ID A0A4T0FQ14_9BASI Unreviewed; 413 AA.
AC A0A4T0FQ14;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 24-JAN-2024, entry version 11.
DE RecName: Full=tRNA(adenine(34)) deaminase {ECO:0000256|ARBA:ARBA00012740};
DE EC=3.5.4.33 {ECO:0000256|ARBA:ARBA00012740};
GN ORFNames=E3P99_01529 {ECO:0000313|EMBL:TIA90551.1};
OS Wallemia hederae.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Wallemiomycotina;
OC Wallemiomycetes; Wallemiales; Wallemiaceae; Wallemia.
OX NCBI_TaxID=1540922 {ECO:0000313|EMBL:TIA90551.1, ECO:0000313|Proteomes:UP000310189};
RN [1] {ECO:0000313|EMBL:TIA90551.1, ECO:0000313|Proteomes:UP000310189}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-5753 {ECO:0000313|EMBL:TIA90551.1,
RC ECO:0000313|Proteomes:UP000310189};
RA Gostincar C.;
RT "Sequencing 23 genomes of Wallemia ichthyophaga.";
RL Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine(34) in tRNA + H(+) + H2O = inosine(34) in tRNA +
CC NH4(+); Xref=Rhea:RHEA:43168, Rhea:RHEA-COMP:10373, Rhea:RHEA-
CC COMP:10374, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:74411, ChEBI:CHEBI:82852; EC=3.5.4.33;
CC Evidence={ECO:0000256|ARBA:ARBA00001103};
CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC family. ADAT3 subfamily. {ECO:0000256|ARBA:ARBA00038160}.
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:TIA90551.1}.
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DR EMBL; SPNW01000018; TIA90551.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4T0FQ14; -.
DR Proteomes; UP000310189; Unassembled WGS sequence.
DR GO; GO:0052717; F:tRNA-specific adenosine-34 deaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0002100; P:tRNA wobble adenosine to inosine editing; IEA:InterPro.
DR Gene3D; 3.40.140.10; Cytidine Deaminase, domain 2; 1.
DR InterPro; IPR002125; CMP_dCMP_dom.
DR InterPro; IPR016193; Cytidine_deaminase-like.
DR InterPro; IPR028883; tRNA_aden_deaminase.
DR PANTHER; PTHR11079; CYTOSINE DEAMINASE FAMILY MEMBER; 1.
DR PANTHER; PTHR11079:SF156; INACTIVE TRNA-SPECIFIC ADENOSINE DEAMINASE-LIKE PROTEIN 3-RELATED; 1.
DR Pfam; PF14437; MafB19-deam; 1.
DR SUPFAM; SSF53927; Cytidine deaminase-like; 1.
DR PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000310189};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT DOMAIN 263..393
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000259|PROSITE:PS51747"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 283..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 413 AA; 46026 MW; 3BE5091104C5A188 CRC64;
MTYDSDSPST STHSTNSTKS SNLIPVESLP FERIANVTEQ TCLDDNNEPY LFDAWIVNLT
SPVQTRDLIR FSTHHRLEDK KCERTKHLRR IRKAFPYDKV DCGPNTDTSN LAGLDYCISV
LLAEATPELT KERVRELLAK TSTQVKDLDP YILRVPSRRA TTPEEYTACQ KYWPVSFTPK
AQFVNGFTYD YWDSRKLDWV MNGLDTAKAL AMEAKERGEL PIAAHVSSPP LDIPIPPGYP
PPTPNMTALG YDTRCSSGNP LNHAIFNCVR KVGELRYKAD AETTTMNGSG SNVDKRDSEV
SDSNNSSTTS SSSSTTIQPT LSGINACQNG AEYLCTSLTL FATHEPCMMC AMALVHSRVR
DIYYLRKSKS SGGCGSVYSV HEMQNLNHHF EAWSLDQHHP LCSGLEIDDD ISP
//
