GENTAUR Belgium BVBA BE0473327336 Voortstraat 49, 1910 Kampenhout BELGIUM Tel 0032 16 58 90 45
GENTAUR U.S.A Genprice Inc,Logistics 547 Yurok Circle, SanJose, CA 95123
Tel (408) 780-0908, Fax (408) 780-0908, [email protected]

Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, Gentaur another in time delivery

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

 J7WWV7_BACCE            Unreviewed;       424 AA.
J7WWV7;
31-OCT-2012, integrated into UniProtKB/TrEMBL.
31-OCT-2012, sequence version 1.
16-JAN-2019, entry version 31.
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};
ORFNames=IEE_05389 {ECO:0000313|EMBL:EJQ36423.1};
Bacillus cereus BAG5X1-1.
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
Bacillus cereus group.
NCBI_TaxID=1053189 {ECO:0000313|EMBL:EJQ36423.1, ECO:0000313|Proteomes:UP000006600};
[1] {ECO:0000313|EMBL:EJQ36423.1, ECO:0000313|Proteomes:UP000006600}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=BAG5X1-1 {ECO:0000313|EMBL:EJQ36423.1,
ECO:0000313|Proteomes:UP000006600};
The Broad Institute Genome Sequencing Platform;
The Broad Institute Genome Sequencing Center for Infectious Disease;
Feldgarden M., Van der Auwera G.A., Mahillon J., Duprez V.,
Timmery S., Mattelet C., Dierick K., Sun M., Yu Z., Zhu L., Hu X.,
Shank E.B., Swiecicka I., Hansen B.M., Andrup L., Young S.K., Zeng Q.,
Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
Arachchi H.M., Berlin A., Chapman S.B., Goldberg J., Griggs A.,
Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C.,
Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M.,
Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
Nusbaum C., Birren B.;
"The Genome Sequence of Bacillus cereus BAG5X1-1.";
Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
-!- 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:
Reaction=ATP + L-serine + tRNA(Sec) = AMP + diphosphate + H(+) +
L-seryl-tRNA(Sec); Xref=Rhea:RHEA:42580, Rhea:RHEA-COMP:9742,
Rhea:RHEA-COMP:10128, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
ChEBI:CHEBI:33019, ChEBI:CHEBI:33384, ChEBI:CHEBI:78442,
ChEBI:CHEBI:78533, ChEBI:CHEBI:456215; EC=6.1.1.11;
Evidence={ECO:0000256|HAMAP-Rule:MF_00176};
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-serine + tRNA(Ser) = AMP + diphosphate + H(+) +
L-seryl-tRNA(Ser); Xref=Rhea:RHEA:12292, Rhea:RHEA-COMP:9669,
Rhea:RHEA-COMP:9703, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
ChEBI:CHEBI:33019, ChEBI:CHEBI:33384, ChEBI:CHEBI:78442,
ChEBI:CHEBI:78533, ChEBI:CHEBI:456215; EC=6.1.1.11;
Evidence={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: Lacks conserved residue(s) required for the propagation
of feature annotation. {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:EJQ36423.1}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AHDJ01000070; EJQ36423.1; -; Genomic_DNA.
RefSeq; WP_002107270.1; NZ_JH791999.1.
EnsemblBacteria; EJQ36423; EJQ36423; IEE_05389.
PATRIC; fig|1053189.3.peg.5493; -.
UniPathway; UPA00906; UER00895.
Proteomes; UP000006600; 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; PTHR43697; PTHR43697; 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,
ECO:0000313|EMBL:EJQ36423.1};
ATP-binding {ECO:0000256|HAMAP-Rule:MF_00176};
Coiled coil {ECO:0000256|SAM:Coils};
Complete proteome {ECO:0000313|Proteomes:UP000006600};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00176};
Ligase {ECO:0000256|HAMAP-Rule:MF_00176, ECO:0000313|EMBL:EJQ36423.1};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00176};
Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00176}.
DOMAIN 172 410 AA_TRNA_LIGASE_II.
{ECO:0000259|PROSITE:PS50862}.
NP_BIND 262 264 ATP. {ECO:0000256|HAMAP-Rule:MF_00176}.
NP_BIND 349 352 ATP. {ECO:0000256|HAMAP-Rule:MF_00176}.
REGION 231 233 Serine binding. {ECO:0000256|HAMAP-
Rule:MF_00176}.
COILED 31 103 {ECO:0000256|SAM:Coils}.
BINDING 285 285 Serine. {ECO:0000256|HAMAP-
Rule:MF_00176}.
BINDING 385 385 Serine. {ECO:0000256|HAMAP-
Rule:MF_00176}.
SEQUENCE 424 AA; 48763 MW; 1A9A638BAECAFD5F CRC64;
MLDIKFLRTN FEEVKAKLQH RGEDLTDFGR FEELDTRRRE LLVQTEELKS KRNEVSQQIS
VLKREKKDAE ALILEMREVG EKVKDLDNEL RTVEEDLERL MLSIPNIPHE SAPVGETEDD
NVVARTWGEV KEFTYEPKPH WDLATDLGIL DFERAGKVTG SRFVFYKGAG ARLERALISF
MLDLHTDEHG YEEVLPPYMV NRASMTGTGQ LPKFEEDAFR IESEDYFLIP TAEVPVTNMH
RDEILSKEQL PIRYAAFSSC FRSEAGSAGR DTRGLIRQHQ FNKVELVKFV KPEDSYEELE
KLTNDAERVL QLLELPYRVM SMCTGDLGFT AAKKYDIEVW IPSYGTYREI SSCSNFEAFQ
ARRANIRFRR EPNGKPEHVH TLNGSGLAIG RTVAAILENY QQEDGTIIIP EVLRPYMGGK
TVIK


