(data stored in ACNUC7421 zone)

HOGENOM: COLP3_1_PE1008

ID   COLP3_1_PE1008                       STANDARD;      PRT;   876 AA.
AC   COLP3_1_PE1008; Q487H5;
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; (COLP3_1.PE1008).
GN   Name=alaS; OrderedLocusNames=CPS_1042;
OS   COLWELLIA PSYCHRERYTHRAEA 34H.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Colwellia.
OX   NCBI_TaxID=167879;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS COLP3_1.PE1008.
CC       Colwellia psychrerythraea 34H chromosome, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:SYA_COLP3
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.
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; Q487H5; -.
DR   EMBL; CP000083; AAZ25326.1; -; Genomic_DNA.
DR   RefSeq; YP_267790.1; NC_003910.7.
DR   ProteinModelPortal; Q487H5; -.
DR   STRING; Q487H5; -.
DR   GeneID; 3519393; -.
DR   GenomeReviews; CP000083_GR; CPS_1042.
DR   KEGG; cps:CPS_1042; -.
DR   NMPDR; fig|167879.3.peg.1008; -.
DR   TIGR; CPS_1042; -.
DR   eggNOG; COG0013; -.
DR   OMA; GESKTDQ; -.
DR   ProtClustDB; PRK00252; -.
DR   BioCyc; CPSY167879:CPS_1042-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; COLP3_1.PE1008; -.
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   876 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MIKSTAEVRQ AFLDFFATKQ HQIVKSSSLV PGNDATLLFT NAGMVPFKDV FLGAETRSYT
     RATSAQRCVR AGGKHNDLEN VGYTARHHTF FEMMGNFSFG DYFKNDAISY AWEFLTGELG
     LAKEKLLVTV YATDEEAFSY WRDEVGVPED KIIRIGDKSA NKKYESDNFW SMGDTGPCGP
     CSEIFYDHGE DIFGGPPGSP DEDGDRFIEI WNIVFMQFNR QSDGRMDPLP NPSIDTGMGL
     ERISAIMQNV HSNYEIDIFQ ALIKDTAALL DCSDLEHKSL RVIGDHIRSC SFLIVDGVVP
     SNEGRGYVLR RIIRRAIRHG HKLEATGHFF HKLVASLIAQ MGEAYPELAQ QQAIIEKLLR
     IEEEQFGRTL DRGMILLEDI LANLSGDIIK GDDVFKLYDT YGFPADLTAD IARERNLKID
     KDGFDVAMKQ QRERAQQASQ FGTDYNQQLK SDQNTAFKGY DNDSYSATVV ELFNSQDQDP
     VSQLNSGEQG IVILDHTPFY AESGGQVGDS GLLHLDGGVF EVTDTIKLGN AFAHRGTAHT
     DVGLNRRVKA EINVERRAAI VKNHTATHLL HEALRKVLGE HVTQKGSLCD SDKLRFDFSH
     FEGVTAQELH DVEQMVNNEI RRNHAKQTES MYIEEAKAKG AMALFGEKYD DEVRVVTLGD
     FSIELCGGVH VNRTGDIGFL KIVSESGIAA GVRRIEAVTG TGALDFINQQ TASLTTIAAL
     VKSDVTNASS KVELLISRSK QLEKEIGQLK QELAAQAGSD LVNNTIEING VKVLIADLGS
     VESKALRGMV DELKNKMQSG VIMLATANGP KVGLIAGVTK DLVGRVKAGD LVNMVAQQVG
     GKGGGRPDMA QAGGSQPENI TSALESVSAW LTEKLA
//

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