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Protein

Methionine aminopeptidase 1

Gene

fma1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: 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).UniRule annotation

Catalytic activityi

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

Cofactori

Co2+UniRule annotation, Zn2+UniRule annotation, Mn2+UniRule annotation, Fe2+UniRule annotationNote: 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.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei192 – 1921SubstrateUniRule annotation
Metal bindingi209 – 2091Divalent metal cation 1UniRule annotation
Metal bindingi220 – 2201Divalent metal cation 1UniRule annotation
Metal bindingi220 – 2201Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi289 – 2891Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
Binding sitei296 – 2961SubstrateUniRule annotation
Metal bindingi322 – 3221Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi353 – 3531Divalent metal cation 1UniRule annotation
Metal bindingi353 – 3531Divalent metal cation 2; catalyticUniRule annotation

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

Enzyme and pathway databases

ReactomeiREACT_348437. Inactivation, recovery and regulation of the phototransduction cascade.

Protein family/group databases

MEROPSiM24.017.

Names & Taxonomyi

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

Organism-specific databases

EuPathDBiFungiDB:SPBC3E7.10.
PomBaseiSPBC3E7.10.

Subcellular locationi

  1. Cytoplasm UniRule annotation1 Publication
  2. 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 1PRO_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.UniRule annotation

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliO59730.
SMRiO59730. Positions 72-373.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni10 – 5344Zinc finger-like; important for proper ribosome associationUniRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG0024.
HOGENOMiHOG000030427.
InParanoidiO59730.
KOiK01265.
OMAiPTIQGER.
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

        10         20         30         40         50
MATEIAKHIC CGIDCNNEAD RLQCPKCLND GVKSYFCGQE CFRNSWNIHK
60 70 80 90 100
HLHRPPNVEK REDGTYNPFP KFHFAGSLKP VYPLSPIRKV PPHIKRPDYA
110 120 130 140 150
KTGVSRSEQI EGRSFKLKRL TPKEQEGMRK VCRLGREVLD AAAAAVRPGT
160 170 180 190 200
TTDELDSIVH NACIERDCFP STLNYYAFPK SVCTSVNEII CHGIPDQRPL
210 220 230 240 250
EDGDIVNIDV SLYHNGFHGD LNETYYVGDK AKANPDLVCL VENTRIALDK
260 270 280 290 300
AIAAVKPGVL FQEFGNIIEK HTNSITEKQI SVVRTYCGHG INQLFHCSPS
310 320 330 340 350
IPHYSHNKAP GIARPGMTFT IEPMLTLGPA RDITWPDDWT SSTASGRCSA
360 370
QFEHTLLVTE TGCEVLTARL PNSPGGPLK
Length:379
Mass (Da):42,139
Last modified:August 1, 1998 - v1
Checksum:iD7A30E2886E3B248
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA19013.1.
PIRiT40384.
RefSeqiNP_596097.1. NM_001022013.2.

3D structure databases

ProteinModelPortaliO59730.
SMRiO59730. Positions 72-373.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Protein family/group databases

MEROPSiM24.017.

Proteomic databases

MaxQBiO59730.
PaxDbiO59730.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:SPBC3E7.10.
PomBaseiSPBC3E7.10.

Phylogenomic databases

eggNOGiCOG0024.
HOGENOMiHOG000030427.
InParanoidiO59730.
KOiK01265.
OMAiPTIQGER.
OrthoDBiEOG78WM23.
PhylomeDBiO59730.

Enzyme and pathway databases

ReactomeiREACT_348437. Inactivation, recovery and regulation of the phototransduction cascade.

Miscellaneous databases

NextBioi20802043.
PROiO59730.

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]
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.
  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: April 29, 2015
This is version 117 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

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.