Related products :

Catalog number Product name Quantity
EIAAB40853 Homo sapiens,Human,SARS2,SARSM,Serine--tRNA ligase,SerRS,SerRSmt,Seryl-tRNA synthetase, mitochondrial,Seryl-tRNA(Ser_Sec) synthetase
EIAAB40854 Mouse,Mus musculus,Sars2,Sarsm,Serine--tRNA ligase,SerRS,SerRSmt,Seryl-tRNA synthetase, mitochondrial,Seryl-tRNA(Ser_Sec) synthetase
EIAAB40855 Bos taurus,Bovine,SARS2,SARSM,Serine--tRNA ligase,SerRS,SerRSmt,Seryl-tRNA synthetase, mitochondrial,Seryl-tRNA(Ser_Sec) synthetase
EIAAB40848 Homo sapiens,Human,SARS,Serine--tRNA ligase,SerRS,SERS,Seryl-tRNA synthetase, cytoplasmic,Seryl-tRNA(Ser_Sec) synthetase
EIAAB40851 Mouse,Mus musculus,Sars,Sars1,Serine--tRNA ligase,SerRS,Sers,Seryl-tRNA synthetase, cytoplasmic,Seryl-tRNA(Ser_Sec) synthetase
EIAAB40852 62 kDa RNA-binding protein,Oryctolagus cuniculus,Rabbit,SARS,Serine--tRNA ligase,SerRS,SERS,Seryl-tRNA synthetase, cytoplasmic,Seryl-tRNA(Ser_Sec) synthetase
EIAAB40850 Rat,Rattus norvegicus,Sars,Sars1,Serine--tRNA ligase,SerRS,Seryl-tRNA synthetase, cytoplasmic,Seryl-tRNA(Ser_Sec) synthetase
EIAAB40849 Bos taurus,Bovine,SARS,Serine--tRNA ligase,SerRS,SERS,Seryl-tRNA synthetase, cytoplasmic,Seryl-tRNA(Ser_Sec) synthetase
18-003-44206 Seryl-tRNA synthetase. cytoplasmic - EC 6.1.1.11; Seryl-tRNA(Ser_Sec) synthetase; Serine--tRNA ligase; SerRS Polyclonal 0.1 mg Protein A
18-003-44205 Seryl-tRNA synthetase. cytoplasmic - EC 6.1.1.11; Seryl-tRNA(Ser_Sec) synthetase; Serine--tRNA ligase; SerRS Polyclonal 0.1 mg Protein A
29-249 CARS is a class 1 aminoacyl-tRNA synthetase, cysteinyl-tRNA synthetase. Each of the twenty aminoacyl-tRNA synthetases catalyzes the aminoacylation of a specific tRNA or tRNA isoaccepting family with t 0.05 mg
25-598 CARS is a class 1 aminoacyl-tRNA synthetase, cysteinyl-tRNA synthetase. Each of the twenty aminoacyl-tRNA synthetases catalyzes the aminoacylation of a specific tRNA or tRNA isoaccepting family with t 0.05 mg
29-250 CARS is a class 1 aminoacyl-tRNA synthetase, cysteinyl-tRNA synthetase. Each of the twenty aminoacyl-tRNA synthetases catalyzes the aminoacylation of a specific tRNA or tRNA isoaccepting family with t 0.05 mg
EIAAB40744 AP-4-A synthetase,Diadenosine tetraphosphate synthetase,Gars,Glycine--tRNA ligase,Glycyl-tRNA synthetase,GlyRS,Rat,Rattus norvegicus
EIAAB40743 AP-4-A synthetase,Diadenosine tetraphosphate synthetase,Gars,Glycine--tRNA ligase,Glycyl-tRNA synthetase,GlyRS,Mouse,Mus musculus
EIAAB40742 AP-4-A synthetase,Diadenosine tetraphosphate synthetase,GARS,Glycine--tRNA ligase,Glycyl-tRNA synthetase,GlyRS,Homo sapiens,Human
