位置:首页 > 蛋白库 > SYN_PYRHO
SYN_PYRHO
ID   SYN_PYRHO               Reviewed;         434 AA.
AC   O57980;
DT   31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   25-MAY-2022, entry version 137.
DE   RecName: Full=Asparagine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00534};
DE            EC=6.1.1.22 {ECO:0000255|HAMAP-Rule:MF_00534};
DE   AltName: Full=Asparaginyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00534};
DE            Short=AsnRS {ECO:0000255|HAMAP-Rule:MF_00534};
GN   Name=asnS {ECO:0000255|HAMAP-Rule:MF_00534}; OrderedLocusNames=PH0241;
OS   Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS   100139 / OT-3).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=70601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX   PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA   Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA   Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA   Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA   Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA   Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT   "Complete sequence and gene organization of the genome of a hyper-
RT   thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL   DNA Res. 5:55-76(1998).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-asparagine + tRNA(Asn) = AMP + diphosphate + H(+) + L-
CC         asparaginyl-tRNA(Asn); Xref=Rhea:RHEA:11180, Rhea:RHEA-COMP:9659,
CC         Rhea:RHEA-COMP:9674, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:58048, ChEBI:CHEBI:78442,
CC         ChEBI:CHEBI:78515, ChEBI:CHEBI:456215; EC=6.1.1.22;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00534};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00534}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BA000001; BAA29313.1; -; Genomic_DNA.
DR   PIR; B71248; B71248.
DR   RefSeq; WP_010884344.1; NC_000961.1.
DR   PDB; 1X54; X-ray; 1.45 A; A=1-434.
DR   PDB; 1X55; X-ray; 1.80 A; A=1-434.
DR   PDB; 1X56; X-ray; 1.98 A; A=1-434.
DR   PDBsum; 1X54; -.
DR   PDBsum; 1X55; -.
DR   PDBsum; 1X56; -.
DR   AlphaFoldDB; O57980; -.
DR   SMR; O57980; -.
DR   STRING; 70601.3256630; -.
DR   EnsemblBacteria; BAA29313; BAA29313; BAA29313.
DR   GeneID; 1444131; -.
DR   KEGG; pho:PH0241; -.
DR   eggNOG; arCOG00407; Archaea.
DR   OMA; DNMDLAE; -.
DR   OrthoDB; 24864at2157; -.
DR   BRENDA; 6.1.1.22; 5244.
DR   EvolutionaryTrace; O57980; -.
DR   Proteomes; UP000000752; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004816; F:asparagine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006421; P:asparaginyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.40.50.140; -; 1.
DR   Gene3D; 3.30.930.10; -; 1.
DR   HAMAP; MF_00534; Asn_tRNA_synth; 1.
DR   InterPro; IPR004364; Aa-tRNA-synt_II.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR004522; Asn-tRNA-ligase.
DR   InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR004365; NA-bd_OB_tRNA.
DR   Pfam; PF00152; tRNA-synt_2; 1.
DR   Pfam; PF01336; tRNA_anti-codon; 1.
DR   PRINTS; PR01042; TRNASYNTHASP.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF55681; SSF55681; 1.
