SYSM_BOVIN
ID SYSM_BOVIN Reviewed; 518 AA.
AC Q9N0F3; A5D7G7; Q58CP7; Q58DN2;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Serine--tRNA ligase, mitochondrial;
DE EC=6.1.1.11 {ECO:0000269|PubMed:10764807};
DE AltName: Full=SerRSmt;
DE AltName: Full=Seryl-tRNA synthetase;
DE Short=SerRS;
DE AltName: Full=Seryl-tRNA(Ser/Sec) synthetase;
DE Flags: Precursor;
GN Name=SARS2; Synonyms=SARSM;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 35-55; 111-145; 167-176;
RP 196-211; 396-407 AND 472-500, FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Liver;
RX PubMed=10764807; DOI=10.1074/jbc.m908473199;
RA Yokogawa T., Shimada N., Takeuchi N., Benkowski L., Suzuki T., Omori A.,
RA Ueda T., Nishikawa K., Spremulli L.L., Watanabe K.;
RT "Characterization and tRNA recognition of mammalian mitochondrial seryl-
RT tRNA synthetase.";
RL J. Biol. Chem. 275:19913-19920(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 35-518 IN COMPLEX WITH
RP SERYLADENYLATE, AND SUBUNIT.
RX PubMed=16163389; DOI=10.1038/sj.emboj.7600811;
RA Chimnaronk S., Gravers Jeppesen M., Suzuki T., Nyborg J., Watanabe K.;
RT "Dual-mode recognition of noncanonical tRNAs(Ser) by seryl-tRNA synthetase
RT in mammalian mitochondria.";
RL EMBO J. 24:3369-3379(2005).
CC -!- FUNCTION: Catalyzes the attachment of serine to tRNA(Ser). Is also
CC probably able to aminoacylate tRNA(Sec) with serine, to form the
CC misacylated tRNA L-seryl-tRNA(Sec), which will be further converted
CC into selenocysteinyl-tRNA(Sec). {ECO:0000269|PubMed:10764807}.
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:0000269|PubMed:10764807};
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:0000269|PubMed:10764807};
CC -!- PATHWAY: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec)
CC biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1.
CC -!- SUBUNIT: Homodimer. The tRNA molecule probably binds across the dimer.
CC {ECO:0000269|PubMed:16163389}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000305|PubMed:10764807}.
CC -!- DOMAIN: Consists of two distinct domains, a catalytic core and a N-
CC terminal extension that is involved in tRNA binding.
CC {ECO:0000305|PubMed:10764807}.
CC -!- PTM: Two N-termini starting at positions 35 and 37 have been identified
CC by direct sequencing. {ECO:0000269|PubMed:10764807}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Type-1 seryl-tRNA synthetase subfamily. {ECO:0000305}.
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DR EMBL; AB029947; BAA99556.1; -; mRNA.
DR EMBL; BT021565; AAX46412.1; -; mRNA.
DR EMBL; BT021900; AAX46747.1; -; mRNA.
DR EMBL; BC140548; AAI40549.1; -; mRNA.
DR RefSeq; NP_776882.1; NM_174457.3.
DR PDB; 1WLE; X-ray; 1.65 A; A/B=35-518.
DR PDBsum; 1WLE; -.
DR AlphaFoldDB; Q9N0F3; -.
DR SMR; Q9N0F3; -.
DR STRING; 9913.ENSBTAP00000002334; -.
DR PaxDb; Q9N0F3; -.
DR PRIDE; Q9N0F3; -.
DR Ensembl; ENSBTAT00000002334; ENSBTAP00000002334; ENSBTAG00000001780.
DR GeneID; 282060; -.
DR KEGG; bta:282060; -.
DR CTD; 54938; -.
DR VEuPathDB; HostDB:ENSBTAG00000001780; -.
DR eggNOG; KOG2509; Eukaryota.
DR GeneTree; ENSGT00940000153792; -.
DR HOGENOM; CLU_023797_4_1_1; -.
