ID J9DQX9_EDHAE Unreviewed; 1149 AA.
AC J9DQX9;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Alanine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_03133};
DE EC=6.1.1.7 {ECO:0000256|HAMAP-Rule:MF_03133};
DE AltName: Full=Alanyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_03133};
DE Short=AlaRS {ECO:0000256|HAMAP-Rule:MF_03133};
GN Name=ALA1 {ECO:0000256|HAMAP-Rule:MF_03133};
GN ORFNames=EDEG_00097 {ECO:0000313|EMBL:EJW04980.1};
OS Edhazardia aedis (strain USNM 41457) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Edhazardia.
OX NCBI_TaxID=1003232 {ECO:0000313|EMBL:EJW04980.1, ECO:0000313|Proteomes:UP000003163};
RN [1] {ECO:0000313|EMBL:EJW04980.1, ECO:0000313|Proteomes:UP000003163}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USNM 41457 {ECO:0000313|EMBL:EJW04980.1,
RC ECO:0000313|Proteomes:UP000003163};
RA Liu Z.J., Shi F.L., Lu J.Q., Li M., Wang Z.L.;
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000003163}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USNM 41457 {ECO:0000313|Proteomes:UP000003163};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cuomo C.A., Sanscrainte N.D., Goldberg J.M., Heiman D., Young S., Zeng Q.,
RA Becnel J.J., Birren B.W.;
RT "Contrasting host-pathogen interactions and genome evolution in two
RT generalist and specialist microsporidian pathogens of mosquitoes.";
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 -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03133}.
CC Cytoplasm {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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EJW04980.1}.
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DR EMBL; AFBI03000001; EJW04980.1; -; Genomic_DNA.
DR AlphaFoldDB; J9DQX9; -.
DR STRING; 1003232.J9DQX9; -.
DR VEuPathDB; MicrosporidiaDB:EDEG_00097; -.
DR HOGENOM; CLU_004485_5_0_1; -.
DR InParanoid; J9DQX9; -.
DR OMA; LTCLEIW; -.
DR OrthoDB; 3639120at2759; -.
DR Proteomes; UP000003163; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; 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:0070143; P:mitochondrial alanyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
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; 4.
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}; Cytoplasm {ECO:0000256|HAMAP-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 Mitochondrion {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:UP000003163};
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..948
FT /note="Alanyl-transfer RNA synthetases family profile"
FT /evidence="ECO:0000259|PROSITE:PS50860"
FT BINDING 795
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03133"
FT BINDING 799
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03133"
FT BINDING 905
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03133"
FT BINDING 909
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03133"
SQ SEQUENCE 1149 AA; 131397 MW; 7CA4199A8BC3CCA6 CRC64;
MKAEELTKLF LDYFTSRNHL EKPSSSVVPH DDDTLLFVNS GMVQFKKNFC LTKNELQKID
KEVCTVQHCI RAGGKHNDLD DVGKDGYHHT YFQMLGNWSF GSYFKREAIY FAYDFLVNIL
KLDKKRLYVT VFDSSCDSTK SLNFVDLETE SIWKNYFGED RILRFGSKDN FWEMGDSGPC
GPCTEIHYDQ RENVCEGGVN GADLVNKDHP EVIEIWNVVF IEYYRNESGD LTTLPVKSVD
TGMGLERVLR IVNNVRSNYL TSGFMDLIQD IIIKSTYNQN KGRDTLKNIG SKDSDLNRNI
EKMSISESKN KKSSSAVNDS TENKELSRII KSDSVNVCIN AEIDSKLYSN DIVSFATCDH
ENANTPENLI YYDCYNKNCK NFHYSMSCRV LADHARALAI CIFYDCEFSS IGRGYVIRRI
LRRAIRFCNE IGIINKFHLI VKKASETLGI NVYEKLYLIE NEEKLFLKTL ENGKKMFNTL
ISQHQNVNKK NKINDNCENK KINGQRNGID NIYASNTDND NNVSDIGEKK IISGKDAFVL
YDTYGFPIDL TLLMAEEKGF TVDIDEFNKI QAIYKIKSKK AKSKDLVFDM NCIKHISKFE
TTQDDLKYTA HHSAADVLCV FKNNNVIYEY NVGNNHENSV RNFVDNVTKC GDLAKDDFDI
VKQFFPGTEN IESYRSKIQE ETFIEDKEDV YAILLDQTCF YAESGGQIGD SGSLVLFNKN
SFAGKSMNST RNNPNVGIRF DVFDTQKYNG YVIHFCRLPR KTNLDVYMPT YKNKNTLKAC
VHIDQERREK IKLNHTATHI LNTVLRNVLK DSKVKVEQRG SLVTDTKLRF DFSSTNITLK
QIKEIEDQCN SIIENSRIVK TEHVNLNDFL CESKKENTNL IYLPGEKYPE KIRVVSIEGI
SSEPCGGTHA THTSLIRKMR IISETSISAN TRRIVAVTND EAFAAEENAR KNNLDADIPL
LERHRIINEQ KEINKQALKS HKILLKKYET QIKSLISLIL DDKIGEYSSN HFPKKQPTDQ
FEKLNPIEEL QFLYFGQQIF SNYQSREISH FIAFLINLNK KNNQALSNIV FFFVSLNNKK
TITKDLNTLA VNFDNSKING CVISILDTTV FYSFKGKSAT LVAQILTSNL KDASFGGVVG
TATGYGTFE
//
