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

 W0Z8E6_9MICO            Unreviewed;       421 AA.
W0Z8E6;
19-MAR-2014, integrated into UniProtKB/TrEMBL.
19-MAR-2014, sequence version 1.
27-SEP-2017, entry version 22.
RecName: Full=Serine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00176};
EC=6.1.1.11 {ECO:0000256|HAMAP-Rule:MF_00176};
AltName: Full=Seryl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00176};
Short=SerRS {ECO:0000256|HAMAP-Rule:MF_00176};
AltName: Full=Seryl-tRNA(Ser/Sec) synthetase {ECO:0000256|HAMAP-Rule:MF_00176};
Name=serS {ECO:0000256|HAMAP-Rule:MF_00176,
ECO:0000313|EMBL:CDJ99631.1};
ORFNames=MIC448_1640005 {ECO:0000313|EMBL:CDJ99631.1};
Microbacterium sp. C448.
Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae;
Microbacterium.
NCBI_TaxID=1177594 {ECO:0000313|EMBL:CDJ99631.1, ECO:0000313|Proteomes:UP000028883};
[1] {ECO:0000313|EMBL:CDJ99631.1, ECO:0000313|Proteomes:UP000028883}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C448 {ECO:0000313|EMBL:CDJ99631.1,
ECO:0000313|Proteomes:UP000028883};
PubMed=24526651; DOI=10.1128/genomeA.01113-13;
Martin-Laurent F., Marti R., Waglechner N., Wright G.D., Topp E.;
"Draft Genome Sequence of the Sulfonamide Antibiotic-Degrading
Microbacterium sp. Strain C448.";
Genome Announc. Announc.2:e01113-e01113(2014).
-!- FUNCTION: Catalyzes the attachment of serine to tRNA(Ser). Is 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). {ECO:0000256|HAMAP-
Rule:MF_00176}.
-!- CATALYTIC ACTIVITY: ATP + L-serine + tRNA(Sec) = AMP + diphosphate
+ L-seryl-tRNA(Sec). {ECO:0000256|HAMAP-Rule:MF_00176}.
-!- CATALYTIC ACTIVITY: ATP + L-serine + tRNA(Ser) = AMP + diphosphate
+ L-seryl-tRNA(Ser). {ECO:0000256|HAMAP-Rule:MF_00176}.
-!- PATHWAY: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec)
biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step
1/1. {ECO:0000256|HAMAP-Rule:MF_00176}.
-!- SUBUNIT: Homodimer. The tRNA molecule binds across the dimer.
{ECO:0000256|HAMAP-Rule:MF_00176}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00176}.
-!- DOMAIN: Consists of two distinct domains, a catalytic core and a
N-terminal extension that is involved in tRNA binding.
{ECO:0000256|HAMAP-Rule:MF_00176}.
-!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
family. Type-1 seryl-tRNA synthetase subfamily.
{ECO:0000256|HAMAP-Rule:MF_00176}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:CDJ99631.1}.
-----------------------------------------------------------------------
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EMBL; CBVQ010000073; CDJ99631.1; -; Genomic_DNA.
RefSeq; WP_036300062.1; NZ_HG779744.1.
EnsemblBacteria; CDJ99631; CDJ99631; MIC448_1640005.
UniPathway; UPA00906; UER00895.
Proteomes; UP000028883; Unassembled WGS sequence.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0004828; F:serine-tRNA ligase activity; IEA:UniProtKB-UniRule.
GO; GO:0016260; P:selenocysteine biosynthetic process; IEA:UniProtKB-UniRule.
GO; GO:0097056; P:selenocysteinyl-tRNA(Sec) biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0006434; P:seryl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
CDD; cd00770; SerRS_core; 1.
HAMAP; MF_00176; Ser_tRNA_synth_type1; 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.
3: Inferred from homology;
Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00176};
ATP-binding {ECO:0000256|HAMAP-Rule:MF_00176};
Coiled coil {ECO:0000256|SAM:Coils};
Complete proteome {ECO:0000313|Proteomes:UP000028883};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00176};
Ligase {ECO:0000256|HAMAP-Rule:MF_00176};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00176};
Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00176};
Reference proteome {ECO:0000313|Proteomes:UP000028883}.
DOMAIN 136 404 AA_TRNA_LIGASE_II.
{ECO:0000259|PROSITE:PS50862}.
NP_BIND 258 260 ATP. {ECO:0000256|HAMAP-Rule:MF_00176}.
NP_BIND 345 348 ATP. {ECO:0000256|HAMAP-Rule:MF_00176}.
REGION 227 229 Serine binding. {ECO:0000256|HAMAP-
Rule:MF_00176}.
COILED 67 94 {ECO:0000256|SAM:Coils}.
BINDING 274 274 ATP; via amide nitrogen and carbonyl
oxygen. {ECO:0000256|HAMAP-
Rule:MF_00176}.
BINDING 281 281 Serine. {ECO:0000256|HAMAP-
Rule:MF_00176}.
BINDING 380 380 Serine. {ECO:0000256|HAMAP-
Rule:MF_00176}.
SEQUENCE 421 AA; 46078 MW; D2886225BBD7AB38 CRC64;
MIDPVLLRDA PDLVTRSQVA RGHSPETVEA ALVADRERRA AITAFEELRA AQNAFGKDVA
KAPKDEKAAL VAEAKGLADR VKQAQAAVAV AEEAADAAFA KIENIIIDGV PAGGEADFVE
IRRVGEVPTF DFTPRDHLEL GELLGAIDME RGAKVSGARF YFLKGIGARL EIALMNLALN
SALEAGFVPL ITPTLVRPEI MRGTGFLGEH SDEVYHLPED DLYLTGTSEV ALAGYHKDEI
LDLADGPLRY AGWSTCYRRE AGSHGKDTRG IIRVHQFNKL EMFVYTTPEE AEAEHERLLG
WQEEMLGKLG LTYRVIDVAA GDLGSSAARK FDVEAWIPTQ DAYRELTSTS NCTTYQSRRL
DIRHRPDGGR TQPVATLNGT LATTRWIVAL LETHQRADGS VWVPEPLRPY LGGLEVLEPL
A


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