(data stored in ACNUC7421 zone)

SWISSPROT: C6WDU4_ACTMD

ID   C6WDU4_ACTMD            Unreviewed;       416 AA.
AC   C6WDU4;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   07-JUN-2017, entry version 60.
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=Amir_0118 {ECO:0000313|EMBL:ACU34089.1};
OS   Actinosynnema mirum (strain ATCC 29888 / DSM 43827 / NBRC 14064 / IMRU
OS   3971).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Actinosynnema.
OX   NCBI_TaxID=446462 {ECO:0000313|EMBL:ACU34089.1, ECO:0000313|Proteomes:UP000002213};
RN   [1] {ECO:0000313|EMBL:ACU34089.1, ECO:0000313|Proteomes:UP000002213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29888 / DSM 43827 / NBRC 14064 / IMRU 3971
RC   {ECO:0000313|Proteomes:UP000002213};
RX   PubMed=21304636; DOI=10.4056/sigs.21137;
RA   Land M., Lapidus A., Mayilraj S., Chen F., Copeland A., Del Rio T.G.,
RA   Nolan M., Lucas S., Tice H., Cheng J.F., Chertkov O., Bruce D.,
RA   Goodwin L., Pitluck S., Rohde M., Goker M., Pati A., Ivanova N.,
RA   Mavromatis K., Chen A., Palaniappan K., Hauser L., Chang Y.J.,
RA   Jeffries C.C., Brettin T., Detter J.C., Han C., Chain P.,
RA   Tindall B.J., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Actinosynnema mirum type strain (101).";
RL   Stand. Genomic Sci. 1:46-53(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; CP001630; ACU34089.1; -; Genomic_DNA.
DR   RefSeq; WP_012782752.1; NC_013093.1.
DR   STRING; 446462.Amir_0118; -.
DR   EnsemblBacteria; ACU34089; ACU34089; Amir_0118.
DR   KEGG; ami:Amir_0118; -.
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; UP000002213; 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; C6WDU4.
DR   SWISS-2DPAGE; C6WDU4.
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00176,
KW   ECO:0000313|EMBL:ACU34089.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00176};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002213};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00176};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00176, ECO:0000313|EMBL:ACU34089.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00176};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00176};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002213}.
FT   DOMAIN      136    401       AA_TRNA_LIGASE_II. {ECO:0000259|PROSITE:
FT                                PS50862}.
FT   NP_BIND     255    257       ATP. {ECO:0000256|HAMAP-Rule:MF_00176}.
FT   NP_BIND     342    345       ATP. {ECO:0000256|HAMAP-Rule:MF_00176}.
FT   REGION      227    229       Serine binding. {ECO:0000256|HAMAP-Rule:
FT                                MF_00176}.
FT   COILED       74    101       {ECO:0000256|SAM:Coils}.
FT   BINDING     271    271       ATP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00176}.
FT   BINDING     278    278       Serine. {ECO:0000256|HAMAP-Rule:
FT                                MF_00176}.
FT   BINDING     377    377       Serine. {ECO:0000256|HAMAP-Rule:
FT                                MF_00176}.
SQ   SEQUENCE   416 AA;  45724 MW;  18EE6A7C0937410A CRC64;
     MIDLKALREN PEAVRASQRA RGEDESLVDA LLSADERRRS AVSRADTLRG EQKAFGKQVG
     KARGEEREAL LVKGKELAAE VKAAEADQAA AEAELTELHR SVPNLVHPDA PEGGEDDYVV
     VKHVGEPREF DFEPLDHLDL GTRLGAIDME RGAKVSGSRF YFLTGIGAQL ELALLNMAVA
     QATAAGFQLM ITPTLVRPEV MAGTGFLGAH SSEIYRLEAD DLYLVGTSEV PLAGYHADEI
     IDGPRRYAGW SSCYRREAGS YGKDTRGIIR VHQFNKVEMF SYVPPEEAEA EHARLLAWEE
     EMLAKVEVPY RVIDTAAGDL GTSASRKFDC EAWVPSQQAY RELTSTSNCT TFQARRLNVR
     YRDENGKSQI TATLNGTLAT TRWIVAILEN HQQADGSVVV PQALRPFLGK DVLLPA
//

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