ID A0A0S9MYG7_9BURK Unreviewed; 247 AA.
AC A0A0S9MYG7;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Ala-tRNA(Pro) hydrolase {ECO:0000313|EMBL:KQP38088.1};
GN ORFNames=ASF44_12805 {ECO:0000313|EMBL:KQP38088.1};
OS Pseudorhodoferax sp. Leaf274.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae.
OX NCBI_TaxID=1736318 {ECO:0000313|EMBL:KQP38088.1, ECO:0000313|Proteomes:UP000051759};
RN [1] {ECO:0000313|EMBL:KQP38088.1, ECO:0000313|Proteomes:UP000051759}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf274 {ECO:0000313|EMBL:KQP38088.1,
RC ECO:0000313|Proteomes:UP000051759};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQP38088.1, ECO:0000313|Proteomes:UP000051759}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf274 {ECO:0000313|EMBL:KQP38088.1,
RC ECO:0000313|Proteomes:UP000051759};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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:KQP38088.1}.
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DR EMBL; LMNA01000026; KQP38088.1; -; Genomic_DNA.
DR RefSeq; WP_056901390.1; NZ_LMNA01000026.1.
DR AlphaFoldDB; A0A0S9MYG7; -.
DR STRING; 1736318.ASF44_12805; -.
DR OrthoDB; 9812949at2; -.
DR Proteomes; UP000051759; Unassembled WGS sequence.
DR GO; GO:0004813; F:alanine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR012947; tRNA_SAD.
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; 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:KQP38088.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000051759};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 1..247
FT /note="Alanyl-transfer RNA synthetases family profile"
FT /evidence="ECO:0000259|PROSITE:PS50860"
SQ SEQUENCE 247 AA; 25831 MW; B27770385E7A9056 CRC64;
MTQDLFRQDA RLRQASATIL SAGPEGIVLD RTVFYPLGGG QAGDTGWLVL ADGQRLGVAD
TRKGKDAEGR PTAAICHVPA PGQDALLARC TAGTPVTAEI DWERRHRLMR FHTTTHLLCH
LVAQPVNGCA ITADAARLDF HTDQPLDKAL LSAGIARLVG AALPVTVGEI AEAELDANPS
LVKSMSVSPP RGTGAVRTIR IGADGLIDLQ PCGGTHVANT AEIGAVVVTK IEKKGAMARR
VVLGFAA
//