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B6QD96

- MAP22_PENMQ

UniProt

B6QD96 - MAP22_PENMQ

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Protein

Methionine aminopeptidase 2-2

Gene

PMAA_077770

Organism
Penicillium marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
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).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 sitei215 – 2151SubstrateUniRule annotation
Metal bindingi236 – 2361Divalent metal cation 1UniRule annotation
Metal bindingi247 – 2471Divalent metal cation 1UniRule annotation
Metal bindingi247 – 2471Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi316 – 3161Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
Binding sitei324 – 3241SubstrateUniRule annotation
Metal bindingi349 – 3491Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi444 – 4441Divalent metal cation 1UniRule annotation
Metal bindingi444 – 4441Divalent metal cation 2; catalyticUniRule annotation

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

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:PMAA_077770
OrganismiPenicillium marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
Taxonomic identifieri441960 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesTrichocomaceaeTalaromyces
ProteomesiUP000001294: Unassembled WGS sequence

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 463463Methionine aminopeptidase 2-2PRO_0000407633Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliB6QD96.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi76 – 794Poly-Lys

Sequence similaritiesi

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

Phylogenomic databases

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]
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.

B6QD96-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGAKTFEGGD NHEDATNALS TKSNAVGGKP RGANMLEDGD GEFGTDDDDD
60 70 80 90 100
GDGQDSSLAV VNPEDGSKPK KRKRSKKKKS NKKKPGDGAQ QQTSPPRVPL
110 120 130 140 150
SQLFPDGKYP VGQMVKVPAV NLRRTTDEEL RYLSRGTITN DEALSDYRKA
160 170 180 190 200
AEVHRQVRHW VHETVHPGQS LTELAVGIED GVRALLGHQG LEPGDSLKGG
210 220 230 240 250
MGFPTGLALN NCAAHYTPNP GQKDIILKKE DVMKVDFGVH VNGWIVDSAF
260 270 280 290 300
TVTFDPVYDN LLAAVKDATN TGLKCAGVDA RVGEIGGYIQ EAMESYEVEI
310 320 330 340 350
NGKVHPVKAI RNITGHDILP YRIHGGKQVP FIKSKDQTKM EEGEVFAIET
360 370 380 390 400
FGTTGKGYMM DGPGVYGYSK DPDARNMHLP LASARALLKT INQNFGTIPF
410 420 430 440 450
CRRYLDRLGL EKYLLGMNSL ISHGIVHMYP PLVDIPGSYT AQFEHTILIK
460
SSGNEIISRG DDY
Length:463
Mass (Da):50,462
Last modified:December 16, 2008 - v1
Checksum:i361160DAEC041D14
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS995901 Genomic DNA. Translation: EEA23746.1.
RefSeqiXP_002147257.1. XM_002147221.1.

Genome annotation databases

GeneIDi7026154.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS995901 Genomic DNA. Translation: EEA23746.1 .
RefSeqi XP_002147257.1. XM_002147221.1.

3D structure databases

ProteinModelPortali B6QD96.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 7026154.

Phylogenomic databases

OrthoDBi EOG7BGHW3.

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 ]
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 Penicillium marneffei strain ATCC 18224."
    Fedorova N.D., Joardar V.S., Maiti R., Schobel S., Amedeo P., Galens K., Inman J.M., White O.R., Whitty B.R., Wortman J.R., Nierman W.C.
    Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 18224 / CBS 334.59 / QM 7333.

Entry informationi

Entry nameiMAP22_PENMQ
AccessioniPrimary (citable) accession number: B6QD96
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: December 16, 2008
Last modified: November 26, 2014
This is version 37 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