ID B4NWF5_DROYA Unreviewed; 158 AA. AC B4NWF5; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 31-JAN-2018, entry version 52. 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 Name=Dyak\GE18745 {ECO:0000313|EMBL:EDW88472.1}; GN ORFNames=Dyak_GE18745 {ECO:0000313|EMBL:EDW88472.1}, GE18745 GN {ECO:0000313|FlyBase:FBgn0236137}; OS Drosophila yakuba (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7245 {ECO:0000313|EMBL:EDW88472.1, ECO:0000313|Proteomes:UP000002282}; RN [1] {ECO:0000313|EMBL:EDW88472.1, ECO:0000313|Proteomes:UP000002282} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tai18E2 / Tucson 14021-0261.01 RC {ECO:0000313|Proteomes:UP000002282}; RX PubMed=17994087; DOI=10.1038/nature06341; RG Drosophila 12 Genomes Consortium; RA Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., RA Markow T.A., Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., RA Pollard D.A., Sackton T.B., Larracuente A.M., Singh N.D., Abad J.P., RA Abt D.N., Adryan B., Aguade M., Akashi H., Anderson W.W., RA Aquadro C.F., Ardell D.H., Arguello R., Artieri C.G., Barbash D.A., RA Barker D., Barsanti P., Batterham P., Batzoglou S., Begun D., RA Bhutkar A., Blanco E., Bosak S.A., Bradley R.K., Brand A.D., RA Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C., RA Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S., RA Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A., RA Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., RA Daub J., David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., RA Edwards K., Eickbush T., Evans J.D., Filipski A., Findeiss S., RA Freyhult E., Fulton L., Fulton R., Garcia A.C., Gardiner A., RA Garfield D.A., Garvin B.E., Gibson G., Gilbert D., Gnerre S., RA Godfrey J., Good R., Gotea V., Gravely B., Greenberg A.J., RA Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A., Haerty W., RA Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V., RA Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., RA Hubisz M.J., Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., RA Jeck W.R., Johnson J., Jones C.D., Jordan W.C., Karpen G.H., RA Kataoka E., Keightley P.D., Kheradpour P., Kirkness E.F., RA Koerich L.B., Kristiansen K., Kudrna D., Kulathinal R.J., Kumar S., RA Kwok R., Lander E., Langley C.H., Lapoint R., Lazzaro B.P., Lee S.J., RA Levesque L., Li R., Lin C.F., Lin M.F., Lindblad-Toh K., Llopart A., RA Long M., Low L., Lozovsky E., Lu J., Luo M., Machado C.A., RA Makalowski W., Marzo M., Matsuda M., Matzkin L., McAllister B., RA McBride C.S., McKernan B., McKernan K., Mendez-Lago M., Minx P., RA Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E., Negre B., RA Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L., RA Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., RA Pesole G., Phillippy A.M., Ponting C.P., Pop M., Porcelli D., RA Powell J.R., Prohaska S., Pruitt K., Puig M., Quesneville H., RA Ram K.R., Rand D., Rasmussen M.D., Reed L.K., Reenan R., Reily A., RA Remington K.A., Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., RA Rohde C., Rozas J., Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., RA Sanchez-Gracia A., Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., RA Schlenke T., Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., RA Sisneros N.B., Smith C.D., Smith T.F., Spieth J., Stage D.E., RA Stark A., Stephan W., Strausberg R.L., Strempel S., Sturgill D., RA Sutton G., Sutton G.G., Tao W., Teichmann S., Tobari Y.N., RA Tomimura Y., Tsolas J.M., Valente V.L., Venter E., Venter J.C., RA Vicario S., Vieira F.G., Vilella A.J., Villasante A., Walenz B., RA Wang J., Wasserman M., Watts T., Wilson D., Wilson R.K., Wing R.A., RA Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G., Yamamoto D., RA Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E., Zhang P., RA Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J., RA Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., RA