SYAC_BOMMO
ID SYAC_BOMMO Reviewed; 967 AA.
AC P21894;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Alanine--tRNA ligase, cytoplasmic {ECO:0000255|HAMAP-Rule:MF_03133};
DE EC=6.1.1.7 {ECO:0000255|HAMAP-Rule:MF_03133};
DE AltName: Full=Alanyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_03133};
DE Short=AlaRS {ECO:0000255|HAMAP-Rule:MF_03133};
OS Bombyx mori (Silk moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Bombycidae; Bombycinae; Bombyx.
OX NCBI_TaxID=7091;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 456-490.
RC TISSUE=Posterior silk gland;
RX PubMed=1701172; DOI=10.1016/s0021-9258(17)45301-4;
RA Chang P.K., Dignam J.D.;
RT "Primary structure of alanyl-tRNA synthetase and the regulation of its mRNA
RT levels in Bombyx mori.";
RL J. Biol. Chem. 265:20898-20906(1990).
RN [2]
RP PROTEIN SEQUENCE OF 456-488.
RC TISSUE=Posterior silk gland;
RX PubMed=2040280; DOI=10.1111/j.1432-1033.1991.tb16002.x;
RA Dignam J.D., Dignam S.S., Brumley L.L.;
RT "Alanyl-tRNA synthetase from Escherichia coli, Bombyx mori and Ratus ratus.
RT Existence of common structural features.";
RL Eur. J. Biochem. 198:201-210(1991).
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:0000255|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:0000255|HAMAP-Rule:MF_03133};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03133};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03133};
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-Rule:MF_03133}.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_03133}.
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DR EMBL; M55993; AAA27821.1; -; mRNA.
DR PIR; A38327; SYMTAT.
DR RefSeq; NP_001037452.1; NM_001043987.1.
DR AlphaFoldDB; P21894; -.
DR SMR; P21894; -.
DR STRING; 7091.BGIBMGA006216-TA; -.
DR GeneID; 693023; -.
DR KEGG; bmor:693023; -.
DR eggNOG; KOG0188; Eukaryota.
DR HOGENOM; CLU_004485_2_0_1; -.
DR OrthoDB; 129373at2759; -.
DR Proteomes; UP000005204; Unassembled WGS sequence.
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:InterPro.
DR Gene3D; 3.30.930.10; -; 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; 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 SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00344; alaS; 1.
DR PROSITE; PS50860; AA_TRNA_LIGASE_II_ALA; 1.
PE 1: Evidence at protein level;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm;
KW Direct protein sequencing; Ligase; Metal-binding; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome; RNA-binding; tRNA-binding; Zinc.
FT CHAIN 1..967
FT /note="Alanine--tRNA ligase, cytoplasmic"
FT /id="PRO_0000075285"
FT BINDING 605
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03133"
FT BINDING 609
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03133"
FT BINDING 724
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03133"
FT BINDING 728
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03133"
SQ SEQUENCE 967 AA; 108178 MW; 54CBF135153DA5D5 CRC64;
MDTSMTGNEI RKTFIDFFIK KGHKYVHSSS TIPLDDPTLL FANAGMNQFK PIFLGSVDPN
SDMAQYIRVV NTQKCIRAGG KHNDLDDVGK DVYHHTFFEM MGNWSFGDYF KKEICAWAWE
LLTDVFKLSR ERLYVTYFEG DPSSGLEPDL ECRNIWLNLG VPEAHILPGS MKDNFWEMGE
TGPCGPCSEL HYDRIGDREA AHLVNMDDPD VLEIWNLVFI QFNRETDGSL KLLPTKHIDC
GLGLERLVSV IQNKRANYDT DFFMPIFKAI ENATGVRPYS GKVGVDDVDG IDMAYRVLAD
HARTLTIALS DGGCPDNTGR GYVLRRILRR AVRYASEKLN AKPGFFGSLV YTVVELLGDV
FPEIKKDPDS IVHVINEEEV QFLKTLLRGR NLLYRTIEKL NNSKTLPGDV AWRLYDTYGF
PIDLTQLMCE EKGLNVDMEG YEKSRKESQL VSQGKAAGQE DLIALDVHAI SHLQDTGIPA
TDDSPKYNYL PSSTDKDALY TFAPCTAKIV ALRKNKEFVS EISSGQECGV ILDRTSFYAE
QGGQIFDEGY MVKIDDETVE FTVKNVQVKG GYVLHAGKVE GILKVGDTLS LHIDTERRRL
VMNNHTGTHV LNNVLRKVLG NDSDQRGSLV MPDRLRFDFT NKGPMTIKQI KDTENEIKEI
IAKNKTVYAN YTSLSEAKKI NGLRAMFDEH YPDPVRVVSV GVPVEDLIKN PDAPTGFETS
VEFCGGSHLH RTSHIGEYVI VSEEGIAKGI RRIVAVTGPE AIKAINKLSV LENEVNNVAN
FIKEQNESIS HKEVSKKIVD LTNEISQAQI SYWKKDELRN MLKNLKKQLD DKERAEKAII
ITQVTEKAKE LCLERKESKY IVSELKAFGN TKALDGALKQ VKQFCPNSAA MFFSVDKDAD
KIYCLAAVPK SDVEKGLLAS EWVQSVVDII GGKGGGKAES AQASGNNPNS LNEAIQIANE
YAKSKLN
