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TRUB_PYRFU
ID   TRUB_PYRFU              Reviewed;         340 AA.
AC   Q7LWY0;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 109.
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=PF1785;
OS   Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=186497;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX   PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA   Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA   DiRuggiero J., Robb F.T.;
RT   "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT   horikoshii inferred from complete genomic sequences.";
RL   Genetics 152:1299-1305(1999).
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   -!- INTERACTION:
CC       Q7LWY0; Q8U1R4: nop10; NbExp=6; IntAct=EBI-9025178, EBI-9025188;
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; AE009950; AAL81909.1; -; Genomic_DNA.
DR   RefSeq; WP_011012926.1; NZ_CP023154.1.
DR   PDB; 2EY4; X-ray; 2.11 A; A/B=1-333.
DR   PDB; 2HVY; X-ray; 2.30 A; A=1-340.
DR   PDB; 2RFK; X-ray; 2.87 A; A=5-338.
DR   PDB; 3HAX; X-ray; 2.11 A; A=1-340.
DR   PDB; 3HAY; X-ray; 4.99 A; A=1-340.
DR   PDB; 3HJW; X-ray; 2.35 A; A=8-334.
DR   PDB; 3HJY; X-ray; 3.65 A; A=8-334.
DR   PDB; 3LWO; X-ray; 2.86 A; A=1-340.
DR   PDB; 3LWP; X-ray; 2.50 A; A=1-340.
DR   PDB; 3LWQ; X-ray; 2.68 A; A=1-340.
DR   PDB; 3LWR; X-ray; 2.20 A; A=1-340.
DR   PDB; 3LWV; X-ray; 2.50 A; A=1-340.
DR   PDB; 3MQK; X-ray; 2.80 A; A=8-335.
DR   PDBsum; 2EY4; -.
DR   PDBsum; 2HVY; -.
DR   PDBsum; 2RFK; -.
DR   PDBsum; 3HAX; -.
DR   PDBsum; 3HAY; -.
DR   PDBsum; 3HJW; -.
DR   PDBsum; 3HJY; -.
DR   PDBsum; 3LWO; -.
DR   PDBsum; 3LWP; -.
DR   PDBsum; 3LWQ; -.
DR   PDBsum; 3LWR; -.
DR   PDBsum; 3LWV; -.
DR   PDBsum; 3MQK; -.
DR   AlphaFoldDB; Q7LWY0; -.
DR   SMR; Q7LWY0; -.
DR   DIP; DIP-48526N; -.
DR   IntAct; Q7LWY0; 1.
DR   STRING; 186497.PF1785; -.
DR   PRIDE; Q7LWY0; -.
DR   EnsemblBacteria; AAL81909; AAL81909; PF1785.
DR   GeneID; 41713603; -.
DR   KEGG; pfu:PF1785; -.
DR   PATRIC; fig|186497.12.peg.1856; -.
DR   eggNOG; arCOG00987; Archaea.
DR   HOGENOM; CLU_032087_3_0_2; -.
DR   OMA; GPFKEDE; -.
DR   OrthoDB; 36028at2157; -.
DR   PhylomeDB; Q7LWY0; -.
DR   EvolutionaryTrace; Q7LWY0; -.
DR   Proteomes; UP000001013; 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; 2.
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   1: Evidence at protein level;
KW   3D-structure; Isomerase; Reference proteome; tRNA processing.
