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 01-MAY-2013, entry version 28.
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:GHF0-1949-MONOMER; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004813; F:alanine-tRNA ligase activity; IEA:HAMAP.
DR GO; GO:0005524; F:ATP binding; IEA: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: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; 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; Ala-tRNA-synth_IIc_anticod-bd; 1.
DR SUPFAM; SSF55186; Thr/Ala-tRNA-synth_IIc_edit; 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
//
