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Database: UniProt/SWISS-PROT
Entry: SYA_SULIY
LinkDB: SYA_SULIY
Original site: SYA_SULIY 
ID   SYA_SULIY               Reviewed;         900 AA.
AC   C3N7E3;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   19-FEB-2014, entry version 31.
DE   RecName: Full=Alanine--tRNA ligase;
DE            EC=6.1.1.7;
DE   AltName: Full=Alanyl-tRNA synthetase;
DE            Short=AlaRS;
GN   Name=alaS; OrderedLocusNames=YG5714_1881;
OS   Sulfolobus islandicus (strain Y.G.57.14 / Yellowstone #1).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=439386;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y.G.57.14 / Yellowstone #1;
RX   PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA   Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT   "Biogeography of the Sulfolobus islandicus pan-genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
CC   -!- FUNCTION: Catalyzes the attachment of alanine to tRNA(Ala) in a
CC       two-step reaction: alanine is first activated by ATP to form Ala-
CC       AMP and then transferred to the acceptor end of tRNA(Ala). Also
CC       edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its
CC       editing domain (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + L-alanine + tRNA(Ala) = AMP +
CC       diphosphate + L-alanyl-tRNA(Ala).
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- DOMAIN: Consists of three domains; the N-terminal catalytic
CC       domain, the editing domain and the C-terminal C-Ala domain. The
CC       editing domain removes incorrectly charged amino acids, while the
CC       C-Ala domain, along with tRNA(Ala), serves as a bridge to
CC       cooperatively bring together the editing and aminoacylation
CC       centers thus stimulating deacylation of misacylated tRNAs (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family.
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DR   EMBL; CP001403; ACP46137.1; -; Genomic_DNA.
DR   RefSeq; YP_002838059.1; NC_012622.1.
DR   ProteinModelPortal; C3N7E3; -.
DR   STRING; 439386.YG5714_1881; -.
DR   EnsemblBacteria; ACP46137; ACP46137; YG5714_1881.
DR   GeneID; 7807284; -.
DR   KEGG; siy:YG5714_1881; -.
DR   eggNOG; COG0013; -.
DR   HOGENOM; HOG000015496; -.
DR   KO; K01872; -.
DR   OMA; SFEFLTS; -.
DR   ProtClustDB; PRK13902; -.
DR   BioCyc; SISL439386:GHF0-1951-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004813; F:alanine-tRNA ligase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006419; P:alanyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP.
DR   HAMAP; MF_00036_A; Ala_tRNA_synth_A; 1.
DR   InterPro; IPR002318; Ala-tRNA-lgiase_IIc.
DR   InterPro; IPR018162; Ala-tRNA-ligase_IIc_anticod-bd.
DR   InterPro; IPR018165; Ala-tRNA-synth_IIc_core.
DR   InterPro; IPR018164; Ala-tRNA-synth_IIc_N.
DR   InterPro; IPR022429; Ala-tRNA_lgiase_arc.
DR   InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
DR   InterPro; IPR009000; Transl_B-barrel.
DR   InterPro; IPR012947; tRNA_SAD.
DR   PANTHER; PTHR11777:SF6; PTHR11777:SF6; 1.
DR   Pfam; PF01411; tRNA-synt_2c; 1.
DR   Pfam; PF07973; tRNA_SAD; 1.
DR   PRINTS; PR00980; TRNASYNTHALA.
DR   SMART; SM00863; tRNA_SAD; 1.
DR   SUPFAM; SSF101353; SSF101353; 1.
DR   SUPFAM; SSF50447; SSF50447; 1.
DR   SUPFAM; SSF55186; SSF55186; 1.
DR   TIGRFAMs; TIGR03683; A-tRNA_syn_arch; 1.
DR   TIGRFAMs; TIGR00344; alaS; 1.
DR   PROSITE; PS50860; AA_TRNA_LIGASE_II_ALA; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Metal-binding; Nucleotide-binding; Protein biosynthesis;
KW   RNA-binding; tRNA-binding; Zinc.
FT   CHAIN         1    900       Alanine--tRNA ligase.
FT                                /FTId=PRO_1000202051.
FT   METAL       604    604       Zinc (By similarity).
FT   METAL       608    608       Zinc (By similarity).
FT   METAL       708    708       Zinc (By similarity).
FT   METAL       712    712       Zinc (By similarity).
SQ   SEQUENCE   900 AA;  103090 MW;  AE89FEAD497CB69C CRC64;
     MKASEEEYRL NFFIKNDFKR KICKSCKTPF WTRDEKKEYC SDIPCTDYYF FDINIKSQPL
     TVKEAREKFL SFFEKRGHTR ISPKPVLARW REDLYLTIAS IVDFQPHVTS GLVPPPANPL
     VVSQPSIRLE DIDNVGITFG RHLTTFEMAA HHAFNYPDHY VYWKEETTAY ATEFFTKELG
     IPEEELNFKE SWWEGGGNAG PCLEVTVGGL ELATLVFMQY KITDNGNYTP LKLKIVDTGY
     GVERIAWITQ KTPSAFHAIY GNLVYKFFNK IGVAYIDETL LKVASRFAGK IDPDNPDTIK
     IHRQMVSKEL GIDIKAVEEE LDRAAKVFQI LDHTKTIMLM LADGLVPSNS GEGYLGRLVI
     RRALKVLRLL KSDVRLYELV KEQIDFWKED FPQVLKNKDY ILDAVELEQQ RFEKILEKVP
     SIASTLARKS EITTEDLIQV YDSNGIPPDL LEEELKKKSV KFELPRNFYA LVAKRHQTST
     IKSAYDKVKL PKDMLEYITA LQPTEKLYYK DQYMRSFEGK VLGVYKNYLI LDKTTFYPEG
     GGQLGDTGLI IDEKSSKRYE VIDTQKVNDV IVHILKEEPS TIKVGDNVRG EINWERRYRL
     MRHHTVTHVI LAAAKKVLGE HVWQAGAEKT PEKGRLDITH HKTLTEEEVK LIENYANSVI
     SDRRQVKPLE MNRMEAEMKY GVSIYEGGVP NSATIRLLEI KDWDIESCGG THVSNTSEIG
     AVKIINVERI QDGVIRLEYV AGPALVDYIR ETQAKIVEAS KIIGTSPDQL TSRLRRILNE
     IEEKNNLIIQ YRRIIETELL NNLKPYEINS NKIYIIEGLG DEEENKEILR KLTSTDNTIA
     ISISDNRLQI ATSKNMRVDK IVEELLKGGG KGGGKGTFAN VILNSKKSKE EIIEIVRKSL
//
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