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Database: UniProt
Entry: K0KI08_WICCF
LinkDB: K0KI08_WICCF
Original site: K0KI08_WICCF 
ID   K0KI08_WICCF            Unreviewed;       314 AA.
AC   K0KI08;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   SubName: Full=tRNA-specific adenosine deaminase subunit TAD3 {ECO:0000313|EMBL:CCH40768.1};
GN   ORFNames=BN7_302 {ECO:0000313|EMBL:CCH40768.1};
OS   Wickerhamomyces ciferrii (strain ATCC 14091 / BCRC 22168 / CBS 111 / JCM
OS   3599 / NBRC 0793 / NRRL Y-1031 F-60-10) (Yeast) (Pichia ciferrii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Phaffomycetaceae; Wickerhamomyces.
OX   NCBI_TaxID=1206466 {ECO:0000313|EMBL:CCH40768.1, ECO:0000313|Proteomes:UP000009328};
RN   [1] {ECO:0000313|EMBL:CCH40768.1, ECO:0000313|Proteomes:UP000009328}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14091 / BCRC 22168 / CBS 111 / JCM 3599 / NBRC 0793 / NRRL
RC   Y-1031 F-60-10 {ECO:0000313|Proteomes:UP000009328};
RX   PubMed=23193139; DOI=10.1128/EC.00258-12;
RA   Schneider J., Andrea H., Blom J., Jaenicke S., Ruckert C., Schorsch C.,
RA   Szczepanowski R., Farwick M., Goesmann A., Puhler A., Schaffer S.,
RA   Tauch A., Kohler T., Brinkrolf K.;
RT   "Draft genome sequence of Wickerhamomyces ciferrii NRRL Y-1031 F-60-10.";
RL   Eukaryot. Cell 11:1582-1583(2012).
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:CCH40768.1}.
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DR   EMBL; CAIF01000005; CCH40768.1; -; Genomic_DNA.
DR   AlphaFoldDB; K0KI08; -.
DR   STRING; 1206466.K0KI08; -.
DR   eggNOG; KOG2771; Eukaryota.
DR   HOGENOM; CLU_013817_2_0_1; -.
DR   InParanoid; K0KI08; -.
DR   Proteomes; UP000009328; Unassembled WGS sequence.
DR   GO; GO:0016814; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines; IEA:UniProt.
DR   GO; GO:0006139; P:nucleobase-containing compound metabolic process; IEA:UniProt.
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   PANTHER; PTHR11079; CYTOSINE DEAMINASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR11079:SF156; INACTIVE TRNA-SPECIFIC ADENOSINE DEAMINASE-LIKE PROTEIN 3-RELATED; 1.
DR   Pfam; PF00383; dCMP_cyt_deam_1; 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:UP000009328}.
FT   DOMAIN          154..275
FT                   /note="CMP/dCMP-type deaminase"
FT                   /evidence="ECO:0000259|PROSITE:PS51747"
SQ   SEQUENCE   314 AA;  35970 MW;  CD389D13BF0D76F9 CRC64;
     MVKKINNKIK IDYENCILEN SLLQIKNKKN VNNLELIEAW LIDINPIDSP KVLGLIKGLS
     TNDKRSLLHL KRLQRFGEQL TVILCSTDYL EESEILSSLE TQSFTYNNLR TKKVPHHCPG
     TKELSLKWSR EYWPIIWKGN PNDQILNDVK LDINIVKEHL NQIAEESNRT TGETLPIITS
     IVDPNTNEIV AISKDNRASH PLHHSVMRCI DAVSEKEKEK KQKNQNYDTH YLCNGFHVYT
     THEPCSMCSM ALIHSRISRL IYLTASPSTG ALDPESGDGH TIHDHSLLNS SFEVWKWVGS
     DHYRLPSLKE EVNA
//
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