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A5DR89

- MAP2_PICGU

UniProt

A5DR89 - MAP2_PICGU

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Protein

Methionine aminopeptidase 2

Gene

MAP2

Organism
Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii)
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 sitei210 – 2101SubstrateUniRule annotation
Metal bindingi230 – 2301Divalent metal cation 1UniRule annotation
Metal bindingi241 – 2411Divalent metal cation 1UniRule annotation
Metal bindingi241 – 2411Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi312 – 3121Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
Binding sitei320 – 3201SubstrateUniRule annotation
Metal bindingi345 – 3451Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi440 – 4401Divalent metal cation 1UniRule annotation
Metal bindingi440 – 4401Divalent 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 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:MAP2UniRule annotation
ORF Names:PGUG_05790
OrganismiMeyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii)
Taxonomic identifieri294746 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeMeyerozyma
ProteomesiUP000001997: 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 – 459459Methionine aminopeptidase 2PRO_0000407663Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi4929.A5DR89.

Structurei

3D structure databases

ProteinModelPortaliA5DR89.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi89 – 9810Poly-Lys

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0024.
InParanoidiA5DR89.
KOiK01265.
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.

A5DR89-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAKTRTNSET VSILHTLHTN QKAPGARVYR VFRFSHHPKM RSNMSQDKEA
60 70 80 90 100
NEIAVNTTET VVSTPTDVTT AETKTDGSPE TNAAPAAAKK KKNKKKKKIT
110 120 130 140 150
SIDSSYPDGV FPEGEWQEYP LEINSYRTSS EELRYLDNQR NNHWQDFRKG
160 170 180 190 200
AEIHRRVRHK AQSSIRPGMT MTEIADLIEN SVRSYAAADH TLKAGIGFPT
210 220 230 240 250
GLSLNEIAAH YTPNAGDKLV LGKDDVMKVD IGVHVNGHIV DSAFTMTFDD
260 270 280 290 300
DHKYDNLLKA VKEATNTGVR EAGIDVRLND IGAAVQEVME SYEMEIGGKT
310 320 330 340 350
YPIKCIRNLN GHNIGDYVIH SGKTVPIVAN GDMTKMEEGE TFAIETFGST
360 370 380 390 400
GNGYVIPTGE CSHYALSEEY KQARVGTDRA KQLLKTIESN FGTLPWCRRY
410 420 430 440 450
LDRVGEEKYL LALNQLVRAG AVQDYPPITD RAGSYTAQFE HTILLHPHKK

EVVSRGDDY
Length:459
Mass (Da):51,166
Last modified:July 22, 2008 - v2
Checksum:iBD5FDC3013D74BC1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH408162 Genomic DNA. Translation: EDK41692.2.
RefSeqiXP_001482027.1. XM_001481977.1.

Genome annotation databases

GeneIDi5123876.
KEGGipgu:PGUG_05790.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH408162 Genomic DNA. Translation: EDK41692.2 .
RefSeqi XP_001482027.1. XM_001481977.1.

3D structure databases

ProteinModelPortali A5DR89.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 4929.A5DR89.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 5123876.
KEGGi pgu:PGUG_05790.

Phylogenomic databases

eggNOGi COG0024.
InParanoidi A5DR89.
KOi K01265.
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 ]
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 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324.

Entry informationi

Entry nameiMAP2_PICGU
AccessioniPrimary (citable) accession number: A5DR89
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: July 22, 2008
Last modified: November 26, 2014
This is version 50 of the entry and version 2 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