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Database: UniProt/SWISS-PROT
Entry: SYA_VIBCH
LinkDB: SYA_VIBCH
Original site: SYA_VIBCH 
ID   SYA_VIBCH               Reviewed;         860 AA.
AC   Q56648; Q9KUH6;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   26-FEB-2020, entry version 126.
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}; OrderedLocusNames=VC_0545;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 44-452.
RC   STRAIN=ATCC 25870 / Classical Inaba 569B / Serotype O1;
RA   Gupta N., Bhasin N., Ghosh A.;
RL   Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the attachment of alanine to tRNA(Ala) in a two-
CC       step reaction: alanine is first activated by ATP to form Ala-AMP and
CC       then transferred to the acceptor end of tRNA(Ala). Also edits
CC       incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing
CC       domain. {ECO:0000255|HAMAP-Rule:MF_00036}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-
CC         tRNA(Ala); Xref=Rhea:RHEA:12540, Rhea:RHEA-COMP:9657, Rhea:RHEA-
CC         COMP:9923, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57972,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78497, ChEBI:CHEBI:456215; EC=6.1.1.7;
CC         Evidence={ECO:0000255|HAMAP-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-Rule:MF_00036};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00036}.
CC   -!- DOMAIN: Consists of three domains; the N-terminal catalytic domain, the
CC       editing domain and the C-terminal C-Ala domain. The editing domain
CC       removes incorrectly charged amino acids, while the C-Ala domain, along
CC       with tRNA(Ala), serves as a bridge to cooperatively bring together the
CC       editing and aminoacylation centers thus stimulating deacylation of
CC       misacylated tRNAs. {ECO:0000255|HAMAP-Rule:MF_00036}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00036}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA99922.1; Type=Frameshift; Evidence={ECO:0000305};
DR   EMBL; AE003852; AAF93713.1; -; Genomic_DNA.
DR   EMBL; L78074; AAA99922.1; ALT_FRAME; Genomic_DNA.
DR   PIR; G82310; G82310.
DR   RefSeq; NP_230196.1; NC_002505.1.
DR   RefSeq; WP_000481017.1; NZ_LT906614.1.
DR   SMR; Q56648; -.
DR   STRING; 243277.VC_0545; -.
DR   PRIDE; Q56648; -.
DR   DNASU; 2615214; -.
DR   EnsemblBacteria; AAF93713; AAF93713; VC_0545.
DR   GeneID; 2615214; -.
DR   KEGG; vch:VC0545; -.
DR   PATRIC; fig|243277.26.peg.521; -.
DR   eggNOG; ENOG4105CIM; Bacteria.
DR   eggNOG; COG0013; LUCA.
DR   HOGENOM; CLU_004485_1_1_6; -.
DR   KO; K01872; -.
DR   OMA; YHHTMFE; -.
DR   BioCyc; VCHO:VC0545-MONOMER; -.
DR   Proteomes; UP000000584; Chromosome 1.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004813; F:alanine-tRNA ligase activity; ISS:TIGR.
DR   GO; GO:0016597; F:amino acid binding; IBA:GO_Central.
DR   GO; GO:0002161; F:aminoacyl-tRNA editing activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IBA:GO_Central.
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; ISS:TIGR.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IBA:GO_Central.
DR   GO; GO:0006400; P:tRNA modification; IBA:GO_Central.
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;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome; RNA-binding;
KW   tRNA-binding; Zinc.
FT   CHAIN           1..860
FT                   /note="Alanine--tRNA ligase"
FT                   /id="PRO_0000075241"
FT   METAL           563
FT                   /note="Zinc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT   METAL           567
FT                   /note="Zinc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT   METAL           665
FT                   /note="Zinc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT   METAL           669
FT                   /note="Zinc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
SQ   SEQUENCE   860 AA;  93827 MW;  0A0EA97910F48FDB CRC64;
     MFMSTDEVRR AFLSFFESKG HQIVESSSLV PANDPTLLFT NAGMNQFKDC FLGLEKRAYT
     RATTAQRCVR AGGKHNDLEN VGFTARHHTF FEMLGNFSFG DYFKEDAIQY AWEFLTDVLQ
     LPKERLLVTV YETDDEAFDI WNKKVGIPAD RIIRIGDKKG GKKFDSDNFW QMGDTGPCGP
     CTEIFYDHGD HIWGGPPGSP EEDGDRFIEI WNNVFMQFNR HADGTMEPLP KPSVDTGMGI
     ERISAIMQGV HSNYEIDVFQ TLIKAAADAI GYQDLTNQSL RVVADHIRSC AFLIVDGVMP
     SNEGRGYVLR RIIRRAVRHG NKLGAQGAFF HKLVGPLAEV MGTAGVELKK QQALVEKVLR
     IEEENFGRTL DRGMSILNDA LDQLSGQVLD GETVFKLYDT YGFPADLTND VARERGFSID
     EAGFEQAMEE QRQRAREAGQ FGTDYNSLIK SATNTEFCGY TASRGQSVVR EMFVEGAEVS
     TLSAGDKAII VLDNTPFYAE SGGQCGDTGV LKTDAGIFHV EDTQKLGNAI AHHGVIAQGV
     LATGDQVDAI VDEKRRAAIS LNHSATHLLH AALRKVLGEH VAQKGSLVRA ETLRFDFSHL
     EAMTAAEIKE VERLVNQEVR RNHSIETNIM NIDEAKAKGA MALFGEKYDD QVRVLSMGDF
     STELCGGIHA SNTGDIGLFK IISEGGIAAG IRRIEAVTGE GALDYLDAQQ AQHDAKVSEM
     AAKAKLLEKE IQQLKDKLAA KESAGLINQV KQIAGVNVLV AQLNGADNKA LRGMVDDLKN
     QLSSGIIMLG NVAEGKVGLI AGVTNDLTNK VKAGELVNMV ALQVGGKGGG RPDMAQAGGT
     DAHALPSALE SVDAWIAERL
//
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