ID A0A2B4RZ87_STYPI Unreviewed; 2036 AA.
AC A0A2B4RZ87;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Aspartate--tRNA(Asp/Asn) ligase {ECO:0000313|EMBL:PFX22466.1};
GN Name=aspS {ECO:0000313|EMBL:PFX22466.1};
GN ORFNames=AWC38_SpisGene13034 {ECO:0000313|EMBL:PFX22466.1};
OS Stylophora pistillata (Smooth cauliflower coral).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Scleractinia;
OC Astrocoeniina; Pocilloporidae; Stylophora.
OX NCBI_TaxID=50429 {ECO:0000313|EMBL:PFX22466.1, ECO:0000313|Proteomes:UP000225706};
RN [1] {ECO:0000313|Proteomes:UP000225706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Voolstra C.R., Li Y., Liew Y.J., Baumgarten S., Zoccola D., Flot J.-F.,
RA Tambutte S., Allemand D., Aranda M.;
RT "Comparative analysis of the genomes of Stylophora pistillata and Acropora
RT digitifera provides evidence for extensive differences between species of
RT corals.";
RL bioRxiv 0:0-0(2017).
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Type 1 subfamily. {ECO:0000256|ARBA:ARBA00006303}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PFX22466.1}.
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DR EMBL; LSMT01000239; PFX22466.1; -; Genomic_DNA.
DR STRING; 50429.A0A2B4RZ87; -.
DR Proteomes; UP000225706; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004812; F:aminoacyl-tRNA ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016884; F:carbon-nitrogen ligase activity, with glutamine as amido-N-donor; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006418; P:tRNA aminoacylation for protein translation; IEA:InterPro.
DR CDD; cd00267; ABC_ATPase; 1.
DR CDD; cd00616; AHBA_syn; 1.
DR CDD; cd04317; EcAspRS_like_N; 1.
DR Gene3D; 1.10.10.410; -; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 2.60.40.1120; Carboxypeptidase-like, regulatory domain; 1.
DR Gene3D; 3.30.1360.30; GAD-like domain; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.170.20; TonB-dependent receptor, beta-barrel domain; 1.
DR Gene3D; 2.170.130.10; TonB-dependent receptor, plug domain; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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; IPR041685; AAA_15.
DR InterPro; IPR006075; Asn/Gln-tRNA_Trfase_suB/E_cat.
DR InterPro; IPR018027; Asn/Gln_amidotransferase.
DR InterPro; IPR047089; Asp-tRNA-ligase_1_N.
DR InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR InterPro; IPR008969; CarboxyPept-like_regulatory.
DR InterPro; IPR000653; DegT/StrS_aminotransferase.
DR InterPro; IPR004115; GAD-like_sf.
DR InterPro; IPR023168; GatB_Yqey_C_2.
DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR012910; Plug_dom.
DR InterPro; IPR037066; Plug_dom_sf.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR036942; TonB_rcpt_b-brl_sf.
DR InterPro; IPR041635; Type_ISP_LLaBIII_C.
DR PANTHER; PTHR30244:SF45; LIPOPOLYSACCHARIDE BIOSYNTHESIS PROTEIN RFBH; 1.
DR PANTHER; PTHR30244; TRANSAMINASE; 1.
DR Pfam; PF13175; AAA_15; 1.
DR Pfam; PF13715; CarbopepD_reg_2; 1.
DR Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR Pfam; PF02934; GatB_N; 1.
DR Pfam; PF02637; GatB_Yqey; 1.
DR Pfam; PF07715; Plug; 1.
DR Pfam; PF00152; tRNA-synt_2; 1.
DR Pfam; PF01336; tRNA_anti-codon; 1.
DR Pfam; PF18135; Type_ISP_C; 1.
DR PRINTS; PR01042; TRNASYNTHASP.
