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Database: UniProt
Entry: D8SBS7_SELML
LinkDB: D8SBS7_SELML
Original site: D8SBS7_SELML 
ID   D8SBS7_SELML            Unreviewed;       555 AA.
AC   D8SBS7;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   RecName: Full=Aminoacyl-transfer RNA synthetases class-II family profile domain-containing protein {ECO:0000259|PROSITE:PS50862};
GN   ORFNames=SELMODRAFT_154078 {ECO:0000313|EMBL:EFJ17972.1};
OS   Selaginella moellendorffii (Spikemoss).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella.
OX   NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514};
RN   [1] {ECO:0000313|EMBL:EFJ17972.1, ECO:0000313|Proteomes:UP000001514}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21551031; DOI=10.1126/science.1203810;
RA   Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M.,
RA   dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., Ashton N.W.,
RA   Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., Bonawitz N.D.,
RA   Chapple C., Cheng C., Correa L.G., Dacre M., DeBarry J., Dreyer I.,
RA   Elias M., Engstrom E.M., Estelle M., Feng L., Finet C., Floyd S.K.,
RA   Frommer W.B., Fujita T., Gramzow L., Gutensohn M., Harholt J., Hattori M.,
RA   Heyl A., Hirai T., Hiwatashi Y., Ishikawa M., Iwata M., Karol K.G.,
RA   Koehler B., Kolukisaoglu U., Kubo M., Kurata T., Lalonde S., Li K., Li Y.,
RA   Litt A., Lyons E., Manning G., Maruyama T., Michael T.P., Mikami K.,
RA   Miyazaki S., Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R.,
RA   Obara M., Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B.,
RA   Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y.,
RA   Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N.,
RA   Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N.,
RA   Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., Wakazuki S.,
RA   Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., Zimmer A.D., Zhu Q.,
RA   Mitros T., Hellsten U., Loque D., Otillar R., Salamov A., Schmutz J.,
RA   Shapiro H., Lindquist E., Lucas S., Rokhsar D., Grigoriev I.V.;
RT   "The Selaginella genome identifies genetic changes associated with the
RT   evolution of vascular plants.";
RL   Science 332:960-963(2011).
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       Type 1 subfamily. {ECO:0000256|ARBA:ARBA00006303}.
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DR   EMBL; GL377611; EFJ17972.1; -; Genomic_DNA.
DR   RefSeq; XP_002980787.1; XM_002980741.1.
DR   AlphaFoldDB; D8SBS7; -.
DR   STRING; 88036.D8SBS7; -.
DR   EnsemblPlants; EFJ17972; EFJ17972; SELMODRAFT_154078.
DR   Gramene; EFJ17972; EFJ17972; SELMODRAFT_154078.
DR   KEGG; smo:SELMODRAFT_154078; -.
DR   eggNOG; KOG2411; Eukaryota.
DR   HOGENOM; CLU_014330_3_2_1; -.
DR   InParanoid; D8SBS7; -.
DR   OMA; LMAILCD; -.
DR   Proteomes; UP000001514; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0004815; F:aspartate-tRNA ligase activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006422; P:aspartyl-tRNA aminoacylation; IBA:GO_Central.
DR   CDD; cd00777; AspRS_core; 1.
DR   Gene3D; 3.30.1360.30; GAD-like domain; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   HAMAP; MF_00044; Asp_tRNA_synth_type1; 1.
DR   InterPro; IPR004364; Aa-tRNA-synt_II.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR004524; Asp-tRNA-ligase_1.
DR   InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR   InterPro; IPR047090; AspRS_core.
DR   InterPro; IPR004115; GAD-like_sf.
DR   InterPro; IPR029351; GAD_dom.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   NCBIfam; TIGR00459; aspS_bact; 1.
DR   PANTHER; PTHR22594:SF5; ASPARTATE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR22594; ASPARTYL/LYSYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF02938; GAD; 1.
DR   Pfam; PF00152; tRNA-synt_2; 1.
DR   PRINTS; PR01042; TRNASYNTHASP.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   SUPFAM; SSF55261; GAD domain-like; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001514}.
FT   DOMAIN          104..522
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
SQ   SEQUENCE   555 AA;  62022 MW;  A1D36D281A65053A CRC64;
     MVQASSCIVI FPFLIRKLHA RLRIEYVVAV EGTVRSRPQG AANTNLKTGS VEIIADKVEV
     LNPVSLNLPF LVTPLDQSKN VISEEVRLRY RHLDLRRPQL NANLRLRHRI VKLMRRYLED
     VHGFVEVETP ILSRSTPEGA RDYLVPSRVQ PATFYALPQS PQLFKQMLMV SGFDRYFQFA
     RCFRDEDLRA DRQPEFTQLD MELAFTPLED MLELNEDLIR LVFREIKGVE LPDPFPRLTY
     AEAMSKYGSD KPDTRFGMQL VELSDVFEKS SFAPFATAIS EGGVVKAITV CGGGKSITAT
     RLKKGDIYQE AVRCGAKGLP FLKVAEGGEV EGSTALKSSL SCPETRDNFL AKCDAKPGDV
     IIFANGPTSL VNATLGRLRT LIAETSDNLI DKSRNDILWI TDFPMFEWND TEKRLEALHH
     PFTAPRPEDM KDLSSARALA YDMVYNGVEI GGGSLRIHRR DVQQKVLEAS GLSAQEAEDK
     FGYLLEALEL GAPPHGGIAY GVDRLVMLLA GEKSIRDVIA FPKTTAAHCS LTRTPSTVDP
     RQLQELRLQC TIAHP
//
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