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Database: UniProt
Entry: R0KUM7_NOSB1
LinkDB: R0KUM7_NOSB1
Original site: R0KUM7_NOSB1 
ID   R0KUM7_NOSB1            Unreviewed;       151 AA.
AC   R0KUM7;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   08-NOV-2023, entry version 24.
DE   SubName: Full=tRNA-specific adenosine deaminase 2 {ECO:0000313|EMBL:EOB14561.1};
GN   Name=ADAT2 {ECO:0000313|EMBL:EOB14561.1};
GN   ORFNames=NBO_24g0007 {ECO:0000313|EMBL:EOB14561.1};
OS   Nosema bombycis (strain CQ1 / CVCC 102059) (Microsporidian parasite)
OS   (Pebrine of silkworm).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Nosematidae; Nosema.
OX   NCBI_TaxID=578461 {ECO:0000313|EMBL:EOB14561.1, ECO:0000313|Proteomes:UP000016927};
RN   [1] {ECO:0000313|EMBL:EOB14561.1, ECO:0000313|Proteomes:UP000016927}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CQ1 / CVCC 102059 {ECO:0000313|Proteomes:UP000016927};
RX   PubMed=23496955; DOI=10.1186/1471-2164-14-186;
RA   Pan G., Xu J., Li T., Xia Q., Liu S.L., Zhang G., Li S., Li C., Liu H.,
RA   Yang L., Liu T., Zhang X., Wu Z., Fan W., Dang X., Xiang H., Tao M., Li Y.,
RA   Hu J., Li Z., Lin L., Luo J., Geng L., Wang L., Long M., Wan Y., He N.,
RA   Zhang Z., Lu C., Keeling P.J., Wang J., Xiang Z., Zhou Z.;
RT   "Comparative genomics of parasitic silkworm microsporidia reveal an
RT   association between genome expansion and host adaptation.";
RL   BMC Genomics 14:186-186(2013).
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DR   EMBL; KB908932; EOB14561.1; -; Genomic_DNA.
DR   AlphaFoldDB; R0KUM7; -.
DR   STRING; 578461.R0KUM7; -.
DR   EnsemblFungi; EOB14561; EOB14561; NBO_24g0007.
DR   VEuPathDB; MicrosporidiaDB:NBO_24g0007; -.
DR   HOGENOM; CLU_025810_8_2_1; -.
DR   OMA; MENEKAP; -.
DR   Proteomes; UP000016927; Unassembled WGS sequence.
DR   GO; GO:0019239; F:deaminase activity; IEA:UniProt.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
DR   InterPro; IPR002125; CMP_dCMP_dom.
DR   InterPro; IPR016193; Cytidine_deaminase-like.
DR   PANTHER; PTHR11079; CYTOSINE DEAMINASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR11079:SF149; TRNA-SPECIFIC ADENOSINE DEAMINASE 2; 1.
DR   Pfam; PF00383; dCMP_cyt_deam_1; 1.
DR   SUPFAM; SSF53927; Cytidine deaminase-like; 1.
DR   PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1.
DR   PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016927};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          1..130
FT                   /note="CMP/dCMP-type deaminase"
FT                   /evidence="ECO:0000259|PROSITE:PS51747"
SQ   SEQUENCE   151 AA;  17594 MW;  9D005B696E839CB2 CRC64;
     MHKFFLEEAY KEAKKALKEQ EVPVGCVIVR NNKILSRSHN LTNKLHDPLA HAEINGLREL
     LQITDDLTFY ITCEPCIMCL GILNRIKARI YYGCKNIIFG GITILETPSD SHFIEDKRCY
     EILQKFYSNE NEFAPEEKRK KKNNRNNCVS L
//
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