SYSC_CANAL
ID SYSC_CANAL Reviewed; 462 AA.
AC Q9HGT6; A0A1D8PJH7; Q5AEY4;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Serine--tRNA ligase, cytoplasmic;
DE EC=6.1.1.11;
DE AltName: Full=Seryl-tRNA synthetase;
DE Short=SerRS;
DE AltName: Full=Seryl-tRNA(Ser/Sec) synthetase;
GN Name=SES1; OrderedLocusNames=CAALFM_C302780WA; ORFNames=CaO19.7901;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 32032 / CBS 5736 / DSM 3454 / NBRC 1856;
RX PubMed=11223940;
RX DOI=10.1002/1097-0061(20010315)18:4<313::aid-yea673>3.0.co;2-7;
RA O'Sullivan J.M., Mihr M.J., Santos M.A.S., Tuite M.F.;
RT "Seryl-tRNA synthetase is not responsible for the evolution of CUG codon
RT reassignment in Candida albicans.";
RL Yeast 18:313-322(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
CC -!- FUNCTION: Catalyzes the attachment of serine to tRNA(Ser). Is also
CC probably able to aminoacylate tRNA(Sec) with serine, to form the
CC misacylated tRNA L-seryl-tRNA(Sec), which will be further converted
CC into selenocysteinyl-tRNA(Sec). {ECO:0000269|PubMed:11223940}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-serine + tRNA(Ser) = AMP + diphosphate + H(+) + L-
CC 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 -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-serine + tRNA(Sec) = AMP + diphosphate + H(+) + L-
CC 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 -!- PATHWAY: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec)
CC biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1.
CC -!- SUBUNIT: Homodimer. The tRNA molecule binds across the dimer (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- DOMAIN: Consists of two distinct domains, a catalytic core and a N-
CC terminal extension that is involved in tRNA binding. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Type-1 seryl-tRNA synthetase subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AOW28309.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF290915; AAG02209.1; -; Genomic_DNA.
DR EMBL; CP017625; AOW28309.1; ALT_FRAME; Genomic_DNA.
DR RefSeq; XP_719967.2; XM_714874.2.
DR PDB; 3QNE; X-ray; 2.00 A; A=1-462.
DR PDB; 3QO5; X-ray; 2.30 A; A=1-462.
DR PDB; 3QO7; X-ray; 2.55 A; A=1-462.
DR PDB; 3QO8; X-ray; 2.00 A; A=1-462.
DR PDBsum; 3QNE; -.
DR PDBsum; 3QO5; -.
DR PDBsum; 3QO7; -.
DR PDBsum; 3QO8; -.
DR AlphaFoldDB; Q9HGT6; -.
DR SMR; Q9HGT6; -.
DR BioGRID; 1221320; 1.
DR DIP; DIP-59702N; -.
DR STRING; 237561.Q9HGT6; -.
DR COMPLUYEAST-2DPAGE; Q9HGT6; -.
DR PRIDE; Q9HGT6; -.
DR GeneID; 3638415; -.
DR KEGG; cal:CAALFM_C302780WA; -.
DR CGD; CAL0000183348; SES1.
DR eggNOG; KOG2509; Eukaryota.
DR HOGENOM; CLU_023797_0_1_1; -.
DR InParanoid; Q9HGT6; -.
DR OrthoDB; 726296at2759; -.
DR BRENDA; 6.1.1.11; 1096.
DR UniPathway; UPA00906; UER00895.
DR EvolutionaryTrace; Q9HGT6; -.
DR Proteomes; UP000000559; Chromosome 3.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004828; F:serine-tRNA ligase activity; IBA:GO_Central.
DR GO; GO:0000049; F:tRNA binding; IBA:GO_Central.
DR GO; GO:0097056; P:selenocysteinyl-tRNA(Sec) biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006434; P:seryl-tRNA aminoacylation; ISS:UniProtKB.
DR CDD; cd00770; SerRS_core; 1.
