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Database: UniProt
Entry: A4YIR8_METS5
LinkDB: A4YIR8_METS5
Original site: A4YIR8_METS5 
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
//
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