(data stored in SCRATCH zone)

SWISSPROT: D5UQ35_TSUPD

ID   D5UQ35_TSUPD            Unreviewed;       417 AA.
AC   D5UQ35;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   08-MAY-2019, entry version 56.
DE   RecName: Full=Serine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00176};
DE            EC=6.1.1.11 {ECO:0000256|HAMAP-Rule:MF_00176};
DE   AltName: Full=Seryl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00176};
DE            Short=SerRS {ECO:0000256|HAMAP-Rule:MF_00176};
DE   AltName: Full=Seryl-tRNA(Ser/Sec) synthetase {ECO:0000256|HAMAP-Rule:MF_00176};
GN   Name=serS {ECO:0000256|HAMAP-Rule:MF_00176};
GN   OrderedLocusNames=Tpau_0149 {ECO:0000313|EMBL:ADG76803.1};
OS   Tsukamurella paurometabola (strain ATCC 8368 / DSM 20162 / JCM 10117 /
OS   NBRC 16120 / NCTC 13040) (Corynebacterium paurometabolum).
OC   Bacteria; Actinobacteria; Corynebacteriales; Tsukamurellaceae;
OC   Tsukamurella.
OX   NCBI_TaxID=521096 {ECO:0000313|EMBL:ADG76803.1, ECO:0000313|Proteomes:UP000001213};
RN   [1] {ECO:0000313|Proteomes:UP000001213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8368 / DSM 20162 / JCM 10117 / NBRC 16120 / NCTC 13040
RC   {ECO:0000313|Proteomes:UP000001213};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K.,
RA   Ivanova N., Mikhailova N., Munk A.C., Brettin T., Detter J.C.,
RA   Tapia R., Han C., Larimer F., Land M., Hauser L., Markowitz V.,
RA   Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Jando M., Brambilla E.,
RA   Klenk H.-P., Eisen J.A.;
RT   "The complete chromosome of Tsukamurella paurometabola DSM 20162.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADG76803.1, ECO:0000313|Proteomes:UP000001213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8368 / DSM 20162 / JCM 10117 / NBRC 16120 / NCTC 13040
RC   {ECO:0000313|Proteomes:UP000001213};
RX   PubMed=21886861;
RA   Munk A.C., Lapidus A., Lucas S., Nolan M., Tice H., Cheng J.F.,
RA   Del Rio T.G., Goodwin L., Pitluck S., Liolios K., Huntemann M.,
RA   Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA   Palaniappan K., Tapia R., Han C., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Brettin T., Yasawong M., Brambilla E.M., Rohde M.,
RA   Sikorski J., Goker M., Detter J.C., Woyke T., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Tsukamurella paurometabola type strain
RT   (no. 33).";
RL   Stand. Genomic Sci. 4:342-351(2011).
CC   -!- FUNCTION: Catalyzes the attachment of serine to tRNA(Ser). Is also
CC       able to aminoacylate tRNA(Sec) with serine, to form the
CC       misacylated tRNA L-seryl-tRNA(Sec), which will be further
CC       converted into selenocysteinyl-tRNA(Sec). {ECO:0000256|HAMAP-
CC       Rule:MF_00176}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-serine + tRNA(Sec) = AMP + diphosphate + H(+) +
CC         L-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:0000256|HAMAP-Rule:MF_00176};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-serine + tRNA(Ser) = AMP + diphosphate + H(+) +
CC         L-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:0000256|HAMAP-Rule:MF_00176};
CC   -!- PATHWAY: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec)
CC       biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step
CC       1/1. {ECO:0000256|HAMAP-Rule:MF_00176}.
CC   -!- SUBUNIT: Homodimer. The tRNA molecule binds across the dimer.
CC       {ECO:0000256|HAMAP-Rule:MF_00176}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00176}.
CC   -!- DOMAIN: Consists of two distinct domains, a catalytic core and a
CC       N-terminal extension that is involved in tRNA binding.
