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Database: UniProt
Entry: H2NYQ9_PONAB
LinkDB: H2NYQ9_PONAB
Original site: H2NYQ9_PONAB 
ID   H2NYQ9_PONAB            Unreviewed;       704 AA.
AC   H2NYQ9;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 3.
DT   27-MAR-2024, entry version 62.
DE   RecName: Full=serine--tRNA ligase {ECO:0000256|ARBA:ARBA00012840};
DE            EC=6.1.1.11 {ECO:0000256|ARBA:ARBA00012840};
DE   AltName: Full=Seryl-tRNA synthetase {ECO:0000256|ARBA:ARBA00031113};
DE   AltName: Full=Seryl-tRNA(Ser/Sec) synthetase {ECO:0000256|ARBA:ARBA00033352};
GN   Name=SARS2 {ECO:0000313|Ensembl:ENSPPYP00000011141.3};
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000011141.3, ECO:0000313|Proteomes:UP000001595};
RN   [1] {ECO:0000313|Ensembl:ENSPPYP00000011141.3, ECO:0000313|Proteomes:UP000001595}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Wilson R.K., Mardis E.;
RT   "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPPYP00000011141.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00001032};
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:0000256|ARBA:ARBA00001706};
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:0000256|ARBA:ARBA00005045}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       Type-1 seryl-tRNA synthetase subfamily.
CC       {ECO:0000256|ARBA:ARBA00010728}.
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DR   AlphaFoldDB; H2NYQ9; -.
DR   Ensembl; ENSPPYT00000011576.3; ENSPPYP00000011141.3; ENSPPYG00000009949.3.
DR   eggNOG; ENOG502RZA6; Eukaryota.
DR   GeneTree; ENSGT00940000153792; -.
DR   HOGENOM; CLU_068548_0_0_1; -.
DR   InParanoid; H2NYQ9; -.
DR   OrthoDB; 587001at2759; -.
DR   TreeFam; TF320527; -.
DR   UniPathway; UPA00906; UER00895.
DR   Proteomes; UP000001595; Chromosome 19.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004828; F:serine-tRNA ligase activity; IEA:InterPro.
DR   GO; GO:0006434; P:seryl-tRNA aminoacylation; IEA:InterPro.
DR   CDD; cd22169; F-box_FBXO17-like; 1.
DR   CDD; cd00770; SerRS_core; 1.
DR   Gene3D; 1.20.1280.50; -; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   InterPro; IPR002314; aa-tRNA-synt_IIb.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR007397; F-box-assoc_dom.
DR   InterPro; IPR036047; F-box-like_dom_sf.
DR   InterPro; IPR001810; F-box_dom.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR002317; Ser-tRNA-ligase_type_1.
DR   InterPro; IPR033729; SerRS_core.
DR   InterPro; IPR010978; tRNA-bd_arm.
DR   NCBIfam; TIGR00414; serS; 1.
DR   PANTHER; PTHR11778:SF7; SERINE--TRNA LIGASE, CYTOPLASMIC-RELATED; 1.
DR   PANTHER; PTHR11778; SERYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF12937; F-box-like; 1.
DR   Pfam; PF04300; FBA; 1.
DR   Pfam; PF00587; tRNA-synt_2b; 1.
DR   PRINTS; PR00981; TRNASYNTHSER.
DR   SMART; SM01198; FBA; 1.
DR   SMART; SM00256; FBOX; 1.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   SUPFAM; SSF81383; F-box domain; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF46589; tRNA-binding arm; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
DR   PROSITE; PS51114; FBA; 1.
DR   PROSITE; PS50181; FBOX; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001595}.
FT   DOMAIN          15..62
FT                   /note="F-box"
FT                   /evidence="ECO:0000259|PROSITE:PS50181"
FT   DOMAIN          99..275
FT                   /note="FBA"
FT                   /evidence="ECO:0000259|PROSITE:PS51114"
FT   DOMAIN          367..643
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   REGION          667..687
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          261..288
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   704 AA;  79252 MW;  B6A89240B9414A05 CRC64;
     MGARLSRRRL PADPSLTLDA LPPELLVQLL SHVPPRALVT RCRPVCRAWR DIVDGPTVWL
     LQLARDRSAE GRALYAVAQR CLPSKEDKEE FPLCALARYC LRAPFGRNLI FNSCGEQGFR
     GWEVEHGGNG WAIEKNLTPV PGAPSQTCFV TSFEWCSKRQ LVDLVMEGVW QELLDSAQIE
     ICVADWWGAR ENCGCVYQLR VRLLDVYEKE VVKFSASPDP VLQWTERGCR QVSHVFTNFG
     KGIRYVSFEQ YGRDISTWQE LRQLREQIRS LEEEKAAVTE GVRALLANQD SGEVQQDPKY
     QGLRARGREI RKELVHLYPR EAQLEEQFYL QALKLPNQTH PDVPVGDESQ ARVLHVVGDK
     PVFSFRPRGH LEIGEKLDII RQKRLSHVSG HRSYYLRGAG ALLQHGLVNF TFNKLLHRGF
     TPMTVPDLLR GAVFEGCGMT PNANPSQIYN IDPARFKDLN LAGTAEVGLA GYFMDHAVAF
     RDLPVRMVCS STCYRAETNT GQEPWGLYRV HHFTKVEMFG VTGPGLEQSS QLLEEFLSLQ
     MEILTELGLH FRVLDMPTQE LGLPTYRKFD IEAWMPGRGH FGEVTSASNC TDFQSRRLHI
     MFQTETGELQ FAHTVNATAC AVPRLLIALL ESNQQKDGSV LVPPALQPYL GTDRITATTH
     VPLQYIGPNQ PRKPGLPGQP ALHARAPGPR GPPLLCPCCL RVSH
//
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