DR   TIGRFAMs; TIGR00457; asnS; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..434
FT                   /note="Asparagine--tRNA ligase"
FT                   /id="PRO_0000176487"
FT   HELIX           7..9
FT                   /evidence="ECO:0007829|PDB:1X54"
FT   HELIX           12..14
FT                   /evidence="ECO:0007829|PDB:1X54"
FT   STRAND          18..31
FT                   /evidence="ECO:0007829|PDB:1X54"
FT   STRAND          34..41
FT                   /evidence="ECO:0007829|PDB:1X54"
FT   STRAND          44..50
FT                   /evidence="ECO:0007829|PDB:1X54"
FT   HELIX           52..55
FT                   /evidence="ECO:0007829|PDB:1X54"
FT   HELIX           57..64
FT                   /evidence="ECO:0007829|PDB:1X54"
FT   STRAND          71..80
FT                   /evidence="ECO:0007829|PDB:1X54"
FT   HELIX           85..87
FT                   /evidence="ECO:0007829|PDB:1X54"
FT   STRAND          88..99
FT                   /evidence="ECO:0007829|PDB:1X54"
FT   HELIX           110..112
FT                   /evidence="ECO:0007829|PDB:1X54"
FT   HELIX           115..120
FT                   /evidence="ECO:0007829|PDB:1X54"
FT   HELIX           122..125
FT                   /evidence="ECO:0007829|PDB:1X54"
FT   HELIX           129..151
FT                   /evidence="ECO:0007829|PDB:1X54"
FT   STRAND          161..164
FT                   /evidence="ECO:0007829|PDB:1X54"
FT   HELIX           170..172
FT                   /evidence="ECO:0007829|PDB:1X54"
FT   STRAND          175..178
FT                   /evidence="ECO:0007829|PDB:1X54"
FT   STRAND          181..185
FT                   /evidence="ECO:0007829|PDB:1X54"
FT   HELIX           190..200
FT                   /evidence="ECO:0007829|PDB:1X54"
FT   STRAND          201..210
FT                   /evidence="ECO:0007829|PDB:1X54"
FT   STRAND          222..232
FT                   /evidence="ECO:0007829|PDB:1X54"
FT   HELIX           236..257
FT                   /evidence="ECO:0007829|PDB:1X54"
FT   HELIX           259..263
FT                   /evidence="ECO:0007829|PDB:1X54"
FT   HELIX           270..273
FT                   /evidence="ECO:0007829|PDB:1X54"
FT   STRAND          281..283
FT                   /evidence="ECO:0007829|PDB:1X54"
FT   HELIX           284..293
FT                   /evidence="ECO:0007829|PDB:1X54"
FT   HELIX           306..313
FT                   /evidence="ECO:0007829|PDB:1X54"
FT   STRAND          320..326
FT                   /evidence="ECO:0007829|PDB:1X54"
FT   HELIX           327..329
FT                   /evidence="ECO:0007829|PDB:1X54"
FT   STRAND          343..351
FT                   /evidence="ECO:0007829|PDB:1X54"
FT   TURN            352..355
FT                   /evidence="ECO:0007829|PDB:1X54"
FT   STRAND          356..364
FT                   /evidence="ECO:0007829|PDB:1X54"
FT   HELIX           368..377
FT                   /evidence="ECO:0007829|PDB:1X54"
FT   HELIX           382..385
FT                   /evidence="ECO:0007829|PDB:1X54"
FT   HELIX           386..390
FT                   /evidence="ECO:0007829|PDB:1X54"
FT   TURN            391..393
FT                   /evidence="ECO:0007829|PDB:1X54"
FT   STRAND          399..405
FT                   /evidence="ECO:0007829|PDB:1X54"
FT   HELIX           406..413
FT                   /evidence="ECO:0007829|PDB:1X54"
FT   HELIX           419..422
FT                   /evidence="ECO:0007829|PDB:1X54"
FT   STRAND          423..425
FT                   /evidence="ECO:0007829|PDB:1X54"
SQ   SEQUENCE   434 AA;  50160 MW;  458F1447BC0CD1DF CRC64;
     MIEKVYCQEV KPELDGKKVR LAGWVYTNMR VGKKIFLWIR DSTGIVQAVV AKNVVGEETF
     EKAKKLGRES SVIVEGIVKA DERAPGGAEV HVEKLEVIQA VSEFPIPENP EQASPELLLD
     YRHLHIRTPK ASAIMKVKET LIMAAREWLL KDGWHEVFPP ILVTGAVEGG ATLFKLKYFD
     KYAYLSQSAQ LYLEAAIFGL EKVWSLTPSF RAEKSRTRRH LTEFWHLELE AAWMDLWDIM
     KVEEELVSYM VQRTLELRKK EIEMFRDDLT TLKNTEPPFP RISYDEAIDI LQSKGVNVEW
     GDDLGADEER VLTEEFDRPF FVYGYPKHIK AFYMKEDPND PRKVLASDML APEGYGEIIG
     GSQREDDYDK LLNRILEEGM DPKDYEWYLD LRRYGSVPHS GFGLGVERLV AWVLKLDHIR
     WAALFPRTPA RLYP
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024