ID   BSD_COCIM               Reviewed;         137 AA.
AC   P0CI02; A0A0E1RVF3; J3K1A6;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 1.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=Blasticidin-S deaminase;
DE            EC=3.5.4.23;
GN   ORFNames=CIMG_08654;
OS   Coccidioides immitis (strain RS) (Valley fever fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=246410;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RS;
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=RS;
RX   PubMed=20516208; DOI=10.1101/gr.103911.109;
RA   Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA   Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA   Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA   FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA   Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA   Taylor J.W., Rounsley S.D.;
RT   "Population genomic sequencing of Coccidioides fungi reveals recent
RT   hybridization and transposon control.";
RL   Genome Res. 20:938-946(2010).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH ZINC IONS, COFACTOR,
RP   AND SUBUNIT.
RG   Seattle structural genomics center for infectious disease (SSGCID);
RT   "Crystal structure of blasticidin S deaminase from Coccidioides immitis.";
RL   Submitted (SEP-2010) to the PDB data bank.
CC   -!- FUNCTION: Catalyzes the deamination of the cytosine moiety of the
CC       antibiotics blasticidin S, cytomycin and acetylblasticidin S.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=blasticidin S + H(+) + H2O = deaminohydroxyblasticidin S +
CC         NH4(+); Xref=Rhea:RHEA:10148, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:57289, ChEBI:CHEBI:57697; EC=3.5.4.23;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|Ref.3};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|Ref.3}.
CC   -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC       family. {ECO:0000305}.
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DR   EMBL; GG704913; EAS29908.1; -; Genomic_DNA.
DR   RefSeq; XP_001241491.1; XM_001241490.2.
DR   PDB; 3OJ6; X-ray; 1.70 A; A/B/C/D=1-137.
DR   PDBsum; 3OJ6; -.
DR   AlphaFoldDB; P0CI02; -.
DR   SMR; P0CI02; -.
DR   EnsemblFungi; EAS29908; EAS29908; CIMG_08654.
DR   GeneID; 4559970; -.
DR   KEGG; cim:CIMG_08654; -.
DR   VEuPathDB; FungiDB:CIMG_08654; -.
DR   InParanoid; P0CI02; -.
DR   OMA; RYRNDWQ; -.
DR   OrthoDB; 1400471at2759; -.
DR   Proteomes; UP000001261; Unassembled WGS sequence.
DR   GO; GO:0047711; F:blasticidin-S deaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006139; P:nucleobase-containing compound metabolic process; IEA:UniProt.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
DR   InterPro; IPR002125; CMP_dCMP_dom.
DR   InterPro; IPR016193; Cytidine_deaminase-like.
DR   Pfam; PF00383; dCMP_cyt_deam_1; 1.
DR   SUPFAM; SSF53927; SSF53927; 1.
DR   PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1.
DR   PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antibiotic resistance; Hydrolase; Metal-binding;
KW   Reference proteome; Zinc.
FT   CHAIN           1..137
FT                   /note="Blasticidin-S deaminase"
FT                   /id="PRO_0000399822"
FT   DOMAIN          1..131
FT                   /note="CMP/dCMP-type deaminase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT   ACT_SITE        59
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         31
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between two homotetrameric
FT                   partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250"
FT   BINDING         57
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT   BINDING         85
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between two homotetrameric
FT                   partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250"
FT   BINDING         91
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT   BINDING         94
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT   BINDING         128
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between two homotetrameric
FT                   partners"
FT                   /evidence="ECO:0000250"
FT   BINDING         130
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between two homotetrameric
FT                   partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250"
FT   HELIX           8..22
FT                   /evidence="ECO:0007829|PDB:3OJ6"
FT   STRAND          28..30
FT                   /evidence="ECO:0007829|PDB:3OJ6"
FT   STRAND          32..38
FT                   /evidence="ECO:0007829|PDB:3OJ6"
FT   STRAND          43..47
FT                   /evidence="ECO:0007829|PDB:3OJ6"
FT   TURN            52..54
FT                   /evidence="ECO:0007829|PDB:3OJ6"
FT   HELIX           58..68
FT                   /evidence="ECO:0007829|PDB:3OJ6"
FT   STRAND          74..81
FT                   /evidence="ECO:0007829|PDB:3OJ6"
FT   TURN            82..85
FT                   /evidence="ECO:0007829|PDB:3OJ6"
FT   STRAND          86..88
FT                   /evidence="ECO:0007829|PDB:3OJ6"
FT   HELIX           92..101
FT                   /evidence="ECO:0007829|PDB:3OJ6"
FT   STRAND          106..109
FT                   /evidence="ECO:0007829|PDB:3OJ6"
FT   STRAND          112..114
FT                   /evidence="ECO:0007829|PDB:3OJ6"
FT   STRAND          116..119
FT                   /evidence="ECO:0007829|PDB:3OJ6"
FT   HELIX           120..123
FT                   /evidence="ECO:0007829|PDB:3OJ6"
FT   STRAND          124..126
FT                   /evidence="ECO:0007829|PDB:3OJ6"
SQ   SEQUENCE   137 AA;  14217 MW;  F23E4F13D06D8EA0 CRC64;
     MAPEPLSAAG QNLIDTATSV INGIPVSDFY SVASAAISDD GRVFSGVNVY HFNGGPCAEL
     VVLGVAAAAG ATKLTHIVAI ANEGRGILSP CGRCRQVLAD LHPGIKAIVI GKEGPKMVAV
     EELLPSIYAW DKDYDRI