位置:首页 > 蛋白库 > SYS2_METM5
SYS2_METM5
ID   SYS2_METM5              Reviewed;         514 AA.
AC   A4FXR4;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Type-2 serine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_01278};
DE            EC=6.1.1.11 {ECO:0000255|HAMAP-Rule:MF_01278};
DE   AltName: Full=Seryl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_01278};
DE            Short=SerRS {ECO:0000255|HAMAP-Rule:MF_01278};
DE   AltName: Full=Seryl-tRNA(Ser/Sec) synthetase {ECO:0000255|HAMAP-Rule:MF_01278};
GN   Name=serS {ECO:0000255|HAMAP-Rule:MF_01278}; OrderedLocusNames=MmarC5_0687;
OS   Methanococcus maripaludis (strain C5 / ATCC BAA-1333).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=402880;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C5 / ATCC BAA-1333;
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., Chertkov O., Brettin T., Bruce D., Han C.,
RA   Detter J.C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of chromosome of Methanococcus maripaludis C5.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the attachment of serine to tRNA(Ser). Is also able
CC       to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-
CC       seryl-tRNA(Sec), which will be further converted into selenocysteinyl-
CC       tRNA(Sec). {ECO:0000255|HAMAP-Rule:MF_01278}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-serine + tRNA(Ser) = AMP + diphosphate + H(+) + L-
CC         seryl-tRNA(Ser); Xref=Rhea:RHEA:12292, Rhea:RHEA-COMP:9669,
CC         Rhea:RHEA-COMP:9703, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:33384, ChEBI:CHEBI:78442,
CC         ChEBI:CHEBI:78533, ChEBI:CHEBI:456215; EC=6.1.1.11;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01278};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-serine + tRNA(Sec) = AMP + diphosphate + H(+) + L-
CC         seryl-tRNA(Sec); Xref=Rhea:RHEA:42580, Rhea:RHEA-COMP:9742,
CC         Rhea:RHEA-COMP:10128, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:33384, ChEBI:CHEBI:78442,
CC         ChEBI:CHEBI:78533, ChEBI:CHEBI:456215; EC=6.1.1.11;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01278};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01278};
CC       Note=Binds 1 Zn(2+) ion per subunit. This ion is coordinated with 2
CC       cysteines, 1 glutamate and a water molecule that dissociates from the
CC       zinc ion to allow the coordination of the amino group of the serine
CC       substrate, which is essential for catalysis. {ECO:0000255|HAMAP-
CC       Rule:MF_01278};
CC   -!- PATHWAY: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec)
CC       biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1.
CC       {ECO:0000255|HAMAP-Rule:MF_01278}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01278}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01278}.
CC   -!- DOMAIN: Consists of two distinct domains, a catalytic core and a N-
CC       terminal extension that is presumably involved in tRNA binding.
CC       {ECO:0000255|HAMAP-Rule:MF_01278}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       Type-2 seryl-tRNA synthetase subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_01278}.
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; CP000609; ABO34998.1; -; Genomic_DNA.
DR   RefSeq; WP_011868452.1; NC_009135.1.
DR   AlphaFoldDB; A4FXR4; -.
DR   SMR; A4FXR4; -.
DR   STRING; 402880.MmarC5_0687; -.
DR   EnsemblBacteria; ABO34998; ABO34998; MmarC5_0687.
DR   GeneID; 4928284; -.
DR   KEGG; mmq:MmarC5_0687; -.
DR   eggNOG; arCOG00403; Archaea.
DR   HOGENOM; CLU_542524_0_0_2; -.
DR   OMA; YYVCPPK; -.
DR   OrthoDB; 9543at2157; -.
DR   UniPathway; UPA00906; UER00895.
DR   Proteomes; UP000000253; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004828; F:serine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016260; P:selenocysteine biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0097056; P:selenocysteinyl-tRNA(Sec) biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006434; P:seryl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.930.10; -; 1.
DR   HAMAP; MF_01278; Ser_tRNA_synth_type2; 1.
DR   InterPro; IPR002314; aa-tRNA-synt_IIb.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR004503; Ser-tRNA-ligase_2_arc.
DR   InterPro; IPR041293; SerS_tRNA-bd.
DR   Pfam; PF00587; tRNA-synt_2b; 1.
DR   Pfam; PF18490; tRNA_bind_4; 1.
DR   SUPFAM; SSF55681; SSF55681; 1.
DR   TIGRFAMs; TIGR00415; serS_MJ; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW   Nucleotide-binding; Protein biosynthesis; Zinc.
FT   CHAIN           1..514
FT                   /note="Type-2 serine--tRNA ligase"
FT                   /id="PRO_1000165221"
FT   BINDING         313
FT                   /ligand="L-serine"
FT                   /ligand_id="ChEBI:CHEBI:33384"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01278"
FT   BINDING         315
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01278"
FT   BINDING         344..346
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01278"
FT   BINDING         344
FT                   /ligand="L-serine"
FT                   /ligand_id="ChEBI:CHEBI:33384"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01278"
FT   BINDING         355..356
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01278"
FT   BINDING         361..363
FT                   /ligand="L-serine"
FT                   /ligand_id="ChEBI:CHEBI:33384"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01278"
FT   BINDING         363
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01278"
FT   BINDING         470
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01278"
FT   BINDING         477
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01278"
SQ   SEQUENCE   514 AA;  59794 MW;  9063E6017D063228 CRC64;
     MRFKLDGRII FSKDVEEETQ KDIVEVLENR DIFLKGVPEG KENEASKIET YEFDGKDLKL
     KMTSGTYTRA HEGIVRLKKP IMEKVGRKHQ IGIRDVAIDK YIVTLTAEPS KVSELKGLKV
     PECEVELESE KINIVFENLG DGELKRNIID RAIKFVKNEL DKQDQDLTFE VCKIAPGTIV
     SDYKAKREIT FDTDPTELAE PYGWVKRFPG RGQWFYTAPM AKLFRAFESI IIEECIDKIG
     FDECLFPKLI PLDVMYKMRY LEGLPEGMYY VCPPKREPEM FQDFVNEMMI KKEIPIEKLK
     TLLRDPAYVL APAQCEPFYT FFDHELVDVD HPSKFFDKSG WTYRWEGGGA KGLDRVNEFL
     RGECVWMGTP EFVEKVRDDT LKYAEKLAEK LDLEYWTEVG DDPFYLEGRK SEARGIEFPD
     VPKYEMRLWL PHVKEERKGV AVTSANIHGT HFVEGFGIKD YKERKVWTGC TGYGLTRWVI
     GFLAQYGYNY DDWPELIQKK VGKLPEIPKV ITWP
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024