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Protein

Putative agmatinase 3

Gene

SPAPB24D3.03

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

Agmatine + H2O = putrescine + urea.

Cofactori

Mn2+PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi198 – 1981Manganese 1PROSITE-ProRule annotation
Metal bindingi222 – 2221Manganese 1PROSITE-ProRule annotation
Metal bindingi222 – 2221Manganese 2PROSITE-ProRule annotation
Metal bindingi224 – 2241Manganese 2PROSITE-ProRule annotation
Metal bindingi226 – 2261Manganese 1PROSITE-ProRule annotation
Metal bindingi319 – 3191Manganese 1PROSITE-ProRule annotation
Metal bindingi319 – 3191Manganese 2PROSITE-ProRule annotation
Metal bindingi321 – 3211Manganese 2PROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_275181. Agmatine biosynthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Putative agmatinase 3 (EC:3.5.3.11)
Alternative name(s):
Agmatine ureohydrolase 3
Short name:
AUH 3
Gene namesi
ORF Names:SPAPB24D3.03
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAPB24D3.03.
PomBaseiSPAPB24D3.03.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence AnalysisAdd
BLAST
Chaini22 – 408387Putative agmatinase 3PRO_0000311760Add
BLAST

Interactioni

Protein-protein interaction databases

BioGridi279984. 6 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ9C0Y9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the arginase family.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0010.
HOGENOMiHOG000204320.
InParanoidiQ9C0Y9.
KOiK01480.
OMAiNPLMEEV.
OrthoDBiEOG718KPD.

Family and domain databases

Gene3Di3.40.800.10. 1 hit.
InterProiIPR006035. Ureohydrolase.
IPR023696. Ureohydrolase_domain.
IPR020855. Ureohydrolase_Mn_BS.
[Graphical view]
PANTHERiPTHR11358. PTHR11358. 1 hit.
PfamiPF00491. Arginase. 1 hit.
[Graphical view]
PIRSFiPIRSF036979. Arginase. 1 hit.
PRINTSiPR00116. ARGINASE.
PROSITEiPS01053. ARGINASE_1. 1 hit.
PS51409. ARGINASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9C0Y9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKSVEWFTWG VFLLLSGFGE AGRMGLGFQE KNPVFVKEKQ SPFYAVPSNY
60 70 80 90 100
EEVEFSSIVE PMYSGIATFG RLENVECLSK RSEDFDIAFI GMPFDTGTSY
110 120 130 140 150
RPGARFGPSS LREGSRRINT KYGAVNVPLE INPFKSWAKL VDCGDIPVTT
160 170 180 190 200
YDILKAMDQL ESAYFQLIAR KPSSFTDHDG FAKNDTVLPR VLSLGGDHTI
210 220 230 240 250
VLPILRALHR VYGQPISVIH FDSHLDTWAP GLIGDGDEAD GINHGSYFYF
260 270 280 290 300
ASQEGIMSKD ANIHAGIRTP ISSFSDYDDD VDCGFKIIEA REIDDLGIDG
310 320 330 340 350
IVKKIRDRVG DNLVYLSIDI DVLDPAFAPA TGTPETGGWS SREMRAILRG
360 370 380 390 400
LQGLKFVGAD LVEVAPAYDV AEITSLAGAQ LLFDIVSMMV KYPLVKEADL

SRYMPIHK
Length:408
Mass (Da):45,085
Last modified:June 13, 2012 - v2
Checksum:i3BB0F4614304C536
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAC36899.2.
RefSeqiNP_593990.2. NM_001019416.2.

Genome annotation databases

EnsemblFungiiSPAPB24D3.03.1; SPAPB24D3.03.1:pep; SPAPB24D3.03.
GeneIDi2543569.
KEGGispo:SPAPB24D3.03.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAC36899.2.
RefSeqiNP_593990.2. NM_001019416.2.

3D structure databases

ProteinModelPortaliQ9C0Y9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi279984. 6 interactions.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAPB24D3.03.1; SPAPB24D3.03.1:pep; SPAPB24D3.03.
GeneIDi2543569.
KEGGispo:SPAPB24D3.03.

Organism-specific databases

EuPathDBiFungiDB:SPAPB24D3.03.
PomBaseiSPAPB24D3.03.

Phylogenomic databases

eggNOGiCOG0010.
HOGENOMiHOG000204320.
InParanoidiQ9C0Y9.
KOiK01480.
OMAiNPLMEEV.
OrthoDBiEOG718KPD.

Enzyme and pathway databases

ReactomeiREACT_275181. Agmatine biosynthesis.

Miscellaneous databases

NextBioi20804576.
PROiQ9C0Y9.

Family and domain databases

Gene3Di3.40.800.10. 1 hit.
InterProiIPR006035. Ureohydrolase.
IPR023696. Ureohydrolase_domain.
IPR020855. Ureohydrolase_Mn_BS.
[Graphical view]
PANTHERiPTHR11358. PTHR11358. 1 hit.
PfamiPF00491. Arginase. 1 hit.
[Graphical view]
PIRSFiPIRSF036979. Arginase. 1 hit.
PRINTSiPR00116. ARGINASE.
PROSITEiPS01053. ARGINASE_1. 1 hit.
PS51409. ARGINASE_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.

Entry informationi

Entry nameiSPEB3_SCHPO
AccessioniPrimary (citable) accession number: Q9C0Y9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: June 13, 2012
Last modified: July 22, 2015
This is version 98 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.