ID A0A1S4EQ86_DIACI Unreviewed; 1082 AA.
AC A0A1S4EQ86;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Alanine--tRNA ligase {ECO:0000256|ARBA:ARBA00017959};
DE EC=6.1.1.7 {ECO:0000256|ARBA:ARBA00013168};
GN Name=LOC103521690 {ECO:0000313|RefSeq:XP_017304364.1};
OS Diaphorina citri (Asian citrus psyllid).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Hemiptera; Sternorrhyncha; Psylloidea; Psyllidae;
OC Diaphorininae; Diaphorina.
OX NCBI_TaxID=121845 {ECO:0000313|Proteomes:UP000079169, ECO:0000313|RefSeq:XP_017304364.1};
RN [1] {ECO:0000313|RefSeq:XP_017304364.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; XP_017304364.1; XM_017448875.2.
DR AlphaFoldDB; A0A1S4EQ86; -.
DR STRING; 121845.A0A1S4EQ86; -.
DR PaxDb; 121845-A0A1S4EQ86; -.
DR GeneID; 103521690; -.
DR KEGG; dci:103521690; -.
DR OMA; HVFVQLM; -.
DR OrthoDB; 3639120at2759; -.
DR Proteomes; UP000079169; Unplaced.
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 Gene3D; 2.40.30.130; -; 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; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR012947; tRNA_SAD.
DR PANTHER; PTHR11777:SF9; ALANINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR PANTHER; PTHR11777; ALANYL-TRNA SYNTHETASE; 1.
DR Pfam; PF01411; tRNA-synt_2c; 2.
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; 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.
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};
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:UP000079169};
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 12..799
FT /note="Alanyl-transfer RNA synthetases family profile"
FT /evidence="ECO:0000259|PROSITE:PS50860"
FT BINDING 649
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03133"
FT BINDING 653
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03133"
FT BINDING 756
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03133"
FT BINDING 760
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03133"
SQ SEQUENCE 1082 AA; 121675 MW; 4EABC088A92F99B5 CRC64;
MNNPNISSYV RLCSKSIRSS FLDYFCNTQG HTLVKSSPIV PYGDDSIAFV NSGMCQFKNV
FLGLTPAPYP RVANSQKCVR VGGKHNDLSC AGRDSYHHTF FEMLGNWSFN DYYKRDACRM
ALEFLTKPPV SLPLDRLYFT YFGGSDQYGL PCDEETRDIW LELGVPRDHI KKEGMKCNFW
EMGSTGPCGY SSEIHYDMKG EPSSALARVN ADRNDLIEIW NIVFISHKRV SADTIVPLSK
NYIDTGLGFE RLVTILQNKT STYDTDLFLP LLETIEKVSG AKPYGRTFTT SNRTDLDTSY
RMLSDYSRMI TVALADNMFP DATAKLRNVV RDALLISEDV FKVKQGKLVK ELSYNIAEIL
GDVYPEIQDS INKIQLILGE ESRIFDNLRK AAVKEWKPLV KTQPELEQFN IMEEPGLVLG
VKYLTKQLAR DPSITEISGD MAFTLYDTYG LSKNIIQELA AAKKLTLCHE AFEQKLNELK
ERSKAKAASN VPDIDLMDLK HFPVTDDKYK YDYHYDTNSK RYTFPCLDTN LVGIVIGDQV
FCIDKHAIRH ARSGASIDSI QLEHNAWVGL IFDKTNLYAT AGGQIDDIGV AYLTNTTQEN
GKVEIGELAS LEGKIVHFGN VVSSFKVTPG LTSRVEVDAR MRLGCMRAHT TSHLLNAALR
RVLTCTYQKS CRVFSDECAL DFSVYGETLS VDSVAAVEKY INDVIANQVQ VDRRHMRASE
LPFLTHLTVI PGEIYPDDVI LIDISDKENV ISREPCCGTH VFNTGHIESC TVIGYKSYNH
GVRSIKCLTG DSSKAAVENG KHLSTAVKQL EATINQNSEQ TDEETLNQQN HEIKTLRELL
EDDLPYAVHK QNDHLLAELS KNVKLKLRQF AKVRITEELI EKCKEDTPYL VHYIRDDAVE
IQALPPLSQI SKPVLVLLYS LGELKARAYV PPQCTTPGFN AQAWLTPIMD RAEGKGVSSK
GSDVQHLYSM NPVKISNNVE DLVKQLVDIA RRSAAELRSN EVDIARRSAA ELRSNEVDIA
RRSAAELRSN EVDIARRSAA ELRSNEVDIA RRSAAELRSN EVDIARRSAA ELRSNEKQEH
KQ
//
