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Database: UniProt
Entry: A0A2K5Z4P6_MANLE
LinkDB: A0A2K5Z4P6_MANLE
Original site: A0A2K5Z4P6_MANLE 
ID   A0A2K5Z4P6_MANLE        Unreviewed;       448 AA.
AC   A0A2K5Z4P6;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 29.
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=SARS1 {ECO:0000313|Ensembl:ENSMLEP00000022777.1};
OS   Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Mandrillus.
OX   NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000022777.1, ECO:0000313|Proteomes:UP000233140};
RN   [1] {ECO:0000313|Ensembl:ENSMLEP00000022777.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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; A0A2K5Z4P6; -.
DR   STRING; 9568.ENSMLEP00000022777; -.
DR   Ensembl; ENSMLET00000046289.1; ENSMLEP00000022777.1; ENSMLEG00000035592.1.
DR   GeneTree; ENSGT00940000153792; -.
DR   OMA; MNDSACL; -.
DR   UniPathway; UPA00906; UER00895.
DR   Proteomes; UP000233140; Unplaced.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
DR   GO; GO:0060090; F:molecular adaptor activity; IEA:Ensembl.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:Ensembl.
DR   GO; GO:0098619; F:selenocysteine-tRNA ligase activity; IEA:Ensembl.
DR   GO; GO:0004828; F:serine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0002181; P:cytoplasmic translation; IEA:Ensembl.
DR   GO; GO:0016525; P:negative regulation of angiogenesis; IEA:Ensembl.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:1904046; P:negative regulation of vascular endothelial growth factor production; IEA:Ensembl.
DR   GO; GO:0001514; P:selenocysteine incorporation; IEA:Ensembl.
DR   GO; GO:0006434; P:seryl-tRNA aminoacylation; IEA:Ensembl.
DR   GO; GO:0006400; P:tRNA modification; IEA:Ensembl.
DR   Gene3D; 1.10.287.40; Serine-tRNA synthetase, tRNA binding domain; 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; IPR002317; Ser-tRNA-ligase_type_1.
DR   InterPro; IPR015866; Ser-tRNA-synth_1_N.
DR   InterPro; IPR042103; SerRS_1_N_sf.
DR   InterPro; IPR010978; tRNA-bd_arm.
DR   PANTHER; PTHR11778:SF7; SERINE--TRNA LIGASE, CYTOPLASMIC-RELATED; 1.
DR   PANTHER; PTHR11778; SERYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF02403; Seryl_tRNA_N; 1.
DR   Pfam; PF00587; tRNA-synt_2b; 1.
DR   PIRSF; PIRSF001529; Ser-tRNA-synth_IIa; 3.
DR   PRINTS; PR00981; TRNASYNTHSER.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   SUPFAM; SSF46589; tRNA-binding arm; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233140}.
FT   DOMAIN          224..356
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   REGION          408..448
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        412..434
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   448 AA;  51146 MW;  39D39B83E42E9BAF CRC64;
     VLDLDLFRVD KGGDPALIRE TQEKRFKDPG LVDQLVKADS EWRRCRFRAD NLNKLKNLCS
     KTIGEKMKVR ELRNEQPALL ILSYNSLTNL KVSQIKKVRL LIDEAILKCD AERIKLEAER
     FENLREIGNL LHPSVPISND EDADNKVERI WGDCTVRKKY SHVDLVVMVD GFEGEKGLNS
     KVYSLRIITT NLYAPRKQRL VSFLPQVIGK GSEKSDDNSY DEKYLIATSE QPIAALHRDE
     WLRPEDLPIK YAGLSTCFRQ EVGSHGRDTR GIFRVHQFEK IEQFVYSSPH DNKSWEMFEE
     MITTAEEFYQ SLGIPYHIVN IVSGMGPSLF PASLSCIPQT VEPDFPSGTL SFQVEFVHML
     NATMCATTRT ICAILENYQT EKGITVPEKL KEFMPPGLQE LIPFVKPAPI DQEPSKKQKK
     QHEGSKKKAA ARDVTLESRL QNMEVTDA
//
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