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Serine--tRNA ligase, cytoplasmic (EC 6.1.1.11) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase)

 SYSC_RAT                Reviewed;         512 AA.
Q6P799; Q8CIQ8;
09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
18-JUL-2018, entry version 121.
RecName: Full=Serine--tRNA ligase, cytoplasmic;
EC=6.1.1.11 {ECO:0000250|UniProtKB:P49591};
AltName: Full=Seryl-tRNA synthetase;
Short=SerRS;
AltName: Full=Seryl-tRNA(Ser/Sec) synthetase;
Name=Sars; Synonyms=Sars1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Prostate;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[2]
PROTEIN SEQUENCE OF 134-157, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
Lubec G., Afjehi-Sadat L.;
Submitted (NOV-2006) to UniProtKB.
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 173-349.
STRAIN=Wistar;
Heneberg P., Draber P.;
Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Catalyzes the attachment of serine to tRNA(Ser) in a
two-step reaction: serine is first activated by ATP to form Ser-
AMP and then transferred to the acceptor end of tRNA(Ser). Is
probably also able to aminoacylate tRNA(Sec) with serine, to form
the misacylated tRNA L-seryl-tRNA(Sec), which will be further
converted into selenocysteinyl-tRNA(Sec). In the nucleus, binds to
the VEGFA core promoter and prevents MYC binding and
transcriptional activation by MYC. Recruits SIRT2 to the VEGFA
promoter, promoting deacetylation of histone H4 at 'Lys-16'
(H4K16). Thereby, inhibits the production of VEGFA and sprouting
angiogenesis mediated by VEGFA. {ECO:0000250|UniProtKB:P49591}.
-!- CATALYTIC ACTIVITY: ATP + L-serine + tRNA(Ser) = AMP + diphosphate
+ L-seryl-tRNA(Ser). {ECO:0000250|UniProtKB:P49591}.
-!- CATALYTIC ACTIVITY: ATP + L-serine + tRNA(Sec) = AMP + diphosphate
+ L-seryl-tRNA(Sec). {ECO:0000250|UniProtKB:P49591}.
-!- PATHWAY: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec)
biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step
1/1.
-!- SUBUNIT: Homodimer. The tRNA molecule may bind across the dimer.
Interacts with SIRT2. {ECO:0000250|UniProtKB:P49591}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P49591}.
Nucleus {ECO:0000250|UniProtKB:P49591}. Note=Predominantly
cytoplasmic, but a minor proportion is also found in the nucleus.
{ECO:0000250|UniProtKB:P49591}.
-!- DOMAIN: Consists of two distinct domains, a catalytic core and a
N-terminal extension that is involved in tRNA binding.
{ECO:0000250|UniProtKB:P49591}.
-!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
family. Type-1 seryl-tRNA synthetase subfamily. {ECO:0000305}.
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EMBL; BC061765; AAH61765.1; -; mRNA.
EMBL; AY145052; AAN52758.1; -; mRNA.
RefSeq; NP_001007607.1; NM_001007606.1.
UniGene; Rn.73067; -.
ProteinModelPortal; Q6P799; -.
SMR; Q6P799; -.
IntAct; Q6P799; 1.
STRING; 10116.ENSRNOP00000038448; -.
iPTMnet; Q6P799; -.
PhosphoSitePlus; Q6P799; -.
PaxDb; Q6P799; -.
PRIDE; Q6P799; -.
Ensembl; ENSRNOT00000033015; ENSRNOP00000038448; ENSRNOG00000020255.
GeneID; 266975; -.
KEGG; rno:266975; -.
UCSC; RGD:628813; rat.
CTD; 6301; -.
RGD; 628813; Sars.
eggNOG; KOG2509; Eukaryota.
eggNOG; COG0172; LUCA.
GeneTree; ENSGT00790000123098; -.
HOGENOM; HOG000035937; -.
HOVERGEN; HBG023172; -.
InParanoid; Q6P799; -.
KO; K01875; -.
PhylomeDB; Q6P799; -.
UniPathway; UPA00906; UER00895.
PRO; PR:Q6P799; -.
Proteomes; UP000002494; Chromosome 2.
Bgee; ENSRNOG00000020255; -.
ExpressionAtlas; Q6P799; baseline and differential.
