Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Deoxycytidylate deaminase

Gene

SPBC2G2.13c

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Supplies the nucleotide substrate for thymidylate synthetase.By similarity

Catalytic activityi

dCMP + H2O = dUMP + NH3.By similarity

Cofactori

Zn2+By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi246 – 2461Zinc; catalyticBy similarity
Active sitei248 – 2481Proton donorBy similarity
Metal bindingi273 – 2731Zinc; catalyticBy similarity
Metal bindingi276 – 2761Zinc; catalyticBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Nucleotide biosynthesis

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_327756. Pyrimidine biosynthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Deoxycytidylate deaminase (EC:3.5.4.12)
Alternative name(s):
dCMP deaminase
Gene namesi
ORF Names:SPBC2G2.13c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC2G2.13c.
PomBaseiSPBC2G2.13c.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: PomBase
  • cytosol Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 322322Deoxycytidylate deaminasePRO_0000310830Add
BLAST

Proteomic databases

MaxQBiO43012.

Interactioni

Protein-protein interaction databases

BioGridi276867. 72 interactions.
MINTiMINT-4674632.

Structurei

3D structure databases

ProteinModelPortaliO43012.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini173 – 311139CMP/dCMP-type deaminasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the cytidine and deoxycytidylate deaminase family.Sequence Analysis
Contains 1 CMP/dCMP-type deaminase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG2131.
HOGENOMiHOG000217578.
InParanoidiO43012.
KOiK01493.
OMAiRLRPTWD.
OrthoDBiEOG7BCNPR.

Family and domain databases

InterProiIPR016192. APOBEC/CMP_deaminase_Zn-bd.
IPR002125. CMP_dCMP_Zn-bd.
IPR016193. Cytidine_deaminase-like.
IPR015517. dCMP_deaminase-rel.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR11086. PTHR11086. 1 hit.
PfamiPF00383. dCMP_cyt_deam_1. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
SSF53927. SSF53927. 1 hit.
PROSITEiPS00903. CYT_DCMP_DEAMINASES_1. 1 hit.
PS51747. CYT_DCMP_DEAMINASES_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O43012-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPTVGLTGPL CSGKDAVVEY LETKHGFNAI FRLPQLNEDG EYIYRTGDLV
60 70 80 90 100
LGSVDDLISY LTPRWRERFV INGIHSPRLL SALLKRPFFL LVYIDAPIML
110 120 130 140 150
RFNRYKTYSS LANTTLEEFC SIQDAAAFQS DNAGTRHRAL ANLLINNDSN
160 170 180 190 200
IKLHLWEKLQ KADLLNPNRF RPSWDSYFME MASLAAKRSN CMKRRVGCVL
210 220 230 240 250
VRGNRVIATG YNGTPRGATN CNEGGCPRCN SASSCGKELD TCLCLHAEEN
260 270 280 290 300
ALLEAGRERV GNNAILYCDT CPCLTCSVKI TQLGIKEVVY HTSYNMDSHT
310 320
ASLLQAAGVQ LRQYIPPENS IF
Length:322
Mass (Da):35,974
Last modified:February 22, 2012 - v2
Checksum:i61047656CC738B69
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA17893.2.
PIRiT40152.
RefSeqiNP_596442.2. NM_001022361.2.

Genome annotation databases

EnsemblFungiiSPBC2G2.13c.1; SPBC2G2.13c.1:pep; SPBC2G2.13c.
GeneIDi2540338.
KEGGispo:SPBC2G2.13c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA17893.2.
PIRiT40152.
RefSeqiNP_596442.2. NM_001022361.2.

3D structure databases

ProteinModelPortaliO43012.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi276867. 72 interactions.
MINTiMINT-4674632.

Proteomic databases

MaxQBiO43012.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC2G2.13c.1; SPBC2G2.13c.1:pep; SPBC2G2.13c.
GeneIDi2540338.
KEGGispo:SPBC2G2.13c.

Organism-specific databases

EuPathDBiFungiDB:SPBC2G2.13c.
PomBaseiSPBC2G2.13c.

Phylogenomic databases

eggNOGiCOG2131.
HOGENOMiHOG000217578.
InParanoidiO43012.
KOiK01493.
OMAiRLRPTWD.
OrthoDBiEOG7BCNPR.

Enzyme and pathway databases

ReactomeiREACT_327756. Pyrimidine biosynthesis.

Miscellaneous databases

NextBioi20801466.
PROiO43012.

Family and domain databases

InterProiIPR016192. APOBEC/CMP_deaminase_Zn-bd.
IPR002125. CMP_dCMP_Zn-bd.
IPR016193. Cytidine_deaminase-like.
IPR015517. dCMP_deaminase-rel.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR11086. PTHR11086. 1 hit.
PfamiPF00383. dCMP_cyt_deam_1. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
SSF53927. SSF53927. 1 hit.
PROSITEiPS00903. CYT_DCMP_DEAMINASES_1. 1 hit.
PS51747. CYT_DCMP_DEAMINASES_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  2. "Comparative functional genomics of the fission yeasts."
    Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N., Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y., Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K.
    , Bayne E.H., Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G., French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A., Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P., Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R., Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J., Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W., Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.
    Science 332:930-936(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVISION OF GENE MODEL.
  3. "ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
    Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
    Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiDCTD_SCHPO
AccessioniPrimary (citable) accession number: O43012
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: February 22, 2012
Last modified: July 22, 2015
This is version 93 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.