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Database: UniProt
Entry: A0A5N6F290_9EURO
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ID   A0A5N6F290_9EURO        Unreviewed;       162 AA.
AC   A0A5N6F290;
DT   22-APR-2020, integrated into UniProtKB/TrEMBL.
DT   22-APR-2020, sequence version 1.
DT   27-MAR-2024, entry version 9.
DE   RecName: Full=tRNA(adenine(34)) deaminase {ECO:0000256|ARBA:ARBA00012740};
DE            EC=3.5.4.33 {ECO:0000256|ARBA:ARBA00012740};
GN   ORFNames=BDV33DRAFT_201022 {ECO:0000313|EMBL:KAB8222884.1};
OS   Aspergillus novoparasiticus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=986946 {ECO:0000313|EMBL:KAB8222884.1, ECO:0000313|Proteomes:UP000326799};
RN   [1] {ECO:0000313|EMBL:KAB8222884.1, ECO:0000313|Proteomes:UP000326799}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 126849 {ECO:0000313|EMBL:KAB8222884.1,
RC   ECO:0000313|Proteomes:UP000326799};
RG   DOE Joint Genome Institute;
RA   Kjaerbolling I., Vesth T.C., Frisvad J.C., Nybo J.L., Theobald S.,
RA   Kildgaard S., Petersen T.I., Kuo A., Sato A., Lyhne E.K., Kogle M.E.,
RA   Wiebenga A., Kun R.S., Lubbers R.J., Makela M.R., Barry K., Chovatia M.,
RA   Clum A., Daum C., Haridas S., He G., LaButti K., Lipzen A., Mondo S.,
RA   Pangilinan J., Riley R., Salamov A., Simmons B.A., Magnuson J.K.,
RA   Henrissat B., Mortensen U.H., Larsen T.O., De vries R.P., Grigoriev I.V.,
RA   Machida M., Baker S.E., Andersen M.R.;
RT   "Fungal friends and foes A comparative genomics study of 23 Aspergillus
RT   species from section Flavi.";
RL   Submitted (APR-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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
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DR   EMBL; ML733409; KAB8222884.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5N6F290; -.
DR   Proteomes; UP000326799; Unassembled WGS sequence.
DR   GO; GO:0008251; F:tRNA-specific adenosine deaminase activity; IEA:InterPro.
DR   GO; GO:0002100; P:tRNA wobble adenosine to inosine editing; IEA:InterPro.
DR   CDD; cd01285; nucleoside_deaminase; 1.
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:SF179; CYTOSINE DEAMINASE; 1.
DR   PANTHER; PTHR11079; CYTOSINE DEAMINASE FAMILY MEMBER; 1.
DR   Pfam; PF14437; MafB19-deam; 1.
DR   SUPFAM; SSF53927; Cytidine deaminase-like; 1.
DR   PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000326799};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT   DOMAIN          4..114
FT                   /note="CMP/dCMP-type deaminase"
FT                   /evidence="ECO:0000259|PROSITE:PS51747"
FT   REGION          143..162
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   162 AA;  17484 MW;  F98B32BE187E39B7 CRC64;
     MVSDSDINYL RRCVDLAREA LEAGDSPFGS VLVDAAGKII NEDRNRTVTE ADVTWHPEFT
     IVKWAQKNLT PTERAAATVY TSGEHCPMCA AAHANAGLGR IVYASSTAQF VQWRTEMGIK
     PGPVAPLSIN QVAPDLLVDG PAPGLDEEVR GLHQEKQARS VS
//
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