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B6HTQ4

- MAP22_PENCW

UniProt

B6HTQ4 - MAP22_PENCW

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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: 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) 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 sitei196 – 1961Substrate By similarity
Metal bindingi216 – 2161Divalent metal cation 1 By similarity
Metal bindingi227 – 2271Divalent metal cation 1 By similarity
Metal bindingi227 – 2271Divalent metal cation 2; catalytic By similarity
Metal bindingi296 – 2961Divalent metal cation 2; catalytic; via tele nitrogen By similarity
Binding sitei304 – 3041Substrate By similarity
Metal bindingi329 – 3291Divalent metal cation 2; catalytic By similarity
Metal bindingi424 – 4241Divalent metal cation 1 By similarity
Metal bindingi424 – 4241Divalent metal cation 2; catalytic By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. protein initiator methionine removal Source: UniProtKB-HAMAP
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 2-2 (EC:3.4.11.18)
Short name:
MAP 2-2
Short name:
MetAP 2-2
Alternative name(s):
Peptidase M
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: Contig Pc00c22

Subcellular locationi

Cytoplasm By similarity UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 439439Methionine aminopeptidase 2-2UniRule annotationPRO_0000407610Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi500485.B6HTQ4.

Structurei

3D structure databases

ProteinModelPortaliB6HTQ4.

Family & Domainsi

Compositional bias

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0024.
HOGENOMiHOG000226278.
KOiK01265.
OMAiIQICEEL.
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

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MAAQTTEKLD QLDLNVQAAP TADQVPAEAE EDSDDAQDEG AAEAGAAGAG    50
STLADKKKKK KKPKKKSKKK GGAKVQSEPP RVPVSNLFPN GQYPEGEIVE 100
YLNDNAYRTT NEEKRYLDRM NNDFLQEYRQ GAEVHRQVRQ YAQKNIKPGQ 150
TLTEIAEGIE DSVRALTGHS GLEEGDNIKG GMGFPCGLSI NHCAAHYTPN 200
AGNKMVLNEG DVMKVDFGAH LNGRIVDSAF TMTFDPVYDP LLAAVKDATN 250
TGIREAGIDV RMSDIGAAIQ EAMESYEVEI NGTMHPVKCI RNLNGHNIDQ 300
HVIHGGKSVP IVKSTDQTKM EEGEVFAIET FGSTGKGYVR EEMETSHYAL 350
AADAPNVPLR LSSAKNLLNL INKNFGTLPF CRRYIDRLGQ DKYLLGLNNL 400
VSSGIVQDYP PLCDIKGSYT AQYEHVCFYF GVFSTLIVY 439
Length:439
Mass (Da):48,103
Last modified:December 16, 2008 - v1
Checksum:i08C432DD67D13107
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AM920437 Genomic DNA. Translation: CAP99089.1 .
RefSeqi XP_002565710.1. XM_002565664.1.

3D structure databases

ProteinModelPortali B6HTQ4.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 500485.B6HTQ4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 8312818.
KEGGi pcs:Pc22g18010.

Phylogenomic databases

eggNOGi COG0024.
HOGENOMi HOG000226278.
KOi K01265.
OMAi IQICEEL.
OrthoDBi EOG7BGHW3.

Enzyme and pathway databases

BioCyci PCHR:PC22G18010-MONOMER.

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. 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: May 14, 2014
This is version 42 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

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

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