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Database: UniProt
Entry: A0A1F2ZVZ1_9PROT
LinkDB: A0A1F2ZVZ1_9PROT
Original site: A0A1F2ZVZ1_9PROT 
ID   A0A1F2ZVZ1_9PROT        Unreviewed;       233 AA.
AC   A0A1F2ZVZ1;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Ala-tRNA(Pro) hydrolase {ECO:0000313|EMBL:OFW98124.1};
GN   ORFNames=A3D94_20565 {ECO:0000313|EMBL:OFW98124.1};
OS   Alphaproteobacteria bacterium RIFCSPHIGHO2_12_FULL_66_14.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria.
OX   NCBI_TaxID=1797225 {ECO:0000313|EMBL:OFW98124.1, ECO:0000313|Proteomes:UP000176194};
RN   [1] {ECO:0000313|EMBL:OFW98124.1, ECO:0000313|Proteomes:UP000176194}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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:OFW98124.1}.
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DR   EMBL; MEMN01000193; OFW98124.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F2ZVZ1; -.
DR   STRING; 1797225.A3D94_20565; -.
DR   Proteomes; UP000176194; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004813; F:alanine-tRNA ligase activity; IEA:UniProtKB-EC.
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   PANTHER; PTHR43462; ALANYL-TRNA EDITING PROTEIN; 1.
DR   PANTHER; PTHR43462:SF1; ALANYL-TRNA EDITING PROTEIN AARSD1; 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:OFW98124.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          1..233
FT                   /note="Alanyl-transfer RNA synthetases family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50860"
SQ   SEQUENCE   233 AA;  25504 MW;  277AABDFC3DFBAFD CRC64;
     MVEELFRQDA YLKEADATVT ALEERGVRLD RSLFYPTGGG QPGDAGVLRW DGGEAKIVDA
     VKADGGDVLH VLAADASRPE VGARVRTALD WDRRYLHMRM HTALHVMSAV IKGNVTGGQV
     GADKSRLDFN LEGEVPAKEW VTEEVNRLIA LDRPVTPQWI TDEELAARPE LVKTMSVRPP
     MGAGRVRLLS IEGVDLQACG GTHVARTGEI GRVECIKIEN KGKMNRRFVI ALA
//
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