(data stored in ACNUC7421 zone)

SWISSPROT: SYA_PARDP

ID   SYA_PARDP               Reviewed;         885 AA.
AC   A1AZL6;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   08-MAY-2019, entry version 85.
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=Pden_0598;
OS   Paracoccus denitrificans (strain Pd 1222).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=318586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pd 1222;
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., Munk A.C., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Spiro S., Richardson D.J., Moir J.W.B., Ferguson S.J.,
RA   van Spanning R.J.M., Richardson P.;
RT   "Complete sequence of chromosome 1 of Paracoccus denitrificans
RT   PD1222.";
RL   Submitted (DEC-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; CP000489; ABL68710.1; -; Genomic_DNA.
DR   RefSeq; WP_011746943.1; NC_008686.1.
DR   SMR; A1AZL6; -.
DR   STRING; 318586.Pden_0598; -.
DR   PRIDE; A1AZL6; -.
DR   EnsemblBacteria; ABL68710; ABL68710; Pden_0598.
DR   KEGG; pde:Pden_0598; -.
DR   eggNOG; ENOG4105CIM; Bacteria.
DR   eggNOG; COG0013; LUCA.
DR   HOGENOM; HOG000156965; -.
DR   KO; K01872; -.
DR   OMA; YHHTMFE; -.
DR   BioCyc; PDEN318586:G1GW1-606-MONOMER; -.
DR   Proteomes; UP000000361; Chromosome 1.
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; A1AZL6.
DR   SWISS-2DPAGE; A1AZL6.
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    885       Alanine--tRNA ligase.
FT                                /FTId=PRO_0000347712.
FT   METAL       563    563       Zinc. {ECO:0000255|HAMAP-Rule:MF_00036}.
FT   METAL       567    567       Zinc. {ECO:0000255|HAMAP-Rule:MF_00036}.
FT   METAL       677    677       Zinc. {ECO:0000255|HAMAP-Rule:MF_00036}.
FT   METAL       681    681       Zinc. {ECO:0000255|HAMAP-Rule:MF_00036}.
SQ   SEQUENCE   885 AA;  95452 MW;  D4BB6DCF75987DB0 CRC64;
     MPSLNDVRST FLNYFERNGH RVVESSPLVP RNDPTLMFTN SGMVQFKNLF TGVETRDYKR
     ATTAQKCVRA GGKHNDLDNV GYTARHHTFF EMLGNFSFGD YFKDGAIPFA WELLTKDFGI
     PKDKLLVTVY HTDDEAADIW KKVAGLSDDR IIRIPTSDNF WQMGPTGPCG PCTEIFYDHG
     EQIWGGPPGS ADEDGDRFIE IWNLVFMQNE QFEDGTMRAL DMQSIDTGMG LERIGALLQG
     KHDNYDTDLM RGLIEASAHA TSADPDGPGK VHHRVIADHL RSTSFLIADG VMPSNEGRGY
     VLRRIMRRAM RHAHMLGAKD PVMHRLVPAL VREMGAAYPE LGRAQALIEE TLKLEETRFK
     QTLDRGLRLL DDELAKLPEG ANLPGEAAFK LYDTYGFPLD LTQDALREKG RAVDTAGFDS
     AMAEQKAKAR AAWAGSGETK DAAIWFDIAE EHGATEFLGY DTEISEGQVL ALVQDGAAVE
     EAGEGQQVQI VVNQTPFYGE AGGQVGDTGL IKTETGAARV TDTKKTGGVF IHIAEVTLGT
     IQRGQGAQLS VDHDRRSAIR ANHSATHLLH EALRRALGEH VAQRGSLNAP DRLRFDFSHA
     KAMTPEELAQ VEREVNDFIR QNSPVETRIM TPDDARALGA QALFGEKYGD EVRVVSMGEL
     PGSGKGTGGQ TYSLELCGGT HVARTGDIGM FALTSETASA AGIRRIEALT GQAAMDELRR
     VDGELNEIAG IVKAQAGDVV SKVRALADER KALANEVAQL KRQLAMGGGS EDKPREINGI
     KLIARRVEGV SGKELGPLVD EMKSRLGSGA VVVLAEADGK ATVAAGVTPD LTGRISAVEL
     VQTATAALGG KGGGGRPDRA QGGAPSLAAA DSAISAVETL IGEKA
//

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