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O60085

- MAP2_SCHPO

UniProt

O60085 - MAP2_SCHPO

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Protein

Methionine aminopeptidase 2

Gene

fma2

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi

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 Fe(2+)-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 sitei179 – 1791SubstrateUniRule annotation
Metal bindingi199 – 1991Divalent metal cation 1UniRule annotation
Metal bindingi210 – 2101Divalent metal cation 1UniRule annotation
Metal bindingi210 – 2101Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi279 – 2791Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
Binding sitei287 – 2871SubstrateUniRule annotation
Metal bindingi312 – 3121Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi407 – 4071Divalent metal cation 1UniRule annotation
Metal bindingi407 – 4071Divalent metal cation 2; catalyticUniRule annotation

GO - Molecular functioni

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

GO - Biological processi

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

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease

Keywords - Ligandi

Metal-binding

Enzyme and pathway databases

ReactomeiREACT_255749. Inactivation, recovery and regulation of the phototransduction cascade.

Protein family/group databases

MEROPSiM24.002.

Names & Taxonomyi

Protein namesi
Recommended name:
Methionine aminopeptidase 2UniRule annotation (EC:3.4.11.18UniRule annotation)
Short name:
MAP 2UniRule annotation
Short name:
MetAP 2UniRule annotation
Alternative name(s):
Peptidase MUniRule annotation
Gene namesi
Name:fma2
Synonyms:map2
ORF Names:SPBC14C8.03
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485: Chromosome II

Organism-specific databases

PomBaseiSPBC14C8.03.

Subcellular locationi

Cytoplasm 1 PublicationUniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: PomBase
  2. cytosol Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 426426Methionine aminopeptidase 2PRO_0000311766Add
BLAST

Proteomic databases

MaxQBiO60085.
PaxDbiO60085.

Interactioni

Protein-protein interaction databases

BioGridi276246. 1 interaction.
MINTiMINT-4677062.
STRINGi4896.SPBC14C8.03-1.

Structurei

3D structure databases

ProteinModelPortaliO60085.
SMRiO60085. Positions 65-426.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi47 – 6014Lys-richAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase M24A family. Methionine aminopeptidase eukaryotic type 2 subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG0024.
HOGENOMiHOG000226278.
InParanoidiO60085.
KOiK01265.
OMAiIQICEEL.
OrthoDBiEOG7BGHW3.
PhylomeDBiO60085.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.90.230.10. 2 hits.
HAMAPiMF_03175. MetAP_2_euk.
InterProiIPR001714. Pept_M24_MAP.
IPR000994. Pept_M24_structural-domain.
IPR002468. Pept_M24A_MAP2.
IPR018349. Pept_M24A_MAP2_BS.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR10804:SF9. PTHR10804:SF9. 1 hit.
PfamiPF00557. Peptidase_M24. 1 hit.
[Graphical view]
PRINTSiPR00599. MAPEPTIDASE.
SUPFAMiSSF55920. SSF55920. 2 hits.
TIGRFAMsiTIGR00501. met_pdase_II. 1 hit.
PROSITEiPS01202. MAP_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O60085-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTSATTTEAT AKDLQEKLSL KENDVVEDDG KVEENDAAEE GASNGEKKKK
60 70 80 90 100
KKKKSSKKKK TPQEQTNPPT VGLSKIFVNK KYPVGEVCDY AEDNLWRTTD
110 120 130 140 150
EEKRALDRQN FDQYNDLRRA AEVHRQARQY AQSVIKPGMS MMDVVNTIEN
160 170 180 190 200
TTRALVEEDG LKSGIGFPTG VSLNHCAAHY TPNAGDTTIL KEKDVMKVDI
210 220 230 240 250
GVHVNGRIVD SAFTMSFDPQ YDNLLAAVKA ATNKGIEEAG IDARLNEIGE
260 270 280 290 300
AIQEVMESYE VEINGKTHQV KSIRNLCGHN LDPYIIHGGK SVPIVKGGEE
310 320 330 340 350
IKMEEGEIFA IETFGSTGRG VVHEDMECSH YAKIPDAGHI PLRLPRAKAL
360 370 380 390 400
LNTITQNFGT LPFCRRYLDR IGESKYLLAL NNLVSAGIVQ DYPPLCDIRG
410 420
SYTAQFEHTI ILHPTQKEVV SRGDDY
Length:426
Mass (Da):47,271
Last modified:August 1, 1998 - v1
Checksum:iE23E56582F7025D3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA18421.1.
PIRiT39431.
RefSeqiNP_595906.1. NM_001021814.2.

Genome annotation databases

EnsemblFungiiSPBC14C8.03.1; SPBC14C8.03.1:pep; SPBC14C8.03.
GeneIDi2539692.
KEGGispo:SPBC14C8.03.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA18421.1 .
PIRi T39431.
RefSeqi NP_595906.1. NM_001021814.2.

3D structure databases

ProteinModelPortali O60085.
SMRi O60085. Positions 65-426.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 276246. 1 interaction.
MINTi MINT-4677062.
STRINGi 4896.SPBC14C8.03-1.

Protein family/group databases

MEROPSi M24.002.

Proteomic databases

MaxQBi O60085.
PaxDbi O60085.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii SPBC14C8.03.1 ; SPBC14C8.03.1:pep ; SPBC14C8.03 .
GeneIDi 2539692.
KEGGi spo:SPBC14C8.03.

Organism-specific databases

PomBasei SPBC14C8.03.

Phylogenomic databases

eggNOGi COG0024.
HOGENOMi HOG000226278.
InParanoidi O60085.
KOi K01265.
OMAi IQICEEL.
OrthoDBi EOG7BGHW3.
PhylomeDBi O60085.

Enzyme and pathway databases

Reactomei REACT_255749. Inactivation, recovery and regulation of the phototransduction cascade.

Miscellaneous databases

NextBioi 20800845.
PROi O60085.

Family and domain databases

Gene3Di 1.10.10.10. 1 hit.
3.90.230.10. 2 hits.
HAMAPi MF_03175. MetAP_2_euk.
InterProi IPR001714. Pept_M24_MAP.
IPR000994. Pept_M24_structural-domain.
IPR002468. Pept_M24A_MAP2.
IPR018349. Pept_M24A_MAP2_BS.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view ]
PANTHERi PTHR10804:SF9. PTHR10804:SF9. 1 hit.
Pfami PF00557. Peptidase_M24. 1 hit.
[Graphical view ]
PRINTSi PR00599. MAPEPTIDASE.
SUPFAMi SSF55920. SSF55920. 2 hits.
TIGRFAMsi TIGR00501. met_pdase_II. 1 hit.
PROSITEi PS01202. MAP_2. 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].

Entry informationi

Entry nameiMAP2_SCHPO
AccessioniPrimary (citable) accession number: O60085
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: August 1, 1998
Last modified: November 26, 2014
This is version 102 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