DR Gene3D; 1.10.287.40; -; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR InterPro; IPR002314; aa-tRNA-synt_IIb.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
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 SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00414; serS; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..462
FT /note="Serine--tRNA ligase, cytoplasmic"
FT /id="PRO_0000122197"
FT BINDING 246..248
FT /ligand="L-serine"
FT /ligand_id="ChEBI:CHEBI:33384"
FT /evidence="ECO:0000250"
FT BINDING 279..281
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 295
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 302
FT /ligand="L-serine"
FT /ligand_id="ChEBI:CHEBI:33384"
FT /evidence="ECO:0000250"
FT BINDING 366..369
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 404
FT /ligand="L-serine"
FT /ligand_id="ChEBI:CHEBI:33384"
FT /evidence="ECO:0000250"
FT HELIX 4..7
FT /evidence="ECO:0007829|PDB:3QNE"
FT HELIX 9..11
FT /evidence="ECO:0007829|PDB:3QNE"
FT HELIX 15..25
FT /evidence="ECO:0007829|PDB:3QNE"
FT HELIX 30..68
FT /evidence="ECO:0007829|PDB:3QNE"
FT HELIX 74..105
FT /evidence="ECO:0007829|PDB:3QNE"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:3QNE"
FT STRAND 126..131
FT /evidence="ECO:0007829|PDB:3QNE"
FT STRAND 138..142
FT /evidence="ECO:0007829|PDB:3QNE"
FT TURN 144..146
FT /evidence="ECO:0007829|PDB:3QNE"
FT HELIX 154..160
FT /evidence="ECO:0007829|PDB:3QNE"
FT HELIX 166..173
FT /evidence="ECO:0007829|PDB:3QNE"
FT HELIX 183..200
FT /evidence="ECO:0007829|PDB:3QNE"
FT TURN 201..203
FT /evidence="ECO:0007829|PDB:3QNE"
FT STRAND 205..208
FT /evidence="ECO:0007829|PDB:3QNE"
FT STRAND 211..214
FT /evidence="ECO:0007829|PDB:3QNE"
FT HELIX 215..221
FT /evidence="ECO:0007829|PDB:3QNE"
FT HELIX 224..227
FT /evidence="ECO:0007829|PDB:3QNE"
FT TURN 228..230
FT /evidence="ECO:0007829|PDB:3QNE"
FT STRAND 233..236
FT /evidence="ECO:0007829|PDB:3QNE"
FT STRAND 239..243
FT /evidence="ECO:0007829|PDB:3QNE"
FT HELIX 248..254
FT /evidence="ECO:0007829|PDB:3QNE"
FT TURN 255..257
FT /evidence="ECO:0007829|PDB:3QNE"
FT STRAND 259..262
FT /evidence="ECO:0007829|PDB:3QNE"
FT HELIX 263..266
FT /evidence="ECO:0007829|PDB:3QNE"
FT STRAND 269..278
FT /evidence="ECO:0007829|PDB:3QNE"
FT STRAND 291..294
FT /evidence="ECO:0007829|PDB:3QNE"
FT STRAND 296..307
FT /evidence="ECO:0007829|PDB:3QNE"
FT HELIX 309..311
FT /evidence="ECO:0007829|PDB:3QNE"
FT HELIX 312..329
FT /evidence="ECO:0007829|PDB:3QNE"
FT STRAND 334..338
FT /evidence="ECO:0007829|PDB:3QNE"
FT HELIX 341..343
FT /evidence="ECO:0007829|PDB:3QNE"
FT STRAND 349..358
FT /evidence="ECO:0007829|PDB:3QNE"
FT TURN 359..362
FT /evidence="ECO:0007829|PDB:3QNE"
FT STRAND 363..372
FT /evidence="ECO:0007829|PDB:3QNE"
FT HELIX 376..380
FT /evidence="ECO:0007829|PDB:3QNE"
FT STRAND 399..407
FT /evidence="ECO:0007829|PDB:3QNE"
FT HELIX 408..418
FT /evidence="ECO:0007829|PDB:3QNE"
FT STRAND 419..421
FT /evidence="ECO:0007829|PDB:3QNE"
FT STRAND 424..426
FT /evidence="ECO:0007829|PDB:3QNE"
FT HELIX 429..434
FT /evidence="ECO:0007829|PDB:3QNE"
FT STRAND 440..443
FT /evidence="ECO:0007829|PDB:3QNE"
SQ SEQUENCE 462 AA; 52991 MW; 9111C72CF7B37CDF CRC64;
MLDINAFLVE KGGDPEIIKA SQKKRGDSVE LVDEIIAEYK EWVKLRFDLD EHNKKLNSVQ
KEIGKRFKAK EDAKDLIAEK EKLSNEKKEI IEKEAEADKN LRSKINQVGN IVHESVVDSQ
DEENNELVRT WTPENYKKPE QIAAATGAPA KLSHHEVLLR LDGYDPERGV RIVGHRGYFL
RNYGVFLNQA LINYGLSFLS SKGYVPLQAP VMMNKEVMAK TAQLSQFDEE LYKVIDGEDE
KYLIATSEQP ISAYHAGEWF ESPAEQLPVR YAGYSSCFRR EAGSHGKDAW GIFRVHAFEK
IEQFVLTEPE KSWEEFDRMI GCSEEFYQSL GLPYRVVGIV SGELNNAAAK KYDLEAWFPF
QQEYKELVSC SNCTDYQSRN LEIRCGIKQQ NQQEKKYVHC LNSTLSATER TICCILENYQ
KEDGLVIPEV LRKYIPGEPE FIPYIKELPK NTTSVKKAKG KN
