(data stored in ACNUC8465 zone)

SWISSPROT: B6H713_PENRW

ID   B6H713_PENRW            Unreviewed;       164 AA.
AC   B6H713;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   07-JUN-2017, entry version 49.
DE   RecName: Full=Cytidine deaminase {ECO:0000256|RuleBase:RU364006};
DE            EC=3.5.4.5 {ECO:0000256|RuleBase:RU364006};
DE   AltName: Full=Cytidine aminohydrolase {ECO:0000256|RuleBase:RU364006};
GN   ORFNames=Pc16g01040 {ECO:0000313|EMBL:CAP92774.1}, PCH_Pc16g01040
GN   {ECO:0000313|EMBL:CAP92774.1};
OS   Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 /
OS   Wisconsin 54-1255) (Penicillium chrysogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=500485 {ECO:0000313|EMBL:CAP92774.1, ECO:0000313|Proteomes:UP000000724};
RN   [1] {ECO:0000313|EMBL:CAP92774.1, ECO:0000313|Proteomes:UP000000724}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255
RC   {ECO:0000313|Proteomes:UP000000724};
RX   PubMed=18820685; DOI=10.1038/nbt.1498;
RA   van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA   Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA   Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA   Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A.,
RA   van der Klei I.J., van Peij N.N.M.E., Veenhuis M., von Doehren H.,
RA   Wagner C., Wortman J.R., Bovenberg R.A.L.;
RT   "Genome sequencing and analysis of the filamentous fungus Penicillium
RT   chrysogenum.";
RL   Nat. Biotechnol. 26:1161-1168(2008).
CC   -!- FUNCTION: This enzyme scavenges exogenous and endogenous cytidine
CC       and 2'-deoxycytidine for UMP synthesis.
CC       {ECO:0000256|RuleBase:RU364006}.
CC   -!- CATALYTIC ACTIVITY: 2'deoxycytidine + H(2)O = 2'-deoxyuridine +
CC       NH(3). {ECO:0000256|RuleBase:RU364006}.
CC   -!- CATALYTIC ACTIVITY: Cytidine + H(2)O = uridine + NH(3).
CC       {ECO:0000256|RuleBase:RU364006}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU364006};
CC   -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC       family. {ECO:0000256|RuleBase:RU364006}.
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DR   EMBL; AM920431; CAP92774.1; -; Genomic_DNA.
DR   RefSeq; XP_002560522.1; XM_002560476.1.
DR   ProteinModelPortal; B6H713; -.
DR   STRING; 500485.XP_002560522.1; -.
DR   EnsemblFungi; CAP92774; CAP92774; PCH_Pc16g01040.
DR   GeneID; 8315371; -.
DR   KEGG; pcs:Pc16g01040; -.
DR   eggNOG; KOG0833; Eukaryota.
DR   eggNOG; COG0295; LUCA.
DR   HOGENOM; HOG000014707; -.
DR   KO; K01489; -.
DR   OMA; AVYMTKP; -.
DR   OrthoDB; EOG092C4VW8; -.
DR   BioCyc; PCHR:PC16G01040-MONOMER; -.
DR   Proteomes; UP000000724; Contig Pc00c16.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004126; F:cytidine deaminase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
DR   InterPro; IPR002125; CMP_dCMP_dom.
DR   InterPro; IPR006262; Cyt_deam_tetra.
DR   InterPro; IPR016193; Cytidine_deaminase-like.
DR   Pfam; PF00383; dCMP_cyt_deam_1; 1.
DR   SUPFAM; SSF53927; SSF53927; 1.
DR   TIGRFAMs; TIGR01354; cyt_deam_tetra; 1.
DR   PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1.
DR   PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; B6H713.
DR   SWISS-2DPAGE; B6H713.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000724};
KW   Hydrolase {ECO:0000256|RuleBase:RU364006};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|RuleBase:RU364006};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000724};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|RuleBase:RU364006}.
FT   TRANSMEM    127    146       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN        8    135       CMP/dCMP-type deaminase.
FT                                {ECO:0000259|PROSITE:PS51747}.
SQ   SEQUENCE   164 AA;  17740 MW;  32E6274B3C6F1ED2 CRC64;
     MAHTITAQEL TTLSTKAIDA KATAYCPYSK FRVGACILTA SGEFITGANV ENASYPVGTC
     AERVTIGAAI VAGHRDFKAL AVATDIKPAA SPCGMCRQFI REFTSPSFPV YMYDGEGNHK
     VMTMEEVGFL SFFSFLFGYI SVLYLVDSLL ISPVAPRLFR PQPS
//

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