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O59730

- MAP1_SCHPO

UniProt

O59730 - MAP1_SCHPO

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Protein
Methionine aminopeptidase 1
Gene
fma1, SPBC3E7.10
Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val) By similarity.UniRule annotation

Catalytic activityi

Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.UniRule annotation

Cofactori

Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe2+-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei192 – 1921Substrate By similarity
Metal bindingi209 – 2091Divalent metal cation 1 By similarity
Metal bindingi220 – 2201Divalent metal cation 1 By similarity
Metal bindingi220 – 2201Divalent metal cation 2; catalytic By similarity
Metal bindingi289 – 2891Divalent metal cation 2; catalytic; via tele nitrogen By similarity
Binding sitei296 – 2961Substrate By similarity
Metal bindingi322 – 3221Divalent metal cation 2; catalytic By similarity
Metal bindingi353 – 3531Divalent metal cation 1 By similarity
Metal bindingi353 – 3531Divalent metal cation 2; catalytic By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-HAMAP
  2. metalloaminopeptidase activity Source: PomBase

GO - Biological processi

  1. protein initiator methionine removal involved in protein maturation Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease

Keywords - Ligandi

Metal-binding

Protein family/group databases

MEROPSiM24.017.

Names & Taxonomyi

Protein namesi
Recommended name:
Methionine aminopeptidase 1 (EC:3.4.11.18)
Short name:
MAP 1
Short name:
MetAP 1
Alternative name(s):
Peptidase M 1
Gene namesi
Name:fma1
ORF Names:SPBC3E7.10
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485: Chromosome II

Organism-specific databases

PomBaseiSPBC3E7.10.

Subcellular locationi

Cytoplasm. Nucleusnucleolus 1 Publication

GO - Cellular componenti

  1. cytosol Source: PomBase
  2. cytosolic ribosome Source: UniProtKB-HAMAP
  3. nucleolus Source: PomBase
  4. nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 379379Methionine aminopeptidase 1UniRule annotation
PRO_0000148972Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei373 – 3731Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO59730.
PaxDbiO59730.

Interactioni

Subunit structurei

Associates with the 60S ribosomal subunit of the 80S translational complex By similarity.

Protein-protein interaction databases

BioGridi277444. 17 interactions.
MINTiMINT-4675730.
STRINGi4896.SPBC3E7.10-1.

Structurei

3D structure databases

ProteinModelPortaliO59730.
SMRiO59730. Positions 72-373.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni10 – 5344Zinc finger-like; important for proper ribosome association By similarity
Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0024.
HOGENOMiHOG000030427.
KOiK01265.
OMAiCFKRNWS.
OrthoDBiEOG78WM23.
PhylomeDBiO59730.

Family and domain databases

Gene3Di3.90.230.10. 1 hit.
HAMAPiMF_01974. MetAP_1.
InterProiIPR001714. Pept_M24_MAP.
IPR000994. Pept_M24_structural-domain.
IPR002467. Pept_M24A_MAP1.
[Graphical view]
PfamiPF00557. Peptidase_M24. 1 hit.
[Graphical view]
PRINTSiPR00599. MAPEPTIDASE.
SUPFAMiSSF55920. SSF55920. 1 hit.
TIGRFAMsiTIGR00500. met_pdase_I. 1 hit.
PROSITEiPS00680. MAP_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O59730-1 [UniParc]FASTAAdd to Basket

« Hide

MATEIAKHIC CGIDCNNEAD RLQCPKCLND GVKSYFCGQE CFRNSWNIHK    50
HLHRPPNVEK REDGTYNPFP KFHFAGSLKP VYPLSPIRKV PPHIKRPDYA 100
KTGVSRSEQI EGRSFKLKRL TPKEQEGMRK VCRLGREVLD AAAAAVRPGT 150
TTDELDSIVH NACIERDCFP STLNYYAFPK SVCTSVNEII CHGIPDQRPL 200
EDGDIVNIDV SLYHNGFHGD LNETYYVGDK AKANPDLVCL VENTRIALDK 250
AIAAVKPGVL FQEFGNIIEK HTNSITEKQI SVVRTYCGHG INQLFHCSPS 300
IPHYSHNKAP GIARPGMTFT IEPMLTLGPA RDITWPDDWT SSTASGRCSA 350
QFEHTLLVTE TGCEVLTARL PNSPGGPLK 379
Length:379
Mass (Da):42,139
Last modified:August 1, 1998 - v1
Checksum:iD7A30E2886E3B248
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CU329671 Genomic DNA. Translation: CAA19013.1.
PIRiT40384.
RefSeqiNP_596097.1. NM_001022013.2.

Genome annotation databases

EnsemblFungiiSPBC3E7.10.1; SPBC3E7.10.1:pep; SPBC3E7.10.
GeneIDi2540928.
KEGGispo:SPBC3E7.10.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CU329671 Genomic DNA. Translation: CAA19013.1 .
PIRi T40384.
RefSeqi NP_596097.1. NM_001022013.2.

3D structure databases

ProteinModelPortali O59730.
SMRi O59730. Positions 72-373.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 277444. 17 interactions.
MINTi MINT-4675730.
STRINGi 4896.SPBC3E7.10-1.

Protein family/group databases

MEROPSi M24.017.

Proteomic databases

MaxQBi O59730.
PaxDbi O59730.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii SPBC3E7.10.1 ; SPBC3E7.10.1:pep ; SPBC3E7.10 .
GeneIDi 2540928.
KEGGi spo:SPBC3E7.10.

Organism-specific databases

PomBasei SPBC3E7.10.

Phylogenomic databases

eggNOGi COG0024.
HOGENOMi HOG000030427.
KOi K01265.
OMAi CFKRNWS.
OrthoDBi EOG78WM23.
PhylomeDBi O59730.

Miscellaneous databases

NextBioi 20802043.
PROi O59730.

Family and domain databases

Gene3Di 3.90.230.10. 1 hit.
HAMAPi MF_01974. MetAP_1.
InterProi IPR001714. Pept_M24_MAP.
IPR000994. Pept_M24_structural-domain.
IPR002467. Pept_M24A_MAP1.
[Graphical view ]
Pfami PF00557. Peptidase_M24. 1 hit.
[Graphical view ]
PRINTSi PR00599. MAPEPTIDASE.
SUPFAMi SSF55920. SSF55920. 1 hit.
TIGRFAMsi TIGR00500. met_pdase_I. 1 hit.
PROSITEi PS00680. MAP_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

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.
  2. "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].
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-373, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiMAP1_SCHPO
AccessioniPrimary (citable) accession number: O59730
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: August 1, 1998
Last modified: June 11, 2014
This is version 111 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. Peptidase families
    Classification of peptidase families and list of entries
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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