DR InParanoid; Q9N0F3; -.
DR OMA; SGWGWYF; -.
DR OrthoDB; 726296at2759; -.
DR BRENDA; 6.1.1.11; 908.
DR UniPathway; UPA00906; UER00895.
DR EvolutionaryTrace; Q9N0F3; -.
DR Proteomes; UP000009136; Chromosome 18.
DR Bgee; ENSBTAG00000001780; Expressed in laryngeal cartilage and 105 other tissues.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0004828; F:serine-tRNA ligase activity; IDA:UniProtKB.
DR GO; GO:0000049; F:tRNA binding; IBA:GO_Central.
DR GO; GO:0070158; P:mitochondrial seryl-tRNA aminoacylation; IBA:GO_Central.
DR GO; GO:0097056; P:selenocysteinyl-tRNA(Sec) biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006434; P:seryl-tRNA aminoacylation; IDA:UniProtKB.
DR CDD; cd00770; SerRS_core; 1.
DR Gene3D; 1.10.287.40; -; 1.
DR Gene3D; 3.30.930.10; -; 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; IPR042103; SerRS_1_N_sf.
DR InterPro; IPR033729; SerRS_core.
DR InterPro; IPR010978; tRNA-bd_arm.
DR PANTHER; PTHR11778; PTHR11778; 1.
DR Pfam; PF00587; tRNA-synt_2b; 1.
DR PRINTS; PR00981; TRNASYNTHSER.
DR SUPFAM; SSF46589; SSF46589; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00414; serS; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Aminoacyl-tRNA synthetase; ATP-binding;
KW Direct protein sequencing; Ligase; Mitochondrion; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome; Transit peptide.
FT TRANSIT 1..34
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:10764807"
FT CHAIN 35..518
FT /note="Serine--tRNA ligase, mitochondrial"
FT /id="PRO_0000035821"
FT REGION 497..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 299..301
FT /ligand="L-serine"
FT /ligand_id="ChEBI:CHEBI:33384"
FT /evidence="ECO:0000269|PubMed:16163389,
FT ECO:0007744|PDB:1WLE"
FT BINDING 330..332
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:16163389,
FT ECO:0007744|PDB:1WLE"
FT BINDING 345
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:16163389,
FT ECO:0007744|PDB:1WLE"
FT BINDING 352
FT /ligand="L-serine"
FT /ligand_id="ChEBI:CHEBI:33384"
FT /evidence="ECO:0000269|PubMed:16163389,
FT ECO:0007744|PDB:1WLE"
FT BINDING 418..421
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:16163389,
FT ECO:0007744|PDB:1WLE"
FT BINDING 453
FT /ligand="L-serine"
FT /ligand_id="ChEBI:CHEBI:33384"
FT /evidence="ECO:0000269|PubMed:16163389,
FT ECO:0007744|PDB:1WLE"
FT MOD_RES 110
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9JJL8"
FT MOD_RES 195
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9JJL8"
FT MOD_RES 337
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9JJL8"
FT CONFLICT 438
FT /note="Q -> H (in Ref. 2; AAX46747)"
FT /evidence="ECO:0000305"
FT HELIX 43..49
FT /evidence="ECO:0007829|PDB:1WLE"
FT HELIX 60..65
FT /evidence="ECO:0007829|PDB:1WLE"
FT HELIX 67..77
