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Protein

Methionine aminopeptidase 2-2

Gene

Pc22g18010

Organism
Penicillium chrysogenum (strain ATCC 28089 / DSM 1075 / Wisconsin 54-1255) (Penicillium notatum)
Status
Reviewed-Annotation score: Annotation score: 3 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 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 sitei196 – 1961SubstrateUniRule annotation
Metal bindingi216 – 2161Divalent metal cation 1UniRule annotation
Metal bindingi227 – 2271Divalent metal cation 1UniRule annotation
Metal bindingi227 – 2271Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi296 – 2961Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
Binding sitei304 – 3041SubstrateUniRule annotation
Metal bindingi329 – 3291Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi424 – 4241Divalent metal cation 1UniRule annotation
Metal bindingi424 – 4241Divalent metal cation 2; catalyticUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease

Keywords - Ligandi

Metal-binding

Enzyme and pathway databases

BioCyciPCHR:PC22G18010-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Methionine aminopeptidase 2-2UniRule annotation (EC:3.4.11.18UniRule annotation)
Short name:
MAP 2-2UniRule annotation
Short name:
MetAP 2-2UniRule annotation
Alternative name(s):
Peptidase MUniRule annotation
Gene namesi
ORF Names:Pc22g18010
OrganismiPenicillium chrysogenum (strain ATCC 28089 / DSM 1075 / Wisconsin 54-1255) (Penicillium notatum)
Taxonomic identifieri500485 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaePenicilliumPenicillium chrysogenum complex
ProteomesiUP000000724 Componenti: Contig Pc00c22

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 439439Methionine aminopeptidase 2-2PRO_0000407610Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi500485.XP_002565710.1.

Structurei

3D structure databases

ProteinModelPortaliB6HTQ4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi56 – 7419Lys-richAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0024.
HOGENOMiHOG000226278.
KOiK01265.
OMAiSTRMEED.
OrthoDBiEOG7BGHW3.

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.

B6HTQ4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAQTTEKLD QLDLNVQAAP TADQVPAEAE EDSDDAQDEG AAEAGAAGAG
60 70 80 90 100
STLADKKKKK KKPKKKSKKK GGAKVQSEPP RVPVSNLFPN GQYPEGEIVE
110 120 130 140 150
YLNDNAYRTT NEEKRYLDRM NNDFLQEYRQ GAEVHRQVRQ YAQKNIKPGQ
160 170 180 190 200
TLTEIAEGIE DSVRALTGHS GLEEGDNIKG GMGFPCGLSI NHCAAHYTPN
210 220 230 240 250
AGNKMVLNEG DVMKVDFGAH LNGRIVDSAF TMTFDPVYDP LLAAVKDATN
260 270 280 290 300
TGIREAGIDV RMSDIGAAIQ EAMESYEVEI NGTMHPVKCI RNLNGHNIDQ
310 320 330 340 350
HVIHGGKSVP IVKSTDQTKM EEGEVFAIET FGSTGKGYVR EEMETSHYAL
360 370 380 390 400
AADAPNVPLR LSSAKNLLNL INKNFGTLPF CRRYIDRLGQ DKYLLGLNNL
410 420 430
VSSGIVQDYP PLCDIKGSYT AQYEHVCFYF GVFSTLIVY
Length:439
Mass (Da):48,103
Last modified:December 16, 2008 - v1
Checksum:i08C432DD67D13107
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM920437 Genomic DNA. Translation: CAP99089.1.
RefSeqiXP_002565710.1. XM_002565664.1.

Genome annotation databases

GeneIDi8312818.
KEGGipcs:Pc22g18010.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM920437 Genomic DNA. Translation: CAP99089.1.
RefSeqiXP_002565710.1. XM_002565664.1.

3D structure databases

ProteinModelPortaliB6HTQ4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi500485.XP_002565710.1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi8312818.
KEGGipcs:Pc22g18010.

Phylogenomic databases

eggNOGiCOG0024.
HOGENOMiHOG000226278.
KOiK01265.
OMAiSTRMEED.
OrthoDBiEOG7BGHW3.

Enzyme and pathway databases

BioCyciPCHR:PC22G18010-MONOMER.

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]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 28089 / DSM 1075 / Wisconsin 54-1255.

Entry informationi

Entry nameiMAP22_PENCW
AccessioniPrimary (citable) accession number: B6HTQ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: December 16, 2008
Last modified: June 24, 2015
This is version 47 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. 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.