位置:首页 > 蛋白库 > SYDND_SULTO
SYDND_SULTO
ID   SYDND_SULTO             Reviewed;         429 AA.
AC   Q976I3; F9VMP5;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Aspartate--tRNA(Asp/Asn) ligase {ECO:0000255|HAMAP-Rule:MF_02075};
DE            EC=6.1.1.23 {ECO:0000255|HAMAP-Rule:MF_02075};
DE   AltName: Full=Aspartyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02075};
DE            Short=AspRS {ECO:0000255|HAMAP-Rule:MF_02075};
DE   AltName: Full=Non-discriminating aspartyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02075};
DE            Short=ND-AspRS {ECO:0000255|HAMAP-Rule:MF_02075};
GN   Name=aspS {ECO:0000255|HAMAP-Rule:MF_02075}; OrderedLocusNames=STK_02050;
OS   Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS   (Sulfolobus tokodaii).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfurisphaera.
OX   NCBI_TaxID=273063;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX   PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA   Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA   Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA   Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA   Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT   "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT   Sulfolobus tokodaii strain7.";
RL   DNA Res. 8:123-140(2001).
CC   -!- FUNCTION: Aspartyl-tRNA synthetase with relaxed tRNA specificity since
CC       it is able to aspartylate not only its cognate tRNA(Asp) but also
CC       tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first
CC       activated by ATP to form Asp-AMP and then transferred to the acceptor
CC       end of tRNA(Asp/Asn). {ECO:0000255|HAMAP-Rule:MF_02075}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-aspartate + tRNA(Asx) = AMP + diphosphate + L-
CC         aspartyl-tRNA(Asx); Xref=Rhea:RHEA:18349, Rhea:RHEA-COMP:9710,
CC         Rhea:RHEA-COMP:9711, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78516,
CC         ChEBI:CHEBI:456215; EC=6.1.1.23; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_02075};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_02075};
CC       Note=Binds 3 Mg(2+) cations per subunit. The strongest magnesium site
CC       (Mg1) is bound to the beta- and gamma-phosphates of ATP and four water
CC       molecules complete its coordination sphere. {ECO:0000255|HAMAP-
CC       Rule:MF_02075};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02075}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02075}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       Type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_02075}.
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; BA000023; BAK54191.1; -; Genomic_DNA.
DR   RefSeq; WP_010978146.1; NC_003106.2.
DR   PDB; 1WYD; X-ray; 2.30 A; A/B=1-429.
DR   PDBsum; 1WYD; -.
DR   AlphaFoldDB; Q976I3; -.
DR   SMR; Q976I3; -.
DR   STRING; 273063.STK_02050; -.
DR   EnsemblBacteria; BAK54191; BAK54191; STK_02050.
DR   GeneID; 1458094; -.
DR   KEGG; sto:STK_02050; -.
DR   PATRIC; fig|273063.9.peg.252; -.
DR   eggNOG; arCOG00406; Archaea.
DR   OMA; WVHEIRD; -.
DR   OrthoDB; 24288at2157; -.
DR   EvolutionaryTrace; Q976I3; -.
DR   Proteomes; UP000001015; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004815; F:aspartate-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0050560; F:aspartate-tRNA(Asn) ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006422; P:aspartyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.40.50.140; -; 1.
DR   Gene3D; 3.30.930.10; -; 1.
DR   HAMAP; MF_02075; Asp_tRNA_synth_type2; 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; IPR004523; Asp-tRNA_synthase_2.
DR   InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR004365; NA-bd_OB_tRNA.
DR   PANTHER; PTHR43450; PTHR43450; 1.
