAP-Rule:MF_00969};
GN   Name=mfd {ECO:0000255|HAMAP-Rule:MF_00969}; OrderedLocusNames=HI_1258;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
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:0000255|HAMAP-Rule:MF_00969}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00969}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the UvrB family.
CC       {ECO:0000255|HAMAP-Rule:MF_00969}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the helicase family.
CC       RecG subfamily. {ECO:0000255|HAMAP-Rule:MF_00969}.
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DR   EMBL; L42023; AAC22905.1; -; Genomic_DNA.
DR   PIR; I64112; I64112.
DR   RefSeq; NP_439413.1; NC_000907.1.
DR   RefSeq; WP_005694314.1; NC_000907.1.
DR   AlphaFoldDB; P45128; -.
DR   SMR; P45128; -.
DR   STRING; 71421.HI_1258; -.
DR   EnsemblBacteria; AAC22905; AAC22905; HI_1258.
DR   KEGG; hin:HI_1258; -.
DR   PATRIC; fig|71421.8.peg.1310; -.
DR   eggNOG; COG1197; Bacteria.
DR   HOGENOM; CLU_005122_0_3_6; -.
DR   OMA; WAPPCRE; -.
DR   PhylomeDB; P45128; -.
DR   BioCyc; HINF71421:G1GJ1-1286-MON; -.
DR   Proteomes; UP000000579; 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:0003677; F:DNA binding; IBA:GO_Central.
DR   GO; GO:0015616; F:DNA translocase activity; IBA:GO_Central.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0043175; F:RNA polymerase core enzyme binding; IBA:GO_Central.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR   GO; GO:0000716; P:transcription-coupled nucleotide-excision repair, DNA damage recognition; IBA:GO_Central.
DR   Gene3D; 3.40.50.300; -; 2.
DR   Gene3D; 3.90.1150.50; -; 1.
DR   HAMAP; MF_00969; TRCF; 1.
DR   InterPro; IPR036101; CarD-like/TRCF_dom_sf.
DR   InterPro; IPR003711; CarD-like/TRCF_domain.
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; IPR037235; TRCF-like_C_D7.
DR   InterPro; IPR005118; TRCF_C.
DR   InterPro; IPR041471; UvrB_inter.
DR   Pfam; PF02559; CarD_CdnL_TRCF; 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; SSF141259; 1.
DR   SUPFAM; SSF143517; SSF143517; 1.
DR   SUPFAM; SSF52540; SSF52540; 4.
DR   TIGRFAMs; TIGR00580; mfd; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; DNA damage; DNA repair; DNA-binding; Helicase;
KW   Hydrolase; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..1146
FT                   /note="Transcription-repair-coupling factor"
FT                   /id="PRO_0000102167"
FT   DOMAIN          617..778
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00969"
FT   DOMAIN          800..953
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00969"
FT   MOTIF           731..734
FT                   /note="DEEH box"
FT   BINDING         630..637
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00969"
SQ   SEQUENCE   1146 AA;  130130 MW;  6E3052B431978475 CRC64;
     MKTAFFQPDI PTQPNDHKIL GNVLPGADAL AISEISEQNQ NLTVVVTPDT RSAVRLSRVL
     SELSSQDVCL FPDWETLPYD TFSPHQEIIS SRLSALFHLQ NAKKGIFLLP ISTLMQRLCP
     PQYLQHNVLL IKKGDRLVID KMRLQLEAAG YRAVEQVLEH GEYAVRGALL DLFPMGSAVP
     FRLDFFDDEI DSIRTFDVDT QRTLDEISSI NLLPAHEFPT DDKGIEFFRA QFRETFGEIR
     RDPEHIYQQI SKGTLISGIE YWQPLFFAEM ATLFDYLPEQ TLFVDMENNQ TQGERFYQDA
     KQRYEQRKVD PMRPLLSPEK LWLNVDEVNR RLKSYPRITF KAEKVRSSVR QKNLPVAALP
     EVTIQSQQKE PLGQLRQFIE HFKGNVLFSV ETEGRRETLL DLLSPLKLKP KQIQSLEQIE
     NEKFSLLVSS LEQGFIIEQS LPVAIIGEAN LLGKRIQQRS RDKRKTINPD TLVRNLAELK
     IGQPVVHLDH GVGRYGGLVT LDTGGIKAEY LLLNYANESK LYVPVTSLHL ISRYVGGSDE
     SAPLHKLGNE AWAKSRQKAA EKIRDVAAEL LDVYAQREAK KGFAFKYDRE EFQQFSATFP
     FEETYDQEMA INAVISDMCQ PKAMDRLVCG DVGFGKTEVA MRAAFLAVMN HKQVAVLVPT
     TLLAQQHYEN FKDRFANLPV NVEVLSRFKT AKEQKQILEN LAEGKVDILI GTHKLIQSDV
     KFNDLGLLII DEEHRFGVGQ KEKIKQLRAN IDILTLTATP IPRTLNMAMN GIRDLSIIST
     PPARRLSIKT FVRQNDDLVV REAILREILR GGQVYYLHND VASIENTAEK LTALVPEARV
     IVGHGQMRER ELERVMSDFY HQRYNVLVCS TIIETGIDVP TANTIIIERA DHFGLAQLHQ
     LRGRVGRSHH QAYAYLLTPP PKMMTKDAER RLDALENLDN LGAGFILATH DLEIRGAGEL
     LGNEQSGQIE SIGFSLYMEL LDAAVKALKE GREPSLEELT QQQADIELRV PALLPDDYLG
     DVNMRLSFYK RIAAAESKAE LDELKVELID RFGLLPDATK NLLQITELRL LVEPLNVVRI
     DAGTQGGFIE FSAKAQVNPD KFIQLIQKEP IVYRFDGPFK FKFMKDLSDN KVRLEFVVDL
     LRTIAA
 
 
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