ID W2R1T8_PHYPN Unreviewed; 922 AA.
AC W2R1T8;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
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=PPTG_04650 {ECO:0000313|EMBL:ETN19293.1};
OS Phytophthora parasitica (strain INRA-310).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=761204 {ECO:0000313|EMBL:ETN19293.1, ECO:0000313|Proteomes:UP000018817};
RN [1] {ECO:0000313|Proteomes:UP000018817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=INRA-310 {ECO:0000313|Proteomes:UP000018817};
RG The Broad Institute Genome Sequencing Platform;
RA Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA Machado M., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Chapman S.B.,
RA Gearin G., Goldberg J., Griggs A., Gujja S., Hansen M., Heiman D.,
RA Howarth C., Larimer J., Lui A., MacDonald P.J.P., McCowen C.,
RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ETN19293.1, ECO:0000313|Proteomes:UP000018817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=INRA-310 {ECO:0000313|EMBL:ETN19293.1,
RC ECO:0000313|Proteomes:UP000018817};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Phytophthora parasitica INRA-310.";
RL Submitted (NOV-2013) 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}.
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DR EMBL; KI669565; ETN19293.1; -; Genomic_DNA.
DR RefSeq; XP_008895154.1; XM_008896906.1.
DR AlphaFoldDB; W2R1T8; -.
DR STRING; 761204.W2R1T8; -.
DR EnsemblProtists; ETN19293; ETN19293; PPTG_04650.
DR GeneID; 20174733; -.
DR VEuPathDB; FungiDB:PPTG_04650; -.
DR OMA; HVFVQLM; -.
DR OrthoDB; 3639120at2759; -.
DR Proteomes; UP000018817; 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 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:UP000018817};
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 21..760
FT /note="Alanyl-transfer RNA synthetases family profile"
FT /evidence="ECO:0000259|PROSITE:PS50860"
FT REGION 463..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 611
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03133"
FT BINDING 615
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03133"
FT BINDING 717
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03133"
FT BINDING 721
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03133"
SQ SEQUENCE 922 AA; 99988 MW; 92409513CAEAAE56 CRC64;
MLRLRRCAGA RRSAVRGLHS LPSTELRSRF LQFFKTQGHR IVPSASLVPP GGDQSLLFVN
AGMVPFKQAF LGLDGGAEAR GYSRATSAQR CVRAGGKHND LDQVGLTRRH HTMFEMLGNF
SFGDYFKEQA IAMCWRFLTQ ELGLPVDRLH VTVLKSDQEA RRLWKQIAGL PDHKILELDE
HDNFWAMGDS GPCGPCSEVF WDLGDHIADP DERFLELWNL VFMQFFRNEG DSELHPLPNC
SVDTGMGLER VASVLQGVPS NYHTDIFVPL LTEVASVLDV NRSSTSRQSF TSALQEELDP
SKNLFGTGKE IQTLRIVSDH LRATYALLHD GVFPSNIGRG YVLRRIIRRA IRHAQQLGVK
GGSDGILASI AVPGWTETAG FQQMRAIVSN EERAFEEMLR NGRGAIEKAF SKTHTVLSGA
DAFRLYDTYG IPLDITQVLA EEKGLSVDIE GYDSCMKSHK QQTSDRSAFA GHNTQPSSEQ
SSAPAATVVS EFVGYDQLSV SKARVLDSWS GPGSNGFSVI LDRCPFYPEG GGQVGDRGHL
IFTSEGSLKH LTIPVENTTK LNEDAIAVKC SLPKDTTFED ITALFVRDDG LKPTVEAHVD
RKLRSSCAVH HTATHLLQRA LKAELGEHVT QAGSQVTSDR LRFDFAHFGA LSPDEMASVE
ARVNAFAAAE LDVTTVELPR EEAERSGAIC NFGDKYGDVV RVVRVGAAEA PLTSEFCGGT
HVQNVREVFP FALVSEGSVA AGTRRVEAVA GAAGARYLQA KAQTLSEVAD QLSTTPAKVV
ERVRKMHKQV KQLESRVQAL GDVLAALPST PLASGSIDGA ISVPQVELHA LDVPGGGEFS
KVLKRRAEFL AEQASPNSVL LVLVGSQVAC IANSEAKVHA GKLLQQVVKP LGGRGGGNAS
FAQGSVPADL TPQEIANRVL SV
//