An P., Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., RA Barry A., Bayul T., Berlin A., Bessette D., Bloom T., Blye J., RA Boguslavskiy L., Bonnet C., Boukhgalter B., Bourzgui I., Brown A., RA Cahill P., Channer S., Cheshatsang Y., Chuda L., Citroen M., RA Collymore A., Cooke P., Costello M., D'Aco K., Daza R., De Haan G., RA DeGray S., DeMaso C., Dhargay N., Dooley K., Dooley E., Doricent M., RA Dorje P., Dorjee K., Dupes A., Elong R., Falk J., Farina A., Faro S., RA Ferguson D., Fisher S., Foley C.D., Franke A., Friedrich D., RA Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T., RA Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B., RA Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L., RA Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D., RA Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., RA LeVine R., Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., RA Lokyitsang Y., Lubonja R., Lui A., MacDonald P., Magnisalis V., RA Maru K., Matthews C., McCusker W., McDonough S., Mehta T., Meldrim J., RA Meneus L., Mihai O., Mihalev A., Mihova T., Mittelman R., Mlenga V., RA Montmayeur A., Mulrain L., Navidi A., Naylor J., Negash T., Nguyen T., RA Nguyen N., Nicol R., Norbu C., Norbu N., Novod N., O'Neill B., RA Osman S., Markiewicz E., Oyono O.L., Patti C., Phunkhang P., RA Pierre F., Priest M., Raghuraman S., Rege F., Reyes R., Rise C., RA Rogov P., Ross K., Ryan E., Settipalli S., Shea T., Sherpa N., Shi L., RA Shih D., Sparrow T., Spaulding J., Stalker J., Stange-Thomann N., RA Stavropoulos S., Stone C., Strader C., Tesfaye S., Thomson T., RA Thoulutsang Y., Thoulutsang D., Topham K., Topping I., Tsamla T., RA Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J., RA Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D., Zimmer A., RA Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J., Chin C., RA Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.; RT "Evolution of genes and genomes on the Drosophila phylogeny."; RL Nature 450:203-218(2007). RN [2] {ECO:0000313|EMBL:EDW88472.1, ECO:0000313|Proteomes:UP000002282} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tai18E2 / Tucson 14021-0261.01 RC {ECO:0000313|Proteomes:UP000002282}; RX PubMed=17550304; DOI=10.1371/journal.pbio.0050152; RA Ranz J.M., Maurin D., Chan Y.S., von Grotthuss M., Hillier L.W., RA Roote J., Ashburner M., Bergman C.M.; RT "Principles of genome evolution in the Drosophila melanogaster species RT group."; RL PLoS Biol. 5:E152-E152(2007). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CM000157; EDW88472.1; -; Genomic_DNA. DR RefSeq; XP_002088760.1; XM_002088724.2. DR ProteinModelPortal; B4NWF5; -. DR STRING; 7245.FBpp0263755; -. DR EnsemblMetazoa; FBtr0265263; FBpp0263755; FBgn0236137. DR GeneID; 6527674; -. DR KEGG; dya:Dyak_GE18745; -. DR FlyBase; FBgn0236137; Dyak\GE18745. DR eggNOG; KOG0833; Eukaryota. DR eggNOG; COG0295; LUCA. DR KO; K01489; -. DR OMA; NQENASY; -. DR OrthoDB; EOG091G09D3; -. DR PhylomeDB; B4NWF5; -. DR Proteomes; UP000002282; Chromosome 2L. DR Bgee; FBgn0236137; -. DR GO; GO:0004126; F:cytidine deaminase activity; IEA:UniProtKB-UniRule. DR GO; GO:0042802; F:identical protein binding; IEA:EnsemblMetazoa. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. 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; PS51747; CYT_DCMP_DEAMINASES_2; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002282}; KW Hydrolase {ECO:0000256|RuleBase:RU364006, KW ECO:0000313|EMBL:EDW88472.1}; KW Metal-binding {ECO:0000256|RuleBase:RU364006}; KW Zinc {ECO:0000256|RuleBase:RU364006}. FT DOMAIN 23 140 CMP/dCMP-type deaminase. FT {ECO:0000259|PROSITE:PS51747}. SQ SEQUENCE 158 AA; 17029 MW; 34160E1F61F301A9 CRC64; MTQVFINGAR DDLNVREFQS LDPSIQELIL AATEARKQAY CPYSNFAVGA ALRTSDGTIY SGCNIENGAY ATCICAERTA AVKAISEGKR DFVACAVVAQ QDNGFTTPCG VCRQFLSEFV NGKDIPLYAA KPTNLPLRVL CTSVLQLLPN GFSFTNGK //