FT /evidence="ECO:0007829|PDB:1WLE"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:1WLE"
FT HELIX 86..124
FT /evidence="ECO:0007829|PDB:1WLE"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:1WLE"
FT HELIX 133..167
FT /evidence="ECO:0007829|PDB:1WLE"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:1WLE"
FT STRAND 187..193
FT /evidence="ECO:0007829|PDB:1WLE"
FT HELIX 205..211
FT /evidence="ECO:0007829|PDB:1WLE"
FT TURN 221..224
FT /evidence="ECO:0007829|PDB:1WLE"
FT STRAND 230..232
FT /evidence="ECO:0007829|PDB:1WLE"
FT HELIX 234..252
FT /evidence="ECO:0007829|PDB:1WLE"
FT STRAND 256..259
FT /evidence="ECO:0007829|PDB:1WLE"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:1WLE"
FT HELIX 266..272
FT /evidence="ECO:0007829|PDB:1WLE"
FT STRAND 276..280
FT /evidence="ECO:0007829|PDB:1WLE"
FT TURN 288..290
FT /evidence="ECO:0007829|PDB:1WLE"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:1WLE"
FT HELIX 300..308
FT /evidence="ECO:0007829|PDB:1WLE"
FT STRAND 311..314
FT /evidence="ECO:0007829|PDB:1WLE"
FT HELIX 315..317
FT /evidence="ECO:0007829|PDB:1WLE"
FT STRAND 319..329
FT /evidence="ECO:0007829|PDB:1WLE"
FT STRAND 341..344
FT /evidence="ECO:0007829|PDB:1WLE"
FT STRAND 346..357
FT /evidence="ECO:0007829|PDB:1WLE"
FT HELIX 361..381
FT /evidence="ECO:0007829|PDB:1WLE"
FT STRAND 386..390
FT /evidence="ECO:0007829|PDB:1WLE"
FT HELIX 393..395
FT /evidence="ECO:0007829|PDB:1WLE"
FT TURN 397..399
FT /evidence="ECO:0007829|PDB:1WLE"
FT STRAND 401..410
FT /evidence="ECO:0007829|PDB:1WLE"
FT TURN 411..414
FT /evidence="ECO:0007829|PDB:1WLE"
FT STRAND 415..424
FT /evidence="ECO:0007829|PDB:1WLE"
FT HELIX 428..433
FT /evidence="ECO:0007829|PDB:1WLE"
FT STRAND 436..438
FT /evidence="ECO:0007829|PDB:1WLE"
FT STRAND 440..442
FT /evidence="ECO:0007829|PDB:1WLE"
FT STRAND 444..446
FT /evidence="ECO:0007829|PDB:1WLE"
FT STRAND 448..456
FT /evidence="ECO:0007829|PDB:1WLE"
FT HELIX 457..468
FT /evidence="ECO:0007829|PDB:1WLE"
FT HELIX 479..481
FT /evidence="ECO:0007829|PDB:1WLE"
FT HELIX 482..485
FT /evidence="ECO:0007829|PDB:1WLE"
FT STRAND 486..490
FT /evidence="ECO:0007829|PDB:1WLE"
FT STRAND 502..505
FT /evidence="ECO:0007829|PDB:1WLE"
SQ SEQUENCE 518 AA; 58296 MW; C4411C953E842595 CRC64;
MAASIVRRLG PLVAGRGLRL RGGCVCNQSF KRSFATERQD RNLLYEHARE GYSALPLLDM
ESLCAYPEDA ARALDLRKGE LRSKDLPGII STWQELRQLR EQIRSLEEEK EAVTEAVRAL
VVNQDNSQVQ QDPQYQSLRA RGREIRKQLT LLYPKEAQLE EQFYLRALRL PNQTHPDVPV
GDESQARVLH VVGDKPAFSF QPRGHLEIAE KLDIIRQKRL SHVSGHRSYY LRGAGALLQH
GLVNFTLNKL IHRGFTPMTV PDLLRGVVFE GCGMTPNAKP SQIYNIDPSR FEDLNLAGTA
EVGLAGYFMD HSVAFRDLPI RMVCSSTCYR AETDTGKEPW GLYRVHHFTK VEMFGVTGPG
LEQSSELLEE FLSLQMEILT ELGLHFRVLD MPTQELGLPA YRKFDIEAWM PGRGRFGEVT
SASNCTDFQS RRLHIMFQTE AGELQFAHTV NATGCAVPRL LIALLESYQQ KDGSVLVPPA
LQPYLGTDRI TTPTHVPLQY IGPNQPQKPR LPGQPASS
