(data stored in ACNUC7421 zone)

SWISSPROT: C7QJ56_CATAD

ID   C7QJ56_CATAD            Unreviewed;       425 AA.
AC   C7QJ56;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   07-JUN-2017, entry version 59.
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=Caci_0245 {ECO:0000313|EMBL:ACU69198.1};
OS   Catenulispora acidiphila (strain DSM 44928 / NRRL B-24433 / NBRC
OS   102108 / JCM 14897).
OC   Bacteria; Actinobacteria; Catenulisporales; Catenulisporaceae;
OC   Catenulispora.
OX   NCBI_TaxID=479433 {ECO:0000313|EMBL:ACU69198.1, ECO:0000313|Proteomes:UP000000851};
RN   [1] {ECO:0000313|EMBL:ACU69198.1, ECO:0000313|Proteomes:UP000000851}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44928 / NRRL B-24433 / NBRC 102108 / JCM 14897
RC   {ECO:0000313|Proteomes:UP000000851};
RX   PubMed=21304647;
RA   Copeland A., Lapidus A., Glavina Del Rio T., Nolan M., Lucas S.,
RA   Chen F., Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chain P., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Chertkov O., Brettin T., Detter J.C., Han C., Ali Z.,
RA   Tindall B.J., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Catenulispora acidiphila type strain (ID
RT   139908).";
RL   Stand. Genomic Sci. 1:119-125(2009).
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: ATP + L-serine + tRNA(Sec) = AMP + diphosphate
CC       + L-seryl-tRNA(Sec). {ECO:0000256|HAMAP-Rule:MF_00176}.
CC   -!- CATALYTIC ACTIVITY: ATP + L-serine + tRNA(Ser) = AMP + diphosphate
CC       + L-seryl-tRNA(Ser). {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; CP001700; ACU69198.1; -; Genomic_DNA.
DR   RefSeq; WP_012784493.1; NC_013131.1.
DR   STRING; 479433.Caci_0245; -.
DR   EnsemblBacteria; ACU69198; ACU69198; Caci_0245.
DR   KEGG; cai:Caci_0245; -.
DR   eggNOG; ENOG4105CGR; Bacteria.
DR   eggNOG; COG0172; LUCA.
DR   HOGENOM; HOG000035937; -.
DR   KO; K01875; -.
DR   OMA; SPCFRRE; -.
DR   OrthoDB; POG091H01YY; -.
DR   UniPathway; UPA00906; UER00895.
DR   Proteomes; UP000000851; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004828; F:serine-tRNA ligase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0016260; P:selenocysteine biosynthetic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0097056; P:selenocysteinyl-tRNA(Sec) biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006434; P:seryl-tRNA aminoacylation; IEA:UniProtKB-HAMAP.
DR   CDD; cd00770; SerRS_core; 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; 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; C7QJ56.
DR   SWISS-2DPAGE; C7QJ56.
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00176,
KW   ECO:0000313|EMBL:ACU69198.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00176};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000851};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00176};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00176, ECO:0000313|EMBL:ACU69198.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00176};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00176};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000851}.
FT   DOMAIN      173    407       AA_TRNA_LIGASE_II. {ECO:0000259|PROSITE:
FT                                PS50862}.
FT   NP_BIND     261    263       ATP. {ECO:0000256|HAMAP-Rule:MF_00176}.
FT   NP_BIND     348    351       ATP. {ECO:0000256|HAMAP-Rule:MF_00176}.
FT   REGION      230    232       Serine binding. {ECO:0000256|HAMAP-Rule:
FT                                MF_00176}.
FT   BINDING     277    277       ATP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00176}.
FT   BINDING     284    284       Serine. {ECO:0000256|HAMAP-Rule:
FT                                MF_00176}.
FT   BINDING     382    382       Serine. {ECO:0000256|HAMAP-Rule:
FT                                MF_00176}.
SQ   SEQUENCE   425 AA;  46467 MW;  7B08D55AD1F28371 CRC64;
     MIDLRLLRTD PERVRASQRA RGEDPALVDA LLSADEARRA AVSRFDTLRN EQKVLGKQIP
     KAAGEEKAAL LEQAKKLADG VKAAEADQHE ADDVLKQLQL SLSNVVIDGV PEGGEDDFVL
     RETVGTPRDF AADGFEPRDH VELGKLLGAI DLERGVKVGG ARQYYLTGVG ALLEIALLNM
     AMAQATTYGF TPMITPSLVK PEAMAGTGFL GQAAENVYHL TEDDMYLVGT SEVPLAAYHM
     DEILDAAKLP LRYAGYSSCY RREAGSYGKD TRGIIRVHQF EKVEMFSYVL PEEAEAEHLR
     LLGWEKEFLT ALEIPFRVID VAAGDLGSSA ARKYDCEAWI PTQGKYREVT STSNCTEFQA
     RRLQIRMRGA DGVKPLATLN GTLCAMTRMI VAILENHQNA DGSVTVPAAL RPYLGGREKL
     EPVAG
//

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