EIAAB40938 Homo sapiens,Human,KIAA1885,Valine--tRNA ligase,ValRS,Valyl-tRNA synthetase, mitochondrial,Valyl-tRNA synthetase-like,VARS2,VARS2L,VARSL
EIAAB40844 Arginine--tRNA ligase,Arginyl-tRNA synthetase-like,ArgRS,Homo sapiens,Human,Probable arginyl-tRNA synthetase, mitochondrial,RARS2,RARSL
EIAAB40912 Homo sapiens,Human,Probable threonyl-tRNA synthetase 2, cytoplasmic,TARSL2,Threonine--tRNA ligase,Threonyl-tRNA synthetase-like protein 2,ThrRS
EIAAB40928 Homo sapiens,Human,TARS2,TARSL1,Threonine--tRNA ligase,Threonyl-tRNA synthetase, mitochondrial,Threonyl-tRNA synthetase-like 1,ThrRS
EIAAB40843 Arginine--tRNA ligase,Arginyl-tRNA synthetase-like,ArgRS,Bos taurus,Bovine,Probable arginyl-tRNA synthetase, mitochondrial,RARS2,RARSL
EIAAB40911 Bos taurus,Bovine,Probable threonyl-tRNA synthetase 2, cytoplasmic,TARSL2,Threonine--tRNA ligase,Threonyl-tRNA synthetase-like protein 2,ThrRS
EIAAB40842 Arginine--tRNA ligase,Arginyl-tRNA synthetase-like,ArgRS,Mouse,Mus musculus,Probable arginyl-tRNA synthetase, mitochondrial,Rars2,Rarsl
EIAAB40910 Mouse,Mus musculus,Probable threonyl-tRNA synthetase 2, cytoplasmic,Tarsl2,Threonine--tRNA ligase,Threonyl-tRNA synthetase-like protein 2,ThrRS
EIAAB40926 Mouse,Mus musculus,Tars2,Tarsl1,Threonine--tRNA ligase,Threonyl-tRNA synthetase, mitochondrial,Threonyl-tRNA synthetase-like 1,ThrRS

Kits Elisa; taq POLYMERASE

Search in Google:

google

Share this page:
share on twitter rss feedsfacebookgoogle gentaur



Quick order!
Enter catalog number :


Gentaur; yes we can

Pathways :
WP219: Cytoplasmic tRNA Synthetases
WP433: tRNA Synthetases
WP106: Alanine and aspartate metabolism
WP1620: Aminoacyl-tRNA biosynthesis
WP1938: tRNA Aminoacylation
WP2199: Seed Development
WP62: Mitochondrial tRNA Synthetases
WP1577: amino acid conjugation of benzoic acid
WP1708: Terpenoid backbone biosynthesis
WP2211: Geranylgeranyldiphosphate biosynthesis II (plastidic)
WP521: amino acid conjugation of benzoic acid
WP1097: Non-homologous end joining
WP1201: Non-homologous end joining
WP1208: Non-homologous end joining
WP1222: Non-homologous end joining
WP1242: Non-homologous end joining
WP1277: Non-homologous end joining
WP1324: Non-homologous end joining
WP1570: Non-homologous end joining
WP1625: Base excision repair
WP1659: Glycine, serine and threonine metabolism
WP1672: Mismatch repair
WP1676: Non-homologous end-joining
WP1678: Nucleotide excision repair
WP1996: Linoleate Biosynthesis

