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Protein

Putative agmatinase 2

Gene

SPBC8E4.03

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 3 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 bindingi206 – 2061Manganese 1PROSITE-ProRule annotation
Metal bindingi229 – 2291Manganese 1PROSITE-ProRule annotation
Metal bindingi229 – 2291Manganese 2PROSITE-ProRule annotation
Metal bindingi231 – 2311Manganese 2PROSITE-ProRule annotation
Metal bindingi233 – 2331Manganese 1PROSITE-ProRule annotation
Metal bindingi331 – 3311Manganese 1PROSITE-ProRule annotation
Metal bindingi331 – 3311Manganese 2PROSITE-ProRule annotation
Metal bindingi333 – 3331Manganese 2PROSITE-ProRule annotation

GO - Molecular functioni

  1. agmatinase activity Source: UniProtKB-EC
  2. manganese ion binding Source: PomBase

GO - Biological processi

  1. cellular amino acid metabolic process Source: PomBase
  2. urea metabolic process Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_241380. Agmatine biosynthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Putative agmatinase 2 (EC:3.5.3.11)
Alternative name(s):
Agmatine ureohydrolase 2
Short name:
AUH 2
Gene namesi
ORF Names:SPBC8E4.03
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485: Chromosome II

Organism-specific databases

PomBaseiSPBC8E4.03.

Subcellular locationi

GO - Cellular componenti

  1. endoplasmic reticulum Source: PomBase
  2. fungal-type vacuole Source: PomBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence AnalysisAdd
BLAST
Chaini23 – 413391Putative agmatinase 2PRO_0000002092Add
BLAST

Proteomic databases

MaxQBiO42887.

Interactioni

Protein-protein interaction databases

BioGridi277792. 19 interactions.
MINTiMINT-4673750.
STRINGi4896.SPBC8E4.03-1.

Structurei

3D structure databases

ProteinModelPortaliO42887.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the arginase family.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0010.
HOGENOMiHOG000204320.
InParanoidiO42887.
KOiK01480.
OMAiCGDISIT.
OrthoDBiEOG718KPD.
PhylomeDBiO42887.

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.

O42887-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFTYQKIIQL ALLLSGVCGA LASIDTDSHL SPKVLEKLRP TENLAYEDDS
60 70 80 90 100
LDDDTWRSKR WEFDYQYSGI STFAHLPHVR CLVEQSEDFD IAIIGVPFDT
110 120 130 140 150
AVSHRPGARF GPKGIRSASS RQMAIRGFNP SLNVNPYESW AKILDCGDIP
160 170 180 190 200
VSSYDNQLAV RQMTEGYIDL LSRKATASPA SNNLKTAGLA KDGIFHPRLI
210 220 230 240 250
TLGGDHSIGL ASLRALGHFY GNVSVIHFDS HLDTWNPKRY YPSYWHSDRA
260 270 280 290 300
DFTHGTMFWM ASKEGLINNG TSIHAGLRTR LSGTDYYDYE EDNRVGFTFI
310 320 330 340 350
EAQEIDEIGV NGIVERIKQV VGDTLVYLSI DIDVVDPGLA PGTGTPETGG
360 370 380 390 400
WTTREMKSIL RKLDGHLNLV GAEVVEVSPP YDDRAESTSL AASDFIFEIL
410
SSMVKHPLYD VKK
Length:413
Mass (Da):45,902
Last modified:June 1, 1998 - v1
Checksum:i577EF7AF936E1346
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA16996.1.
PIRiT50379. T39168.
RefSeqiNP_596844.1. NM_001023866.2.

Genome annotation databases

EnsemblFungiiSPBC8E4.03.1; SPBC8E4.03.1:pep; SPBC8E4.03.
GeneIDi2541279.
KEGGispo:SPBC8E4.03.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA16996.1.
PIRiT50379. T39168.
RefSeqiNP_596844.1. NM_001023866.2.

3D structure databases

ProteinModelPortaliO42887.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi277792. 19 interactions.
MINTiMINT-4673750.
STRINGi4896.SPBC8E4.03-1.

Proteomic databases

MaxQBiO42887.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC8E4.03.1; SPBC8E4.03.1:pep; SPBC8E4.03.
GeneIDi2541279.
KEGGispo:SPBC8E4.03.

Organism-specific databases

PomBaseiSPBC8E4.03.

Phylogenomic databases

eggNOGiCOG0010.
HOGENOMiHOG000204320.
InParanoidiO42887.
KOiK01480.
OMAiCGDISIT.
OrthoDBiEOG718KPD.
PhylomeDBiO42887.

Enzyme and pathway databases

ReactomeiREACT_241380. Agmatine biosynthesis.

Miscellaneous databases

NextBioi20802390.

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

  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.

Entry informationi

Entry nameiSPEB2_SCHPO
AccessioniPrimary (citable) accession number: O42887
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: June 1, 1998
Last modified: January 7, 2015
This is version 105 of the entry and version 1 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.