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Alanine--tRNA ligase (EC 6.1.1.7) (Alanyl-tRNA synthetase) (AlaRS)

 B3T833_9ARCH            Unreviewed;       898 AA.
B3T833;
02-SEP-2008, integrated into UniProtKB/TrEMBL.
02-SEP-2008, sequence version 1.
27-SEP-2017, entry version 36.
RecName: Full=Alanine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00036};
EC=6.1.1.7 {ECO:0000256|HAMAP-Rule:MF_00036};
AltName: Full=Alanyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00036};
Short=AlaRS {ECO:0000256|HAMAP-Rule:MF_00036};
Name=alaS {ECO:0000256|HAMAP-Rule:MF_00036};
ORFNames=ALOHA_HF4000APKG4H17ctg1g36 {ECO:0000313|EMBL:ABZ08742.1};
uncultured marine crenarchaeote HF4000_APKG4H17.
Archaea; Thaumarchaeota; Nitrosopumilales; environmental samples.
NCBI_TaxID=455589 {ECO:0000313|EMBL:ABZ08742.1};
[1] {ECO:0000313|EMBL:ABZ08742.1}
NUCLEOTIDE SEQUENCE.
PubMed=18580971; DOI=10.1038/ismej.2008.62;
Konstantinidis K.T., Delong E.F.;
"Genomic patterns of recombination, clonal divergence and environment
in marine microbial populations.";
ISME J. 2:1052-1065(2008).
-!- FUNCTION: Catalyzes the attachment of alanine to tRNA(Ala) in a
two-step reaction: alanine is first activated by ATP to form Ala-
AMP and then transferred to the acceptor end of tRNA(Ala). Also
edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its
editing domain. {ECO:0000256|HAMAP-Rule:MF_00036}.
-!- CATALYTIC ACTIVITY: ATP + L-alanine + tRNA(Ala) = AMP +
diphosphate + L-alanyl-tRNA(Ala). {ECO:0000256|HAMAP-
Rule:MF_00036, ECO:0000256|SAAS:SAAS00346608}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000256|HAMAP-Rule:MF_00036};
Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-
Rule:MF_00036};
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00036,
ECO:0000256|SAAS:SAAS00346605}.
-!- DOMAIN: Consists of three domains; the N-terminal catalytic
domain, the editing domain and the C-terminal C-Ala domain. The
editing domain removes incorrectly charged amino acids, while the
C-Ala domain, along with tRNA(Ala), serves as a bridge to
cooperatively bring together the editing and aminoacylation
centers thus stimulating deacylation of misacylated tRNAs.
{ECO:0000256|HAMAP-Rule:MF_00036}.
-!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
family. {ECO:0000256|HAMAP-Rule:MF_00036,
ECO:0000256|SAAS:SAAS00541819}.
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EMBL; EU016635; ABZ08742.1; -; Genomic_DNA.
ProteinModelPortal; B3T833; -.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0004813; F:alanine-tRNA ligase activity; IEA:UniProtKB-UniRule.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
GO; GO:0006419; P:alanyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
HAMAP; MF_00036_A; Ala_tRNA_synth_A; 1.
InterPro; IPR002318; Ala-tRNA-lgiase_IIc.
InterPro; IPR018162; Ala-tRNA-ligase_IIc_anticod-bd.
InterPro; IPR018165; Ala-tRNA-synth_IIc_core.
InterPro; IPR018164; Ala-tRNA-synth_IIc_N.
InterPro; IPR022429; Ala-tRNA_lgiase_arc.
InterPro; IPR003156; DHHA1_dom.
InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
InterPro; IPR009000; Transl_B-barrel.
InterPro; IPR012947; tRNA_SAD.
Pfam; PF02272; DHHA1; 1.
Pfam; PF01411; tRNA-synt_2c; 1.
Pfam; PF07973; tRNA_SAD; 1.
PRINTS; PR00980; TRNASYNTHALA.
SMART; SM00863; tRNA_SAD; 1.
SUPFAM; SSF101353; SSF101353; 1.
SUPFAM; SSF50447; SSF50447; 1.
SUPFAM; SSF55186; SSF55186; 1.
TIGRFAMs; TIGR03683; A-tRNA_syn_arch; 1.
TIGRFAMs; TIGR00344; alaS; 1.
