(data stored in ACNUC7421 zone)

SWISSPROT: SYA_PSEHT

ID   SYA_PSEHT               Reviewed;         868 AA.
AC   Q3ILF3;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   07-JUN-2017, entry version 84.
DE   RecName: Full=Alanine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00036};
DE            EC=6.1.1.7 {ECO:0000255|HAMAP-Rule:MF_00036};
DE   AltName: Full=Alanyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00036};
DE            Short=AlaRS {ECO:0000255|HAMAP-Rule:MF_00036};
GN   Name=alaS {ECO:0000255|HAMAP-Rule:MF_00036};
GN   OrderedLocusNames=PSHAa0532;
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125;
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N.,
RA   Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G.,
RA   Ho C., Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C.,
RA   Rouy Z., Sekowska A., Tutino M.L., Vallenet D., von Heijne G.,
RA   Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
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. {ECO:0000255|HAMAP-Rule:MF_00036}.
CC   -!- CATALYTIC ACTIVITY: ATP + L-alanine + tRNA(Ala) = AMP +
CC       diphosphate + L-alanyl-tRNA(Ala). {ECO:0000255|HAMAP-
CC       Rule:MF_00036}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00036};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00036};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00036}.
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.
CC       {ECO:0000255|HAMAP-Rule:MF_00036}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family. {ECO:0000255|HAMAP-Rule:MF_00036}.
DR   EMBL; CR954246; CAI85621.1; -; Genomic_DNA.
DR   RefSeq; WP_011327234.1; NC_007481.1.
DR   ProteinModelPortal; Q3ILF3; -.
DR   SMR; Q3ILF3; -.
DR   STRING; 326442.PSHAa0532; -.
DR   EnsemblBacteria; CAI85621; CAI85621; PSHAa0532.
DR   KEGG; pha:PSHAa0532; -.
DR   PATRIC; fig|326442.8.peg.501; -.
DR   eggNOG; ENOG4105CIM; Bacteria.
DR   eggNOG; COG0013; LUCA.
DR   HOGENOM; HOG000156964; -.
DR   KO; K01872; -.
DR   OMA; FEMMAHH; -.
DR   OrthoDB; POG091H01PM; -.
DR   Proteomes; UP000006843; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004813; F:alanine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:InterPro.
DR   HAMAP; MF_00036_B; Ala_tRNA_synth_B; 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; IPR023033; Ala_tRNA_ligase_euk/bac.
DR   InterPro; IPR003156; DHHA1_dom.
DR   InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
DR   InterPro; IPR009000; Transl_B-barrel.
DR   InterPro; IPR012947; tRNA_SAD.
DR   Pfam; PF02272; DHHA1; 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; TIGR00344; alaS; 1.
DR   PROSITE; PS50860; AA_TRNA_LIGASE_II_ALA; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q3ILF3.
DR   SWISS-2DPAGE; Q3ILF3.
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Metal-binding; Nucleotide-binding; Protein biosynthesis;
KW   Reference proteome; RNA-binding; tRNA-binding; Zinc.
FT   CHAIN         1    868       Alanine--tRNA ligase.
FT                                /FTId=PRO_0000347734.
FT   METAL       555    555       Zinc. {ECO:0000255|HAMAP-Rule:MF_00036}.
FT   METAL       559    559       Zinc. {ECO:0000255|HAMAP-Rule:MF_00036}.
FT   METAL       657    657       Zinc. {ECO:0000255|HAMAP-Rule:MF_00036}.
FT   METAL       661    661       Zinc. {ECO:0000255|HAMAP-Rule:MF_00036}.
SQ   SEQUENCE   868 AA;  94885 MW;  697EAB5B11CF1BF5 CRC64;
     MQHMTTAQIR QQFLDFFASK QHQVVPSSSL IPGNDATLLF NNAGMVQFKD VFLGAESRPY
     TRATSSQRCV RAGGKHNDLE NVGYTARHHT FFEMLGNFSF GDYFKQDAIK FAWQFLTEEV
     KLPKEKLLVT IYHDDEEAFN YWSNDIGLPA DRIIRIATAD NFWSMGDTGP CGPCSEIFYD
     HGEHIWGGPP GSPEEDGDRF IEIWNLVFMQ YNRQNDGTML PLPKQSVDTG MGLERIAAIL
     QGVHSNYEID LFKGLIAAAA SVTNAQDMDD KSLRVVADHI RSCAFLISDG VMPSNEGRGY
     VLRRIIRRAV RHGNKLGAQG AFFYKLVAAL IEQMGQAYPE LAKQQEIIEK VLRIEEEQFG
     KTLERGLAIL EESLSDLKGD VIPGDLVFKL YDTYGFPADL TADVARERQM TIDNKGFEEC
     MAVQRKTAQQ AGKFGADYND QLKSDKQTTY KGYTTTSHSA TVVEVFAGSE SVSLLEDGQK
     GIVILDRTPF YAESGGQVGD TGVISVAGGE FTVTNTTKLG NAFAHHGIVQ GRIGLNDKVE
     ATIDDARRER IKKNHTATHI LHETLRQLLG EHVGQKGSLV QAERLRFDFS HFEAVTKEEL
     REIERVVNDE IRCNFALSTE LMAIDDAKAK GAMALFGEKY DDEVRVVTIG DYSIELCGGT
     HVERAGDIGL FKIVSESGIA AGVRRIEAVT GADAIAYVSE QEQKLNDVAA VVKADSASVL
     EKVTALLDKS KQLEKQIAQL NDKLASAAGA SLLDSVVEIN GIKLLIANVK GTESKALRGM
     VDDLKNKIGS GVIALGVASD DKVSLIAGVT KDLTGRVKAG ELVNHMASQV GGKGGGRPDM
     AQAGGSEPEN LTAALDSVTA WFTEKTQA
//

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