ID D0N2D2_PHYIT Unreviewed; 897 AA.
AC D0N2D2;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 27-MAR-2024, entry version 76.
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 ORFNames=PITG_04918 {ECO:0000313|EMBL:EEY68461.1};
OS Phytophthora infestans (strain T30-4) (Potato late blight agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=403677 {ECO:0000313|EMBL:EEY68461.1, ECO:0000313|Proteomes:UP000006643};
RN [1] {ECO:0000313|Proteomes:UP000006643}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T30-4 {ECO:0000313|Proteomes:UP000006643};
RX PubMed=19741609; DOI=10.1038/nature08358;
RG The Broad Institute Genome Sequencing Platform;
RA Haas B.J., Kamoun S., Zody M.C., Jiang R.H., Handsaker R.E., Cano L.M.,
RA Grabherr M., Kodira C.D., Raffaele S., Torto-Alalibo T., Bozkurt T.O.,
RA Ah-Fong A.M., Alvarado L., Anderson V.L., Armstrong M.R., Avrova A.,
RA Baxter L., Beynon J., Boevink P.C., Bollmann S.R., Bos J.I., Bulone V.,
RA Cai G., Cakir C., Carrington J.C., Chawner M., Conti L., Costanzo S.,
RA Ewan R., Fahlgren N., Fischbach M.A., Fugelstad J., Gilroy E.M., Gnerre S.,
RA Green P.J., Grenville-Briggs L.J., Griffith J., Grunwald N.J., Horn K.,
RA Horner N.R., Hu C.H., Huitema E., Jeong D.H., Jones A.M., Jones J.D.,
RA Jones R.W., Karlsson E.K., Kunjeti S.G., Lamour K., Liu Z., Ma L.,
RA Maclean D., Chibucos M.C., McDonald H., McWalters J., Meijer H.J.,
RA Morgan W., Morris P.F., Munro C.A., O'Neill K., Ospina-Giraldo M.,
RA Pinzon A., Pritchard L., Ramsahoye B., Ren Q., Restrepo S., Roy S.,
RA Sadanandom A., Savidor A., Schornack S., Schwartz D.C., Schumann U.D.,
RA Schwessinger B., Seyer L., Sharpe T., Silvar C., Song J., Studholme D.J.,
RA Sykes S., Thines M., van de Vondervoort P.J., Phuntumart V., Wawra S.,
RA Weide R., Win J., Young C., Zhou S., Fry W., Meyers B.C., van West P.,
RA Ristaino J., Govers F., Birch P.R., Whisson S.C., Judelson H.S.,
RA Nusbaum C.;
RT "Genome sequence and analysis of the Irish potato famine pathogen
RT Phytophthora infestans.";
RL Nature 461:393-398(2009).
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}.
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DR EMBL; DS028123; EEY68461.1; -; Genomic_DNA.
DR RefSeq; XP_002905620.1; XM_002905574.1.
DR AlphaFoldDB; D0N2D2; -.
DR STRING; 403677.D0N2D2; -.
DR EnsemblProtists; PITG_04918T0; PITG_04918T0; PITG_04918.
DR GeneID; 9478825; -.
DR KEGG; pif:PITG_04918; -.
DR VEuPathDB; FungiDB:PITG_04918; -.
DR eggNOG; KOG0188; Eukaryota.
DR HOGENOM; CLU_004485_1_1_1; -.
DR InParanoid; D0N2D2; -.
DR OMA; HVFVQLM; -.
DR OrthoDB; 3639120at2759; -.
DR Proteomes; UP000006643; Partially assembled 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; 3.10.310.40; -; 1.
DR Gene3D; 3.30.54.20; -; 1.
DR Gene3D; 6.10.250.550; -; 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 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; 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; 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:UP000006643};
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 22..736
FT /note="Alanyl-transfer RNA synthetases family profile"
FT /evidence="ECO:0000259|PROSITE:PS50860"
FT REGION 457..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 586
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03133"
FT BINDING 590
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03133"
FT BINDING 693
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03133"
FT BINDING 697
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03133"
SQ SEQUENCE 897 AA; 97524 MW; 1B3CF2F62FDA9C7B CRC64;
MLRLRGSAGV RRSSAVRNMH SLPSTELRSR FLQFFESQGH RVVPSASLVP PGGDQSLLFV
NAGMVPFKQA FLGIDGGAKA RGYSRATSAQ RCVRAGGKHN DLDQVGLTRR HHTMFEMLGN
FSFGDYFKEQ AITMCWRFLT QELELPIDRL HVTVLKSDQE ARRLWKQIAG LPDHKIQELD
EHDNFWAMGD SGPCGPCSEV FWDLGDHIAD PDERFLELWN LVFMQFFRNE GDSELHALPN
CSVDTGMGLE RVASVLQGVP SNYHTDVFVP LLTEVATVLD ANRSSTLRQS FTSALQEELD
PRKNLFGTGK EIQTLRIVSD HLRATYALLQ DGVFPSNIGR GYVLRRIIRR AIRHAQQLGV
RSGSDGILAS IAVPGWSEAA GLQQMRAIVA NEERAFEEML RNGRGAIEKA FSKTQVMLSG
ADAFRLYDTF GIPLDITQVL AEEKGLSVDT EGYDACRKSH KQQTSDRSVF HTQASSEQSS
STPAATVVSE FVGYEQLSVS KARVLDCWSG SGSAGFSVIL DRCPFYPEGG GQVGDRGHLI
NEDAIAIKCT LPKDTTFEDI SALFLNEATV EAHVDRRFRS GCAVHHTATH LLQRALKAEL
GEHVTQAGSQ VTSDRLRFDF AHFGALSADE MASVEARVNA FAAAELDVST VELPREDAER
SGAICNFGDK YGDVVRVVRV GGEAETPVSS EFCGGTHVNN VREIFPFAMV SEGSVAAGTR
RVEAVAGHAG ARYLQAKAQT LSDVADQLST TPAKVVERVA KMHKQMKQLE SRVQALGDVL
STLPSTPLAS GAIDGAITAP HVELHALNVP GGGEFSKVLK RRAEFLAEQA SPSSVLVVLL
GCQIACIANA EAKVHAGKLM QQVVKSLGGR GGGNASFAQG SVPADLTPQE IARRVLR
//
