(data stored in ACNUC7421 zone)

SWISSPROT: SYA_MARMM

ID   SYA_MARMM               Reviewed;         884 AA.
AC   Q0AQY6;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   08-MAY-2019, 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=Mmar10_1008;
OS   Maricaulis maris (strain MCS10).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Hyphomonadaceae; Maricaulis.
OX   NCBI_TaxID=394221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCS10;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Saunders E., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Viollier P., Stephens C., Richardson P.;
RT   "Complete sequence of Maricaulis maris MCS10.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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:
CC       Reaction=ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-
CC         alanyl-tRNA(Ala); Xref=Rhea:RHEA:12540, Rhea:RHEA-COMP:9657,
CC         Rhea:RHEA-COMP:9923, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57972, ChEBI:CHEBI:78442, ChEBI:CHEBI:78497,
CC         ChEBI:CHEBI:456215; EC=6.1.1.7; Evidence={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; CP000449; ABI65301.1; -; Genomic_DNA.
DR   RefSeq; WP_011642948.1; NC_008347.1.
DR   SMR; Q0AQY6; -.
DR   STRING; 394221.Mmar10_1008; -.
DR   PRIDE; Q0AQY6; -.
DR   EnsemblBacteria; ABI65301; ABI65301; Mmar10_1008.
DR   KEGG; mmr:Mmar10_1008; -.
DR   eggNOG; ENOG4105CIM; Bacteria.
DR   eggNOG; COG0013; LUCA.
DR   HOGENOM; HOG000156965; -.
DR   KO; K01872; -.
DR   OMA; YHHTMFE; -.
DR   OrthoDB; 91428at2; -.
DR   BioCyc; MMAR394221:G1G79-1049-MONOMER; -.
DR   Proteomes; UP000001964; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004813; F:alanine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006419; P:alanyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
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_sf.
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; Q0AQY6.
DR   SWISS-2DPAGE; Q0AQY6.
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    884       Alanine--tRNA ligase.
FT                                /FTId=PRO_0000347666.
FT   METAL       565    565       Zinc. {ECO:0000255|HAMAP-Rule:MF_00036}.
FT   METAL       569    569       Zinc. {ECO:0000255|HAMAP-Rule:MF_00036}.
FT   METAL       675    675       Zinc. {ECO:0000255|HAMAP-Rule:MF_00036}.
FT   METAL       679    679       Zinc. {ECO:0000255|HAMAP-Rule:MF_00036}.
SQ   SEQUENCE   884 AA;  93754 MW;  3D671916D8F8B02F CRC64;
     MASLRDIRAT FLDYFAKHEH EVVPSAPLVP QDDPTLLFVN AGMVPFKNSF TGQEKRASLR
     ATSSQKCVRA GGKHNDLDNV GYTARHHTFF EMLGNFSFGD YFKEEAISHA WNLVTGEFGL
     PAEKLLVTVY AEDEQARALW RKIAGLTDDR IIGISTSDNF WSMGDTGPCG PCSEIFFDHG
     PSIAGGPPGS PDEDGDRFIE IWNLVFMQYE QLGPDERINL PKPSIDTGMG LERISAILQG
     KHNNYETDLF RNLIAAGESV LGVKAEGDAL ASHRVIADHL RSTCFLMADG VTPSNEGRGY
     VLRRIMRRAM RHAHLLGAGE PVMWKLVDAL KSEMGDAYPE LERAQALLEE TLQVEEERFQ
     RTLGRGLSLL EEATADMGEG DALAGATAFK LYDTYGFPLD LTQDALRAKG MTVDEAGFNS
     AMDKQRADAR ASKFSSGDAA PDAVWFAVRD KVGATAFTGY AGTGGKGRLT AIVSGGQEAK
     ALGSGQRAEL VFDETPFYGE SGGQCGDTGE IRFVDGAVFT VEDTQKRGGD MHAHIGVLTK
     GEITLGDVAA LDADAPRRAA IRANHSATHL AHAALRDVLG AHVTQKGSHV GPDRLRFDFS
     HNKSVSADQI AAIEAQVNAV IRQNVPVSTR EMTPDAAIEA GALALFGEKY GDTVRVLAMG
     QGLADHATPY SVELCGGTHV ERTGDIALFK IIAETAVSSG IRRIEAMTGE GARLYMDEQI
     GFGRAAADAL KTPPSDLATR VAALVDERRK LERQLAEAKK QLAMGGGASG APAGPETING
     VNFIGRVVEG VGGKDLRGLI DEAKAQMGSG VAAFIGVNDG KAALAVGVTD DLKDRFVAVD
     LVKAGAAAVG GKGGGGRPDF AQAGGPDGAK ANDGLAAIRA ALAG
//

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