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Database: UniProt
Entry: W0DH46_9AQUI
LinkDB: W0DH46_9AQUI
Original site: W0DH46_9AQUI 
ID   W0DH46_9AQUI            Unreviewed;       863 AA.
AC   W0DH46;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   08-MAY-2019, entry version 38.
DE   RecName: Full=Alanine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00036};
DE            EC=6.1.1.7 {ECO:0000256|HAMAP-Rule:MF_00036};
DE   AltName: Full=Alanyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00036};
DE            Short=AlaRS {ECO:0000256|HAMAP-Rule:MF_00036};
GN   Name=alaS {ECO:0000256|HAMAP-Rule:MF_00036};
GN   ORFNames=THERU_07665 {ECO:0000313|EMBL:AHE96572.1};
OS   Thermocrinis ruber.
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Thermocrinis.
OX   NCBI_TaxID=75906 {ECO:0000313|Proteomes:UP000018914};
RN   [1] {ECO:0000313|EMBL:AHE96572.1, ECO:0000313|Proteomes:UP000018914}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23557 {ECO:0000313|EMBL:AHE96572.1,
RC   ECO:0000313|Proteomes:UP000018914};
RG   DOE Joint Genome Institute;
RA   Eisen J., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA   Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA   Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL   Submitted (DEC-2013) 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:0000256|HAMAP-Rule:MF_00036,
CC       ECO:0000256|SAAS:SAAS00015829}.
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:0000256|HAMAP-
CC         Rule:MF_00036, ECO:0000256|SAAS:SAAS01125460};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00036};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00036};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00036,
CC       ECO:0000256|SAAS:SAAS00832879}.
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:0000256|HAMAP-Rule:MF_00036}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family. {ECO:0000256|HAMAP-Rule:MF_00036,
CC       ECO:0000256|SAAS:SAAS00575517}.
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DR   EMBL; CP007028; AHE96572.1; -; Genomic_DNA.
DR   RefSeq; WP_025306648.1; NZ_CP007028.1.
DR   STRING; 932678.THERU_07665; -.
DR   EnsemblBacteria; AHE96572; AHE96572; THERU_07665.
DR   KEGG; trd:THERU_07665; -.
DR   PATRIC; fig|75906.3.peg.1475; -.
DR   KO; K01872; -.
DR   OrthoDB; 91428at2; -.
DR   Proteomes; UP000018914; 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;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00036,
KW   ECO:0000256|SAAS:SAAS00249969, ECO:0000313|EMBL:AHE96572.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00036,
KW   ECO:0000256|SAAS:SAAS00250154}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000018914};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00036,
KW   ECO:0000256|SAAS:SAAS00299154};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00036,
KW   ECO:0000256|SAAS:SAAS00249928};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00036,
KW   ECO:0000256|SAAS:SAAS00423853};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00036,
KW   ECO:0000256|SAAS:SAAS00250206};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00036,
KW   ECO:0000256|SAAS:SAAS00250204};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018914};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_00036,
KW   ECO:0000256|SAAS:SAAS00250135};
KW   tRNA-binding {ECO:0000256|HAMAP-Rule:MF_00036,
KW   ECO:0000256|SAAS:SAAS00250194};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00036, ECO:0000256|SAAS:SAAS00423813}.
FT   DOMAIN        1    701       AA_TRNA_LIGASE_II_ALA.
FT                                {ECO:0000259|PROSITE:PS50860}.
FT   COILED      717    751       {ECO:0000256|SAM:Coils}.
FT   METAL       556    556       Zinc. {ECO:0000256|HAMAP-Rule:MF_00036}.
FT   METAL       560    560       Zinc. {ECO:0000256|HAMAP-Rule:MF_00036}.
FT   METAL       658    658       Zinc. {ECO:0000256|HAMAP-Rule:MF_00036}.
FT   METAL       662    662       Zinc. {ECO:0000256|HAMAP-Rule:MF_00036}.
SQ   SEQUENCE   863 AA;  98006 MW;  397AAA67FA12F294 CRC64;
     MSGNEIRELF LSFFESKGHT RVKSASLVPE SDPTLLFTNA GMVPFKNVFL GLEKRPYKRA
     VSCQKCLRVS GKHNDLESVG YTSRHHTFFE MLGNFSFGDY FKREAILYAW EFVTEYLKLP
     KEKLYVSVFR DDEEAYRIWN EEVGLPSERI WRLGEEDNFW QMGDTGPCGP SSEIYVDRGE
     EYGEERFLEI WNLVFMQYNR DEKGNLTPLP NPNIDTGMGL ERIASVLQGT KTNFEIDLIK
     PLIDFGQEIS GKTYGENFED TVAMRVIADH LRAITFAISD GVLPSNTARG YVIRRILRRA
     LRFGYKLGIR EPFLYKGVDV VVEVMKDAYP ELLQTRAFVK GVVKAEEERF LHTFRNSMPV
     VEEFINTALE EGRRFLKGEE VFKLYDTYGF PLDLLEEIAK EKGLSLDMEG FEREMEIQRE
     RARQNFKIQT KEVQPIYQHL KNIGRTSTFV GYEQYVAQSK VIALLKNGEL VSELKEGEEG
     EVFLDITPFY AERGGQIGDT GTIESVDGLF VVDDTQSPVD GVISHKGKVV KGTIKVGDQV
     IASIDRERRE DIKRNHTATH LLHSALRLVL GEHVRQAGSL VADKYLRFDF THFQALSVDE
     LKRVEELVNE QIRKNEPVIV EEKDYREAIK EGAIAIFEEK YGERVRVLSV GDFSKELCGG
     THVSRTGEIG YFKIISESSI GAGLRRIVAK TGRWAVEEAF LESLTLKQVA QSLGVSTEEV
     LEGLSKLQER VKELERELQR VKSESARKQA KERIKEEGFG EYTLFYGVLE DVEGDLLREL
     ADQFRQGRTK TVVFLASKRE GKLSTLIALS KDLVGSLSAK ELIKEVGKVL GGGGGGRDDL
     AQGGGTKPEN FEKALELLKE KLR
//
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