(data stored in ACNUC7421 zone)

HOGENOM: MARMM_1_PE1005

ID   MARMM_1_PE1005                       STANDARD;      PRT;   884 AA.
AC   MARMM_1_PE1005; Q0AQY6;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Alanyl-tRNA synthetase; EC=6.1.1 7;AltName:
DE   Full=Alanine--tRNA ligase; Short=AlaRS; (MARMM_1.PE1005).
GN   Name=alaS; OrderedLocusNames=Mmar10_1008;
OS   MARICAULIS MARIS MCS10.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Hyphomonadaceae; Maricaulis.
OX   NCBI_TaxID=394221;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS MARMM_1.PE1005.
CC       Maricaulis maris MCS10, complete genome.
CC       Genomes
CC   -!- ANNOTATIONS ORIGIN:SYA_MARMM
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.
CC   -!- GENE_FAMILY: HOG000156965 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q0AQY6; -.
DR   EMBL; CP000449; ABI65301.1; -; Genomic_DNA.
DR   RefSeq; YP_756239.1; NC_008347.1.
DR   ProteinModelPortal; Q0AQY6; -.
DR   STRING; Q0AQY6; -.
DR   GeneID; 4284348; -.
DR   GenomeReviews; CP000449_GR; Mmar10_1008.
DR   KEGG; mmr:Mmar10_1008; -.
DR   NMPDR; fig|394221.5.peg.985; -.
DR   eggNOG; COG0013; -.
DR   OMA; GESKTDQ; -.
DR   PhylomeDB; Q0AQY6; -.
DR   ProtClustDB; PRK00252; -.
DR   BioCyc; MMAR394221:MMAR10_1008-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004813; F:alanine-tRNA ligase activity; IEA: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-synth_IIc.
DR   InterPro; IPR018162; Ala-tRNA-synth_IIc_anticod-bd.
DR   InterPro; IPR018165; Ala-tRNA-synth_IIc_core.
DR   InterPro; IPR018164; Ala-tRNA-synth_IIc_N.
DR   InterPro; IPR023033; Ala_tRNA_synth_euk/bac.
DR   InterPro; IPR003156; Pesterase_DHHA1.
DR   InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
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; Ala-tRNA-synth_IIc_anticod-bd; 1.
DR   SUPFAM; SSF55186; Thr/Ala-tRNA-synth_IIc_edit; 1.
DR   TIGRFAMs; TIGR00344; AlaS; 1.
DR   PROSITE; PS50860; AA_TRNA_LIGASE_II_ALA; 1.
DR   HOGENOMDNA; MARMM_1.PE1005; -.
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Metal-binding; Nucleotide-binding; Protein biosynthesis;
KW   RNA-binding; tRNA-binding; Zinc.
SQ   SEQUENCE   884 AA;  UNKNOWN MW;  UNKNOWN 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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