Genevisible; Q6P799; RN.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0004828; F:serine-tRNA ligase activity; ISS:UniProtKB.
GO; GO:0016525; P:negative regulation of angiogenesis; ISS:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
GO; GO:1904046; P:negative regulation of vascular endothelial growth factor production; ISS:UniProtKB.
GO; GO:0097056; P:selenocysteinyl-tRNA(Sec) biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0006434; P:seryl-tRNA aminoacylation; ISS:UniProtKB.
CDD; cd00770; SerRS_core; 1.
InterPro; IPR002314; aa-tRNA-synt_IIb.
InterPro; IPR006195; aa-tRNA-synth_II.
InterPro; IPR002317; Ser-tRNA-ligase_type_1.
InterPro; IPR015866; Ser-tRNA-synth_1_N.
InterPro; IPR033729; SerRS_core.
InterPro; IPR010978; tRNA-bd_arm.
PANTHER; PTHR11778; PTHR11778; 1.
Pfam; PF02403; Seryl_tRNA_N; 1.
Pfam; PF00587; tRNA-synt_2b; 1.
PIRSF; PIRSF001529; Ser-tRNA-synth_IIa; 1.
PRINTS; PR00981; TRNASYNTHSER.
SUPFAM; SSF46589; SSF46589; 1.
TIGRFAMs; TIGR00414; serS; 1.
PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
1: Evidence at protein level;
Acetylation; Aminoacyl-tRNA synthetase; ATP-binding;
Complete proteome; Cytoplasm; Direct protein sequencing; DNA-binding;
Ligase; Nucleotide-binding; Nucleus; Phosphoprotein;
Protein biosynthesis; Reference proteome.
CHAIN 1 512 Serine--tRNA ligase, cytoplasmic.
/FTId=PRO_0000270765.
NP_BIND 302 304 ATP. {ECO:0000250|UniProtKB:P49591}.
NP_BIND 318 321 ATP. {ECO:0000250|UniProtKB:P49591}.
NP_BIND 391 394 ATP. {ECO:0000250|UniProtKB:P49591}.
REGION 9 61 Interaction with tRNA.
{ECO:0000250|UniProtKB:P49591}.
MOTIF 482 494 Nuclear localization signal.
{ECO:0000250|UniProtKB:P49591}.
BINDING 271 271 L-serine. {ECO:0000250|UniProtKB:P49591}.
BINDING 302 302 L-serine. {ECO:0000250|UniProtKB:P49591}.
BINDING 325 325 L-serine. {ECO:0000250|UniProtKB:P49591}.
BINDING 427 427 L-serine. {ECO:0000250|UniProtKB:P49591}.
BINDING 429 429 Important for serine binding.
{ECO:0000250|UniProtKB:P49591}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:P49591}.
MOD_RES 241 241 Phosphoserine.
{ECO:0000250|UniProtKB:P49591}.
MOD_RES 323 323 N6-acetyllysine.
{ECO:0000250|UniProtKB:P49591}.
SEQUENCE 512 AA; 58588 MW; 960A30015F1F4A37 CRC64;
MVLDLDLFRV DKGGDPALIR ETQEKRFKDP GLVDQLVKAD SEWRRCRFRA DNLNKLKNLC
SKTIGEKMKK KEPVGEDESI PEDVLNFDDL TADTLAALKV SQIKKVRLLV DEAIQKCDGE
RVKLEAERFE NLREIGNLLH PSVPISNDED ADNKVERIWG DCTVRKKYSH VDLVVMVDGF
EGEKGAVVAG SRGYFLKGVL VFLEQALIQY ALRTLGSRGY TPIYTPFFMR KEVMQEVAQL
SQFDEELYKV IGKGSEKSDD SSYDEKYLIA TSEQPIAALH RDEWLRPEDL PIKYAGFSTC
FRQEVGSHGR DTRGIFRVHQ FEKIEQFVYS SPHDNKSWEM FDEMITTAEE FYQSLGIPYH
IVNIVSGSLN HAASKKLDLE AWFPGSGAFR ELVSCSNCTD YQARRLRIRY GQTKKMMDKV
EFVHMLNATM CATTRTICAI LENYQTEKGI VVPEKLREFM PPGLQELIPF VKPAPIDQEP
SKKQKKQHEG SKKKAKEVTL ENQLQNMEVT EA


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