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; TIGR00458; aspS_nondisc; 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   Magnesium; Metal-binding; Nucleotide-binding; Protein biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..429
FT                   /note="Aspartate--tRNA(Asp/Asn) ligase"
FT                   /id="PRO_0000111007"
FT   REGION          189..192
FT                   /note="Aspartate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02075"
FT   BINDING         167
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02075"
FT   BINDING         210..212
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02075"
FT   BINDING         210
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02075"
FT   BINDING         352
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02075"
FT   BINDING         352
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02075"
FT   BINDING         352
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02075"
FT   BINDING         355
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02075"
FT   BINDING         355
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02075"
FT   BINDING         359
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02075"
FT   BINDING         400..403
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02075"
FT   SITE            82
FT                   /note="Important for tRNA non-discrimination"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02075"
FT   TURN            7..9
FT                   /evidence="ECO:0007829|PDB:1WYD"
FT   HELIX           12..14
FT                   /evidence="ECO:0007829|PDB:1WYD"
FT   STRAND          18..31
FT                   /evidence="ECO:0007829|PDB:1WYD"
FT   STRAND          34..41
FT                   /evidence="ECO:0007829|PDB:1WYD"
FT   STRAND          44..50
FT                   /evidence="ECO:0007829|PDB:1WYD"
FT   HELIX           57..60
FT                   /evidence="ECO:0007829|PDB:1WYD"
FT   STRAND          68..77
FT                   /evidence="ECO:0007829|PDB:1WYD"
FT   STRAND          79..81
FT                   /evidence="ECO:0007829|PDB:1WYD"
FT   HELIX           82..84
FT                   /evidence="ECO:0007829|PDB:1WYD"
FT   STRAND          85..96
FT                   /evidence="ECO:0007829|PDB:1WYD"
FT   STRAND          106..108
FT                   /evidence="ECO:0007829|PDB:1WYD"
FT   HELIX           114..119
FT                   /evidence="ECO:0007829|PDB:1WYD"
FT   HELIX           121..125
FT                   /evidence="ECO:0007829|PDB:1WYD"
FT   HELIX           128..150
FT                   /evidence="ECO:0007829|PDB:1WYD"
FT   STRAND          160..164
FT                   /evidence="ECO:0007829|PDB:1WYD"
FT   STRAND          174..177
FT                   /evidence="ECO:0007829|PDB:1WYD"
FT   STRAND          180..184
FT                   /evidence="ECO:0007829|PDB:1WYD"
FT   HELIX           189..199
FT                   /evidence="ECO:0007829|PDB:1WYD"
FT   STRAND          200..209
FT                   /evidence="ECO:0007829|PDB:1WYD"
FT   STRAND          216..218
FT                   /evidence="ECO:0007829|PDB:1WYD"
FT   STRAND          221..231
FT                   /evidence="ECO:0007829|PDB:1WYD"
FT   HELIX           235..256
FT                   /evidence="ECO:0007829|PDB:1WYD"
FT   HELIX           258..264
FT                   /evidence="ECO:0007829|PDB:1WYD"
FT   STRAND          276..279
FT                   /evidence="ECO:0007829|PDB:1WYD"
FT   HELIX           280..289
FT                   /evidence="ECO:0007829|PDB:1WYD"
FT   HELIX           302..312
FT                   /evidence="ECO:0007829|PDB:1WYD"
FT   STRAND          315..320
FT                   /evidence="ECO:0007829|PDB:1WYD"
FT   HELIX           324..326
FT                   /evidence="ECO:0007829|PDB:1WYD"
FT   STRAND          340..348
FT                   /evidence="ECO:0007829|PDB:1WYD"
FT   STRAND          351..359
FT                   /evidence="ECO:0007829|PDB:1WYD"
FT   HELIX           363..372
FT                   /evidence="ECO:0007829|PDB:1WYD"
FT   HELIX           377..380
FT                   /evidence="ECO:0007829|PDB:1WYD"
FT   HELIX           381..384
FT                   /evidence="ECO:0007829|PDB:1WYD"
FT   HELIX           385..388
FT                   /evidence="ECO:0007829|PDB:1WYD"
FT   STRAND          394..400
FT                   /evidence="ECO:0007829|PDB:1WYD"
FT   HELIX           401..409
FT                   /evidence="ECO:0007829|PDB:1WYD"
FT   HELIX           414..416
FT                   /evidence="ECO:0007829|PDB:1WYD"
FT   STRAND          418..420
FT                   /evidence="ECO:0007829|PDB:1WYD"
SQ   SEQUENCE   429 AA;  49074 MW;  5BABA8F4D9437D69 CRC64;
     MYRSHFIADV TPEYDGKEVI WAGWVHLLRD LGGKKFIILR DKTGLGQVVV DKNSSAFGIS
     QELTQESVIQ VRGIVKADKR APRGIELHAE EITLLSKAKA PLPLDVSGKV KADIDTRLRE
     RVLDLRRQEM QAVIKIQSLA LKAFRETLYK EGFIEIFTPK IIASATEGGA QLFPVIYFGK
     EAFLAQSPQL YKELMAGVVE RVFEVAPAWR AEESDTPFHL AEFISMDVEM AFADYNDVMQ
     LLEKILHNIV KTIKEEGKEE LKILNYEPPE VKIPIKRLKY TEAIEILRSK GYNIKFGDDI
     GTPELRILNE ELKEDLYFIV DWPSDARPFY TKSKSENPEL SESFDLIYKF LEIVSGSTRN
     HKREVLEEAL KKKGLKPESF EFFLKWFDYG MPPHAGFGMG LARLMVMLTG IQSVKEIVPF
     PRDKKRLTP
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024