CC       {ECO:0000256|HAMAP-Rule:MF_00176}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family. Type-1 seryl-tRNA synthetase subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00176}.
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DR   EMBL; CP001966; ADG76803.1; -; Genomic_DNA.
DR   RefSeq; WP_013124858.1; NC_014158.1.
DR   STRING; 521096.Tpau_0149; -.
DR   EnsemblBacteria; ADG76803; ADG76803; Tpau_0149.
DR   KEGG; tpr:Tpau_0149; -.
DR   eggNOG; ENOG4105CGR; Bacteria.
DR   eggNOG; COG0172; LUCA.
DR   HOGENOM; HOG000035937; -.
DR   KO; K01875; -.
DR   OMA; SPCFRRE; -.
DR   OrthoDB; 353391at2; -.
DR   BioCyc; TPAU521096:G1GKO-149-MONOMER; -.
DR   UniPathway; UPA00906; UER00895.
DR   Proteomes; UP000001213; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004828; F:serine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016260; P:selenocysteine biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0097056; P:selenocysteinyl-tRNA(Sec) biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006434; P:seryl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd00770; SerRS_core; 1.
DR   Gene3D; 1.10.287.40; -; 1.
DR   HAMAP; MF_00176; Ser_tRNA_synth_type1; 1.
DR   InterPro; IPR002314; aa-tRNA-synt_IIb.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
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; IPR033729; SerRS_core.
DR   InterPro; IPR010978; tRNA-bd_arm.
DR   PANTHER; PTHR11778; PTHR11778; 1.
DR   Pfam; PF02403; Seryl_tRNA_N; 1.
DR   Pfam; PF00587; tRNA-synt_2b; 1.
DR   PIRSF; PIRSF001529; Ser-tRNA-synth_IIa; 1.
DR   PRINTS; PR00981; TRNASYNTHSER.
DR   SUPFAM; SSF46589; SSF46589; 1.
DR   TIGRFAMs; TIGR00414; serS; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
DR   PRODOM; D5UQ35.
DR   SWISS-2DPAGE; D5UQ35.
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00176,
KW   ECO:0000313|EMBL:ADG76803.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00176};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001213};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00176};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00176, ECO:0000313|EMBL:ADG76803.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00176};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00176};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001213}.
FT   DOMAIN      135    403       AA_TRNA_LIGASE_II. {ECO:0000259|PROSITE:
FT                                PS50862}.
FT   NP_BIND     257    259       ATP. {ECO:0000256|HAMAP-Rule:MF_00176}.
FT   NP_BIND     344    347       ATP. {ECO:0000256|HAMAP-Rule:MF_00176}.
FT   REGION      226    228       Serine binding. {ECO:0000256|HAMAP-Rule:
FT                                MF_00176}.
FT   BINDING     273    273       ATP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00176}.
FT   BINDING     280    280       Serine. {ECO:0000256|HAMAP-Rule:
FT                                MF_00176}.
FT   BINDING     379    379       Serine. {ECO:0000256|HAMAP-Rule:
FT                                MF_00176}.
SQ   SEQUENCE   417 AA;  45672 MW;  F3D5037BF7130EDE CRC64;
     MIDVKLLREN PDLVRASQRA RGEDAALVDA LLEADAHRRA AVLAADNLRA EHKTSSKSIG
     KAAPEERPAL VAAAGELAAK VKEAEAEQAR ADEVFDETAR KIGNVIIEGV PAGGEDDFEV
     LEHVGTIPEI TDPKDHLELA EGLGLLDMER GAKVSGSRFY FMTGHGALFQ MALLQLAVQK
     AVAHGFTLMI PPVLVKPEIM GGTGFLGAHA DEIYRLEADD LYLVGTSEVP LAGYHMGEII
     DLNDGPIRYA AQSSCFRREA GSYGKDTRGI IRVHQFDKIE MFVYCKPEDA EAEHQRLLDF
     EKEMLAAVEV PYRVIDVAAG DLGSSAARKF DCEAWVPSQE RYRELTSTSN CTTFQARRLG
     VRYRDEDGRP QIAATLNGTL ATTRWLVAIW ENHQQPDGSV RVPAALQPFL GTDVLRP
//

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