ID A0A0N0BEJ4_9HYME Unreviewed; 1206 AA.
AC A0A0N0BEJ4;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Alanine--tRNA ligase {ECO:0000256|ARBA:ARBA00017959};
DE EC=6.1.1.7 {ECO:0000256|ARBA:ARBA00013168};
GN ORFNames=WN51_02317 {ECO:0000313|EMBL:KOX71748.1};
OS Melipona quadrifasciata.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Melipona.
OX NCBI_TaxID=166423 {ECO:0000313|EMBL:KOX71748.1, ECO:0000313|Proteomes:UP000053105};
RN [1] {ECO:0000313|EMBL:KOX71748.1, ECO:0000313|Proteomes:UP000053105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0111107301 {ECO:0000313|EMBL:KOX71748.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KOX71748.1};
RA Pan H., Kapheim K.;
RT "The genome of Melipona quadrifasciata.";
RL Submitted (JUL-2015) 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 tRNA(Ala) via its editing domain.
CC {ECO:0000256|HAMAP-Rule:MF_03133}.
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:0000256|HAMAP-Rule:MF_03133};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03133};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_03133};
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_03133}.
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:0000256|HAMAP-Rule:MF_03133}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Alax-L subfamily. {ECO:0000256|ARBA:ARBA00008429}.
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DR EMBL; KQ435830; KOX71748.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N0BEJ4; -.
DR STRING; 166423.A0A0N0BEJ4; -.
DR OrthoDB; 3639120at2759; -.
DR Proteomes; UP000053105; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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:InterPro.
DR CDD; cd00673; AlaRS_core; 1.
DR CDD; cd03181; GST_C_EF1Bgamma_like; 1.
DR Gene3D; 1.20.1050.10; -; 1.
DR Gene3D; 2.40.30.130; -; 1.
DR Gene3D; 3.10.310.40; -; 1.
DR HAMAP; MF_00036_B; Ala_tRNA_synth_B; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
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; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR012947; tRNA_SAD.
DR NCBIfam; TIGR00344; alaS; 1.
DR PANTHER; PTHR11777:SF9; ALANINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR PANTHER; PTHR11777; ALANYL-TRNA SYNTHETASE; 1.
DR Pfam; PF02272; DHHA1; 1.
DR Pfam; PF00043; GST_C; 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; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR SUPFAM; SSF101353; Putative anticodon-binding domain of alanyl-tRNA synthetase (AlaRS); 1.
DR SUPFAM; SSF55186; ThrRS/AlaRS common domain; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS50860; AA_TRNA_LIGASE_II_ALA; 1.
DR PROSITE; PS50405; GST_CTER; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_03133};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_03133}; Coiled coil {ECO:0000256|SAM:Coils};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_03133};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_03133};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_03133};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_03133}; Reference proteome {ECO:0000313|Proteomes:UP000053105};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_03133};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|HAMAP-
KW Rule:MF_03133}; Zinc {ECO:0000256|HAMAP-Rule:MF_03133}.
FT DOMAIN 1..780
FT /note="Alanyl-transfer RNA synthetases family profile"
FT /evidence="ECO:0000259|PROSITE:PS50860"
FT DOMAIN 1077..1206
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
FT COILED 828..855
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 598
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03133"
FT BINDING 602
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03133"
FT BINDING 737
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03133"
FT BINDING 741
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03133"
SQ SEQUENCE 1206 AA; 135180 MW; 5A13ACEC8C29BC76 CRC64;
MSAEQIRQAY IDFFKSKNHE YVHSSSTIPH DDPTLLFTNA GMNQFKPIFL GIVDPNSDLG
KLVRAVNSQK CIRAGGKHND LDDVGKDVYH HTFFEMMGNW SFGDYFKKEI CTWAWEFLTV
KLKLPADRLY VTYFGGEEKN NLKPDEECKE IWLSLGVAPN HVLPGNMKDN FWEMGETGPC
GPCSEIHYDR IGNREAAHLV NQDDPDVLEI WNLVFIQFNR ETDGSLKLLP KKHVDCGLGL
ERLVSVIQNK KANYDTDLFV PLFDAIQKGT GAPPYQGRIG MEDKDGIDMA YRVLADHART
ITIALADGGV PDNTGRGRIL RRAVRYATEK LNAKPGFFGS LVNVVVDLLG NTFPEVTKDP
QYIIDIINEE ETQFLKTLSR GRNLLNRTIT KLESSNILPG DVAWRLYDTY GFPVDLTQLM
AEEKGLKVDI IGYEEAKKQA QLISQSKSGG VDDQINLDVH AITDLQNKGI KPTNDLPKYN
YNVINNNLYE EYEFVPCSGT VITLRSAKTF VDEISSGEEV GILLDQTNFY AEQGGQIYDE
GFLVKINDED TEVRIKNVQV RGGYVLHIGT VGQGKLRKGD KVSLNIDITR RRFIMSNHTA
THVLNYALRK VLGAEVDQKG SLVAPDRLRF DFTNKEYNIH FKTFLELIYS KYLFIGAMTA
EQIRKVEEIV NDMIKENRKV YTKESNLALA KTIQGLRAMF EETYPDPVRI VSLGIQVEDL
EKDPLGPGAL QTSVEFCGGT HLHYTEHIGD FVITSEEAIA KGIRRIVALT GPEATKAQKK
ASVLESHLDR LQAIIVADTS GVNIKEHIKK IIELTDDISH AVISSWKKDK MRKMLKDLKK
TLDDKERAAK TAIANAVVDT IQQIIQQDIG RLVLVEVLQA YSNTKALDSA LKKIKAISPE
TSALLISVDL DAKKIFALCA VSKPAVNKGL KANEWIQEIV PLMEGKGGGK TESAQASGTN
ISCVTKLIYT AKNFANSKLG IAEDSVNENH EQLKNNEKSI CSENSKNKLV LSSDIGSVKY
YRTQIVAKYS DIELITLQYK NDDTSKSIKL EGNGFELFDS NAIAFYLSNN QLKCSSNPFA
FSEVLQWLSY ADNHILPAVL GWIVPCFSKN VSNDIKTNIK TSKEDVLSSL KKLNNILLTK
TYLVGERVSL ADIAVFTALM PLYEYVLDSM SRKQYTNLNR WFFTILNQSE VASAIKKFKV
CEKAVN
//