FT   CHAIN           1..340
FT                   /note="Probable tRNA pseudouridine synthase B"
FT                   /id="PRO_0000121968"
FT   DOMAIN          250..325
FT                   /note="PUA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01081"
FT   ACT_SITE        82
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01081"
FT   HELIX           11..13
FT                   /evidence="ECO:0007829|PDB:2EY4"
FT   STRAND          18..21
FT                   /evidence="ECO:0007829|PDB:2EY4"
FT   HELIX           35..37
FT                   /evidence="ECO:0007829|PDB:2EY4"
FT   HELIX           40..45
FT                   /evidence="ECO:0007829|PDB:2EY4"
FT   STRAND          47..53
FT                   /evidence="ECO:0007829|PDB:2EY4"
FT   STRAND          55..57
FT                   /evidence="ECO:0007829|PDB:2EY4"
FT   HELIX           59..69
FT                   /evidence="ECO:0007829|PDB:2EY4"
FT   STRAND          75..79
FT                   /evidence="ECO:0007829|PDB:2EY4"
FT   STRAND          86..93
FT                   /evidence="ECO:0007829|PDB:2EY4"
FT   HELIX           94..99
FT                   /evidence="ECO:0007829|PDB:2EY4"
FT   HELIX           100..103
FT                   /evidence="ECO:0007829|PDB:2EY4"
FT   STRAND          104..106
FT                   /evidence="ECO:0007829|PDB:2RFK"
FT   STRAND          108..118
FT                   /evidence="ECO:0007829|PDB:2EY4"
FT   HELIX           122..130
FT                   /evidence="ECO:0007829|PDB:2EY4"
FT   STRAND          133..138
FT                   /evidence="ECO:0007829|PDB:2EY4"
FT   STRAND          142..144
FT                   /evidence="ECO:0007829|PDB:2EY4"
FT   STRAND          151..164
FT                   /evidence="ECO:0007829|PDB:2EY4"
FT   STRAND          167..174
FT                   /evidence="ECO:0007829|PDB:2EY4"
FT   HELIX           180..190
FT                   /evidence="ECO:0007829|PDB:2EY4"
FT   STRAND          191..193
FT                   /evidence="ECO:0007829|PDB:3HAX"
FT   STRAND          195..205
FT                   /evidence="ECO:0007829|PDB:2EY4"
FT   STRAND          208..211
FT                   /evidence="ECO:0007829|PDB:2EY4"
FT   STRAND          214..216
FT                   /evidence="ECO:0007829|PDB:3HJW"
FT   HELIX           217..230
FT                   /evidence="ECO:0007829|PDB:2EY4"
FT   HELIX           234..238
FT                   /evidence="ECO:0007829|PDB:2EY4"
FT   STRAND          240..242
FT                   /evidence="ECO:0007829|PDB:2EY4"
FT   HELIX           243..247
FT                   /evidence="ECO:0007829|PDB:2EY4"
FT   STRAND          252..255
FT                   /evidence="ECO:0007829|PDB:2EY4"
FT   HELIX           257..263
FT                   /evidence="ECO:0007829|PDB:2EY4"
FT   TURN            264..266
FT                   /evidence="ECO:0007829|PDB:2EY4"
FT   HELIX           271..273
FT                   /evidence="ECO:0007829|PDB:2EY4"
FT   STRAND          274..278
FT                   /evidence="ECO:0007829|PDB:2EY4"
FT   STRAND          286..291
FT                   /evidence="ECO:0007829|PDB:2EY4"
FT   STRAND          296..304
FT                   /evidence="ECO:0007829|PDB:2EY4"
FT   HELIX           306..311
FT                   /evidence="ECO:0007829|PDB:2EY4"
FT   STRAND          314..323
FT                   /evidence="ECO:0007829|PDB:2EY4"
SQ   SEQUENCE   340 AA;  38561 MW;  76CFE5095C5562FC CRC64;
     MARDEVRRIL PADIKREVLI KDENAETNPD WGFPPEKRPI EMHIQFGVIN LDKPPGPTSH
     EVVAWIKKIL NLEKAGHGGT LDPKVSGVLP VALEKATRVV QALLPAGKEY VALMHLHGDV
     PEDKIIQVMK EFEGEIIQRP PLRSAVKRRL RTRKVYYIEV LEIEGRDVLF RVGVEAGTYI
     RSLIHHIGLA LGVGAHMSEL RRTRSGPFKE DETLITLHDL VDYYYFWKED GIEEYFRKAI
     QPMEKAVEHL PKVWIKDSAV AAVTHGADLA VPGIAKLHAG IKRGDLVAIM TLKDELVALG
     KAMMTSQEML EKTKGIAVDV EKVFMPRDWY PKLWEKRDRS
 
 
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