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Protein

Putative agmatinase 1

Gene

SPAC11D3.09

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 bindingi186 – 1861Manganese 1PROSITE-ProRule annotation
Metal bindingi209 – 2091Manganese 1PROSITE-ProRule annotation
Metal bindingi209 – 2091Manganese 2PROSITE-ProRule annotation
Metal bindingi211 – 2111Manganese 2PROSITE-ProRule annotation
Metal bindingi213 – 2131Manganese 1PROSITE-ProRule annotation
Metal bindingi307 – 3071Manganese 1PROSITE-ProRule annotation
Metal bindingi307 – 3071Manganese 2PROSITE-ProRule annotation
Metal bindingi309 – 3091Manganese 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 1 (EC:3.5.3.11)
Alternative name(s):
Agmatine ureohydrolase 1
Short name:
AUH 1
Gene namesi
ORF Names:SPAC11D3.09
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC11D3.09.
PomBaseiSPAC11D3.09.

Subcellular locationi

GO - Cellular componenti

  • endoplasmic reticulum Source: PomBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence AnalysisAdd
BLAST
Chaini21 – 394374Putative agmatinase 1PRO_0000002091Add
BLAST

Interactioni

Protein-protein interaction databases

BioGridi278065. 3 interactions.
MINTiMINT-4696816.

Structurei

3D structure databases

ProteinModelPortaliQ10088.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the arginase family.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0010.
HOGENOMiHOG000204320.
InParanoidiQ10088.
KOiK01480.
OMAiTYFYWAS.
OrthoDBiEOG718KPD.
PhylomeDBiQ10088.

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.

Q10088-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALQSLFLIL LAGAAQLAQA HPKIFEQSRA NAVETFDDAF PGDGETQADS
60 70 80 90 100
VFSGIATFGR LPYWKCLNDK SQSFDIAFLG APFDTGTSYR PGARFGPSGI
110 120 130 140 150
REGSRRLNLY GGYNVPMETN PFNNWAKIVD CGDIPLTSYD NAVAIKQIEN
160 170 180 190 200
GHFELLTRKP TSYSEKDGYA LDGSVLPRVI TLGGDHTIVL PILRSVSRAY
210 220 230 240 250
GPVSIIHFDS HLDSWKPKVF GGGKSSVGSI NHGTYFYHAS QEGLVSNDSN
260 270 280 290 300
IHAGIRTTLS GLSDYDNDAD CGFEIIEARE IDTIGIDAII KRIRDRVGDG
310 320 330 340 350
IAYLSIDIDV LDPAYAPATG TPESAGWTTR ELRTILRGLD GIKLVGADIV
360 370 380 390
EVAPAYDFAE VTTLAAADIL FEVMSIMVKT PVYKEQAKQQ SRFY
Length:394
Mass (Da):42,879
Last modified:February 1, 1996 - v1
Checksum:iD6CFFBF3945C5036
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAA92310.1.
PIRiT37520.
RefSeqiNP_592806.1. NM_001018206.2.

Genome annotation databases

EnsemblFungiiSPAC11D3.09.1; SPAC11D3.09.1:pep; SPAC11D3.09.
GeneIDi2541568.
KEGGispo:SPAC11D3.09.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAA92310.1.
PIRiT37520.
RefSeqiNP_592806.1. NM_001018206.2.

3D structure databases

ProteinModelPortaliQ10088.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi278065. 3 interactions.
MINTiMINT-4696816.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC11D3.09.1; SPAC11D3.09.1:pep; SPAC11D3.09.
GeneIDi2541568.
KEGGispo:SPAC11D3.09.

Organism-specific databases

EuPathDBiFungiDB:SPAC11D3.09.
PomBaseiSPAC11D3.09.

Phylogenomic databases

eggNOGiCOG0010.
HOGENOMiHOG000204320.
InParanoidiQ10088.
KOiK01480.
OMAiTYFYWAS.
OrthoDBiEOG718KPD.
PhylomeDBiQ10088.

Enzyme and pathway databases

ReactomeiREACT_275181. Agmatine biosynthesis.

Miscellaneous databases

NextBioi20802662.
PROiQ10088.

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 nameiSPEB1_SCHPO
AccessioniPrimary (citable) accession number: Q10088
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: July 22, 2015
This is version 108 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.