ID A4YIR8_METS5 Unreviewed; 235 AA.
AC A4YIR8;
DT 29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2007, sequence version 1.
DT 24-JAN-2024, entry version 72.
DE SubName: Full=Ala-tRNA(Pro) hydrolase {ECO:0000313|EMBL:ABP96320.1};
DE EC=3.1.1.- {ECO:0000313|EMBL:ABP96320.1};
GN OrderedLocusNames=Msed_2181 {ECO:0000313|EMBL:ABP96320.1};
OS Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509
OS / TH2).
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Metallosphaera.
OX NCBI_TaxID=399549 {ECO:0000313|EMBL:ABP96320.1, ECO:0000313|Proteomes:UP000000242};
RN [1] {ECO:0000313|EMBL:ABP96320.1, ECO:0000313|Proteomes:UP000000242}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2
RC {ECO:0000313|Proteomes:UP000000242};
RX PubMed=18083856; DOI=10.1128/AEM.02019-07;
RA Auernik K.S., Maezato Y., Blum P.H., Kelly R.M.;
RT "The genome sequence of the metal-mobilizing, extremely thermoacidophilic
RT archaeon Metallosphaera sedula provides insights into bioleaching-
RT associated metabolism.";
RL Appl. Environ. Microbiol. 74:682-692(2008).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; CP000682; ABP96320.1; -; Genomic_DNA.
DR AlphaFoldDB; A4YIR8; -.
DR STRING; 399549.Msed_2181; -.
DR KEGG; mse:Msed_2181; -.
DR eggNOG; arCOG01254; Archaea.
DR HOGENOM; CLU_004485_3_2_2; -.
DR OMA; LMRLHTA; -.
DR Proteomes; UP000000242; Chromosome.
DR GO; GO:0004813; F:alanine-tRNA ligase activity; IEA:InterPro.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006419; P:alanyl-tRNA aminoacylation; IEA:InterPro.
DR Gene3D; 2.40.30.130; -; 1.
DR InterPro; IPR018165; Ala-tRNA-synth_IIc_core.
DR InterPro; IPR018164; Ala-tRNA-synth_IIc_N.
DR InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR012947; tRNA_SAD.
DR NCBIfam; NF040865; a_tRNA_ed_AlaXM; 1.
DR PANTHER; PTHR43462; ALANYL-TRNA EDITING PROTEIN; 1.
DR PANTHER; PTHR43462:SF2; THREONYL AND ALANYL TRNA SYNTHETASE SECOND ADDITIONAL DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01411; tRNA-synt_2c; 1.
DR Pfam; PF07973; tRNA_SAD; 1.
DR SMART; SM00863; tRNA_SAD; 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 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:ABP96320.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000000242};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 1..235
FT /note="Alanyl-transfer RNA synthetases family profile"
FT /evidence="ECO:0000259|PROSITE:PS50860"
SQ SEQUENCE 235 AA; 26427 MW; 087578BBD15ADBDA CRC64;
MVTEELYAKD SYIKNFSAKV TKIVPSGVIL DRTAFHPRGG GLESDTGALI LGGNTYRVTE
VKFEGNEIVH VLEKLDGLRE GDEVEGRIDW ERRYRMMRLH TASHIIASIA FSKYNALITG
GNITPEYAKD DFNVENKDLL PKIVEEANEI AKRGIKVKVY FLPREEAMKI PGVVKLAEKM
PPELETWRIV EIEGIDIQAD GGPHVSNTEE IGSIEVIKVE NRGKGKKRLY YTVKP
//