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TRUB_PYRAR
ID   TRUB_PYRAR              Reviewed;         331 AA.
AC   A4WH37;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Probable tRNA pseudouridine synthase B {ECO:0000255|HAMAP-Rule:MF_01081};
DE            EC=5.4.99.25 {ECO:0000255|HAMAP-Rule:MF_01081};
DE   AltName: Full=tRNA pseudouridine(55) synthase {ECO:0000255|HAMAP-Rule:MF_01081};
DE            Short=Psi55 synthase {ECO:0000255|HAMAP-Rule:MF_01081};
DE   AltName: Full=tRNA pseudouridylate synthase {ECO:0000255|HAMAP-Rule:MF_01081};
DE   AltName: Full=tRNA-uridine isomerase {ECO:0000255|HAMAP-Rule:MF_01081};
GN   Name=truB {ECO:0000255|HAMAP-Rule:MF_01081}; OrderedLocusNames=Pars_0089;
OS   Pyrobaculum arsenaticum (strain DSM 13514 / JCM 11321 / PZ6).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=340102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700994 / DSM 13514 / JCM 11321 / PZ6;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Cozen A.E.,
RA   Fitz-Gibbon S.T., House C.H., Saltikov C., Lowe T.M., Richardson P.;
RT   "Complete sequence of Pyrobaculum arsenaticum DSM 13514.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Could be responsible for synthesis of pseudouridine from
CC       uracil-55 in the psi GC loop of transfer RNAs. {ECO:0000255|HAMAP-
CC       Rule:MF_01081}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=uridine(55) in tRNA = pseudouridine(55) in tRNA;
CC         Xref=Rhea:RHEA:42532, Rhea:RHEA-COMP:10101, Rhea:RHEA-COMP:10102,
CC         ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; EC=5.4.99.25;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01081};
CC   -!- SIMILARITY: Belongs to the pseudouridine synthase TruB family. Type 2
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01081}.
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DR   EMBL; CP000660; ABP49704.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4WH37; -.
DR   SMR; A4WH37; -.
DR   STRING; 340102.Pars_0089; -.
DR   EnsemblBacteria; ABP49704; ABP49704; Pars_0089.
DR   KEGG; pas:Pars_0089; -.
DR   HOGENOM; CLU_032087_3_0_2; -.
DR   OMA; GPFKEDE; -.
DR   PhylomeDB; A4WH37; -.
DR   Proteomes; UP000001567; Chromosome.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0106029; F:tRNA pseudouridine synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0031119; P:tRNA pseudouridine synthesis; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.30.130.10; -; 1.
DR   HAMAP; MF_01081; TruB_arch; 1.
DR   InterPro; IPR012960; Dyskerin-like.
DR   InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR   InterPro; IPR002501; PsdUridine_synth_N.
DR   InterPro; IPR002478; PUA.
DR   InterPro; IPR015947; PUA-like_sf.
DR   InterPro; IPR036974; PUA_sf.
DR   InterPro; IPR004802; tRNA_PsdUridine_synth_B_fam.
DR   InterPro; IPR026326; TruB_arch.
DR   InterPro; IPR032819; TruB_C.
DR   InterPro; IPR004521; Uncharacterised_CHP00451.
DR   PANTHER; PTHR23127; PTHR23127; 1.
DR   Pfam; PF08068; DKCLD; 1.
DR   Pfam; PF01472; PUA; 1.
DR   Pfam; PF16198; TruB_C_2; 1.
DR   Pfam; PF01509; TruB_N; 1.
DR   SMART; SM01136; DKCLD; 1.
DR   SMART; SM00359; PUA; 1.
DR   SUPFAM; SSF55120; SSF55120; 1.
DR   SUPFAM; SSF88697; SSF88697; 1.
DR   TIGRFAMs; TIGR00425; CBF5; 1.
DR   TIGRFAMs; TIGR00451; unchar_dom_2; 1.
DR   PROSITE; PS50890; PUA; 1.
PE   3: Inferred from homology;
KW   Isomerase; tRNA processing.
FT   CHAIN           1..331
FT                   /note="Probable tRNA pseudouridine synthase B"
FT                   /id="PRO_1000084724"
FT   DOMAIN          238..313
FT                   /note="PUA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01081"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        71
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01081"
SQ   SEQUENCE   331 AA;  37173 MW;  F4E3B69A14997756 CRC64;
     MRCSQREVFV KREEPTNPEW GKPPSQRTAD EYIRHSFVIL DKPRGPSSHE VAAWVKKILG
     VERAGHAGTL DPKVSGVLPI AVAEGTKVLM ALSRSDKVYV AVAKFHGDVD EERLRAVLRE
     FQGEIYQKPP LRSAVKRQLR TRRVFSLELL ELEGRYAVIK MHVEAGTYAR KIIHDIGEVL
     GVGANMRELR RVAVTCFTED EAVTLQDVAD AYYIWKKYGD DTYLRSVLLP IEEIARHLPK
     IWVRDSAVDA VCHGAPLAAP GISKFEVPFS KGDIVAMFTL KGELVGIGRA LVDSEEVKKM
     ERGAVVRTDR VVMRRGTYPA MWKKGQRAAK T
 
 
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