PROSITE; PS50860; AA_TRNA_LIGASE_II_ALA; 1.
3: Inferred from homology;
Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00036,
ECO:0000256|SAAS:SAAS00017577, ECO:0000313|EMBL:ABZ08742.1};
ATP-binding {ECO:0000256|HAMAP-Rule:MF_00036,
ECO:0000256|SAAS:SAAS00017587}; Coiled coil {ECO:0000256|SAM:Coils};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00036,
ECO:0000256|SAAS:SAAS00017589};
Ligase {ECO:0000256|HAMAP-Rule:MF_00036,
ECO:0000256|SAAS:SAAS00017577, ECO:0000313|EMBL:ABZ08742.1};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_00036,
ECO:0000256|SAAS:SAAS00017586};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00036,
ECO:0000256|SAAS:SAAS00017587};
Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00036,
ECO:0000256|SAAS:SAAS00017579};
RNA-binding {ECO:0000256|HAMAP-Rule:MF_00036,
ECO:0000256|SAAS:SAAS00017585};
tRNA-binding {ECO:0000256|HAMAP-Rule:MF_00036,
ECO:0000256|SAAS:SAAS00017585};
Zinc {ECO:0000256|HAMAP-Rule:MF_00036, ECO:0000256|SAAS:SAAS00017591}.
DOMAIN 70 732 AA_TRNA_LIGASE_II_ALA.
{ECO:0000259|PROSITE:PS50860}.
COILED 740 764 {ECO:0000256|SAM:Coils}.
METAL 585 585 Zinc. {ECO:0000256|HAMAP-Rule:MF_00036}.
METAL 589 589 Zinc. {ECO:0000256|HAMAP-Rule:MF_00036}.
METAL 689 689 Zinc. {ECO:0000256|HAMAP-Rule:MF_00036}.
METAL 693 693 Zinc. {ECO:0000256|HAMAP-Rule:MF_00036}.
SEQUENCE 898 AA; 101708 MW; CBE8BEC536A2712B CRC64;
MDKKEILSKF SADPERYYKV KLFDDEKFER KSCATCKRFY WTIDENRVNC PDHSDDTYSF
IGNPPTTKRF DYTQAWKEVE SFFVKNGHTS VNRYPVVCRW RDDLYFTIAS IVDFQRVMGS
KVVFEFPANP LVVPQTCLRF KDLENVGVTG RHFSSFCMIG QHSIPNSNGY WKDECVDLDY
RLLTEQFGVD KKEVVFVEDV WEGGGSFGSS LEFFVKGLEL GNAVFTEFQG DLSNYKTLDQ
QIIDMGAGLE RFAWLTMGTP TAYDCCFGPI TNNLLQQAGI DTNDELLVTY FTKIAKHFER
FSDLSEVRKN AIKSAGLSDE QVNKIIIPLE GIYLIVDHIR TLIFAISDGA LPSNVGGGYN
LRMMLRRIIS TMDRLSLKLD MNGIVDAQID YLKNTYPELE KTREDIKTII GIESGRYENS
KLRMEKIVSK LNQKPTVDDL IRLYESDGVT PDYLKEMKVI SDIPSTFYSK LSELHQSKKQ
KEQDQLSLAG LPGTELLYYG DDPKEFDAKV LKSFDKYVVL DKTSFYARGG GQEPDHGTIE
NFEVVDVSKH GNVIVHELKN GIPKEGSTVS CVVNSKRRDD ITKNHTSTHI LNSSSRSVLG
SWVWQHSAFK EEDHARLDIT HHSALTDDEI TKIEDLANSV VEKNIPVTIE NFDRGTAEQK
YGFKIYQGGI VPVKSIRIVS IEDFDIEACG GTHVKQTDEI ELIKITRTKR IQDGVVRIEF
VSGDTALDYV KRHDADLIKK SSELKDKTEL KEKRREQKQE LREKFPLLVE NIIQSKIGSA
IVDEIVVDIT ESGKPNFCCT DSDQYDEFFH IGLGEKLIEK DPWMVYCGVF EDGDKIRAII
YSGDQAGKDK KAGDIAKIVS EILGGAGGGT QRFAQGGGKD KSKKNDAIEK VKSMVLEV


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