DR SUPFAM; SSF49464; Carboxypeptidase regulatory domain-like; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR SUPFAM; SSF56935; Porins; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell outer membrane {ECO:0000256|ARBA:ARBA00023237};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:PFX22466.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000225706};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 1544..1838
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT COILED 1785..1822
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 2036 AA; 229174 MW; AD13F20C446DFDF0 CRC64;
MLPAGHSANG AYWFEGASEV FGTLLMSAQN QIVRGVVTDT NKQALAGVSV MVKGSSIGTA
TGVDGTYQIG AVKGATLVFK MMGFFTKEVV ITSEKISVRL KENAQSLQNI LVEGHLNQNL
KAVSSSRMPV KAVDMPTNTS YVGQFQMEEQ MILKPSEVFQ NVAGVYQFNQ GYGGSGETVG
IRGVSLRYQG NMFRNGLRMG ANQSGATPEM LAFEAVEIHK GASAINFGYT SIGGAINYVT
KKPTFKTGGA VIARMAQYGL FKNSFDLNVK VSDRVGLRFI GTVEDAGSFR ETLYSKRRFG
SLIGEIKTTD RSKLSFNVDY LYDKIPRDFG IPIFETNVQT GTKTVSGKTV PVYKQESKES
DVQRLWKGLD RTRFIGSPFN DRVTKQLNAN LRYDTNIFKE KGIFKDWKGV LLFGLSQSKN
TYIQTGSGFR NKYLLLADGD VQITRTLEKG RVDDEYSSFL ASLQGSSSTA NFDFINSENG
VWNSGYLMTY NATTKKMYLI ANGGLIEVEV ANLSAKKEIT KVSDAIKNDA NKENYLMLYN
DYIYYNNAKE NKIYRVKKDG TAKELFIEGD FNDLITYELA DKIFQDVAFS SKIPANIEEE
VNKERLNRAG DKILEPKVDI GEDIGTKTGL ENYRGVNAVK INKDKVFLSD RTILDIGFEW
FSDAEREQVN EVLETGVLMR YGFDGMRKDR WKAKELEAAL CKKFGVGYAQ LTSSGTTALS
TAMAVLGVGA GDEVIMPSFT FVASFEAIIA AGATPVVVDI DDSLTLCPKA VENAITSRTK
AVMPVHMCGA MADLDPLKKL CKKHGLYMIE DACQAIGGTY KGAYLGTIAD MGTFSFDFVK
TITCGEGGVV LTNDQKWATN ADAYTDHGHD HIGNDRGAEQ HPYMGYNFRI SELHAAVGLA
QLGRLDQIIV TQRSHKKILK DALATLPEIS FRRLPDPSGD NAGFLSFFLP DADTAQKTMD
AFADHKIDAC WNYFENNWHY IRRWEHLKRV QSFRPIIPDG KVECFREDGT IFTVDLEQVH
LEEDAAKLMH ETKQSLVDFN KAGVPLIEIV TTPCIRSIKD AATYAQYVHR IVQNLGISDA
NLEKGEFKSD VSVSLRKKGT QDLNPRTEIK NLNSFKFMIQ ALEEEVQKQL GYFLENGDFR
PDQTTVLWDE ALKKTQEMRK KEYEADYRFI TEPDLPFVRI AKAVKNTSIQ KEKLPFAVEK
ILIDGGVLPK DAKFFTSDPL RSDAFSRINE VLKQPAFVAK SLTNLLKVED YERIKNIDAI
IAVFNALQMQ KITSVVAGGA VQNLLENPEF DYEKFFKKNT VDASKITETI ENIIAANAQI
SEEIKNGNQG KAGVLVGKVM GVLGKGVSGG VVRKKILEML LEGGAKTTNT LSKTTEQKDA
PKTISENDVI EKVPMVVRDH YRTHLIKDIT EQNLGTVMEL SGWVSSVRDH GELVFIDLRE
ADGSVLQVRL SSECFPNLEA LVKLKPETVI AVKGTLVLRG EEDFNPSIKT GKWELQTQKL
EVLNLSKTLP FEIKRATKTN EQTRFQYKFL DHRNTDVRRA IVGRHKVIKL IRDFLDSENF
LEIETPILTA GTDEGAREFI VPSRKAPGSF YTLPQAPQQF KQMLMVGGFD RYFQIARCFR
DEDSRGDRQP EFTQLDLEMS YASMQDIIQL NTDIFNRIVK EIYGKKWILK PIQTITYKEA
MDKYGCDRPD IRFGLPMQDI TAIVQETEFQ DGLNIGYIET KKVGDKDLYG KKQNKEQFDS
PKYREKYRDF LKTDFPRVPY PNQNKEKFWN LVKLGAERGA IDIFNKELSI RRNEALDRLL
ELSNNENESD SVERRIARAL GENKRYTLPV RDALKYADDL YNYSQSDSEF SHIADKIEEN
ILKGKLFVSK EGKVFFKHNK LKSQKAPLDI AASAIKSVAK LVFFMRHTAK KGMALFIDEP
ELNLHPDNQV LIARVLVQIA NSGIKLFVST HSDYIVREFN NMIIADQVKD EKYYSRETYL
NKKDIAVTRL FYKQDKNRQV TSEKVLIEND GFTIESVDET IEDQEYINGE LLENLE
//