Related Genes :
[SARS QccE-14020] Serine--tRNA ligase, cytoplasmic (EC 6.1.1.11) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase)
[serS OR1_03230] Serine--tRNA ligase (EC 6.1.1.11) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase)
[serS OR16_34668] Serine--tRNA ligase (EC 6.1.1.11) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase)
[serS OR37_03554] Serine--tRNA ligase (EC 6.1.1.11) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase)
[serS OR214_02672] Serine--tRNA ligase (EC 6.1.1.11) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase)
[serS ATE51_03436 CC14983A_1504 NCTC11366_01668] Serine--tRNA ligase (EC 6.1.1.11) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase)
[serS HPHPH6_1663] Serine--tRNA ligase (EC 6.1.1.11) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase)
[serS HPHPA6_1621] Serine--tRNA ligase (EC 6.1.1.11) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase)
[serS HPHPP11_1453] Serine--tRNA ligase (EC 6.1.1.11) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase)
[serS HPHPH11_0081] Serine--tRNA ligase (EC 6.1.1.11) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase)
[serS OR221_0117] Serine--tRNA ligase (EC 6.1.1.11) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase)
[serS Loa_02333] Serine--tRNA ligase (EC 6.1.1.11) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase)
[serS MCAL106_1042 MCAL106E_1042 MCAL106L_1042] Serine--tRNA ligase (EC 6.1.1.11) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase)
[serS HPHPP1_0039] Serine--tRNA ligase (EC 6.1.1.11) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase)
[Eprs Qprs] Bifunctional glutamate/proline--tRNA ligase (Bifunctional aminoacyl-tRNA synthetase) [Includes: Glutamate--tRNA ligase (EC 6.1.1.17) (Glutamyl-tRNA synthetase) (GluRS); Proline--tRNA ligase (EC 6.1.1.15) (Prolyl-tRNA synthetase) (ProRS)]
[serS MCAL160E_1042 MCAL160L_1042] Serine--tRNA ligase (EC 6.1.1.11) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase)
[serS MSMEG_6413 MSMEI_6245] Serine--tRNA ligase (EC 6.1.1.11) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase)
[serS OUG_0047] Serine--tRNA ligase (EC 6.1.1.11) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase)
[serS OUS_0164] Serine--tRNA ligase (EC 6.1.1.11) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase)
[serS OUM_1601] Serine--tRNA ligase (EC 6.1.1.11) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase)
[serS OUK_0115] Serine--tRNA ligase (EC 6.1.1.11) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase)
[serS OUO_1462] Serine--tRNA ligase (EC 6.1.1.11) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase)
[serS OUE_1624] Serine--tRNA ligase (EC 6.1.1.11) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase)
[serS HPHPP16_1399] Serine--tRNA ligase (EC 6.1.1.11) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase)
[serS HPHPA8_1507] Serine--tRNA ligase (EC 6.1.1.11) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase)
[serS HPHPA26_1457] Serine--tRNA ligase (EC 6.1.1.11) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase)
[serS HPHPP3_1606] Serine--tRNA ligase (EC 6.1.1.11) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase)
[serS HPNQ4099_1605] Serine--tRNA ligase (EC 6.1.1.11) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase)
[serS HPCPY1124_1577] Serine--tRNA ligase (EC 6.1.1.11) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase)
[serS HPNQ4200_1443] Serine--tRNA ligase (EC 6.1.1.11) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase)

Bibliography :
[28808125] Insights into substrate promiscuity of human seryl-tRNA synthetase.
[26433229] SerRS-tRNASec complex structures reveal mechanism of the first step in selenocysteine biosynthesis.
[23649835] Tertiary structure of bacterial selenocysteine tRNA.
[9637248] Minimal tRNA(Ser) and tRNA(Sec) substrates for human seryl-tRNA synthetase: contribution of tRNA domains to serylation and tertiary structure.
[8065908] Seryl-tRNA synthetase from Escherichia coli: implication of its N-terminal domain in aminoacylation activity and specificity.
[8284203] The long extra arms of human tRNA((Ser)Sec) and tRNA(Ser) function as major identify elements for serylation in an orientation-dependent, but not sequence-specific manner.
?>