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Protein

Methionine aminopeptidase 2-1

Gene

ACLA_062640

Organism
Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1)
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 sitei230 – 2301SubstrateUniRule annotation
Metal bindingi251 – 2511Divalent metal cation 1UniRule annotation
Metal bindingi262 – 2621Divalent metal cation 1UniRule annotation
Metal bindingi262 – 2621Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi331 – 3311Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
Binding sitei339 – 3391SubstrateUniRule annotation
Metal bindingi364 – 3641Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi459 – 4591Divalent metal cation 1UniRule annotation
Metal bindingi459 – 4591Divalent metal cation 2; catalyticUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease

Keywords - Ligandi

Metal-binding

Protein family/group databases

MEROPSiM24.002.

Names & Taxonomyi

Protein namesi
Recommended name:
Methionine aminopeptidase 2-1UniRule annotation (EC:3.4.11.18UniRule annotation)
Short name:
MAP 2-1UniRule annotation
Short name:
MetAP 2-1UniRule annotation
Alternative name(s):
Peptidase MUniRule annotation
Gene namesi
ORF Names:ACLA_062640
OrganismiAspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1)
Taxonomic identifieri344612 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000006701 Componenti: Unassembled WGS sequence

Organism-specific databases

EuPathDBiFungiDB:ACLA_062640.

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 – 478478Methionine aminopeptidase 2-1PRO_0000407620Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliA1CCP2.
SMRiA1CCP2. Positions 110-478.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi92 – 987Poly-Lys

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0024.
HOGENOMiHOG000226278.
KOiK01265.
OMAiRNITGHD.
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.

A1CCP2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSKSPEGHN QAPHGAPNAL DKPANPAVKA QNGSGSADLD RGTISNDDDD
60 70 80 90 100
ADDDEKETQI NGSSNAGRIY LFPSRPAKFQ HRPTDTPSTP EKKKKKRKRS
110 120 130 140 150
KKKAKPTEAK QTSPPRVPLS TLFPSGYPVG ELVADDRTSR VTDEETRYNS
160 170 180 190 200
RLWDDGFLAD YRQAAEIHRQ VRQYAQRELI KPGATLSSIA DGIEDGVRAL
210 220 230 240 250
SGHQGLETGD GLNAGMGFPT GLCVNHVAAH WTPNPGAKEV VLEKSDVLKV
260 270 280 290 300
DFGVHVNGRI VDSAFTVAFD PVYDNLLEAV KEATNTGIAH AGIDARVSDI
310 320 330 340 350
GAAIQEVMES YELEIAGKSV PVKAIRNITG HNILRYHIHG GKQVPFIKNN
360 370 380 390 400
RRDKMEEGEV FAIETFGSTG KGYLDDDFGI YGYGRNEHVP ATGLRLASAR
410 420 430 440 450
SLVKTIDANF GSLVFSRRYL ERLGVKSYHL AMKNLIDNGI VESYAPLVDV
460 470
KGSYTAQFEH TILLHSGGKE VISRGDDY
Length:478
Mass (Da):52,088
Last modified:January 23, 2007 - v1
Checksum:i2AEF66AA80F97A18
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS027050 Genomic DNA. Translation: EAW12299.1.
RefSeqiXP_001273725.1. XM_001273724.1.

Genome annotation databases

EnsemblFungiiCADACLAT00005915; CADACLAP00005778; CADACLAG00005915.
GeneIDi4706022.
KEGGiact:ACLA_062640.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS027050 Genomic DNA. Translation: EAW12299.1.
RefSeqiXP_001273725.1. XM_001273724.1.

3D structure databases

ProteinModelPortaliA1CCP2.
SMRiA1CCP2. Positions 110-478.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiM24.002.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADACLAT00005915; CADACLAP00005778; CADACLAG00005915.
GeneIDi4706022.
KEGGiact:ACLA_062640.

Organism-specific databases

EuPathDBiFungiDB:ACLA_062640.

Phylogenomic databases

eggNOGiCOG0024.
HOGENOMiHOG000226278.
KOiK01265.
OMAiRNITGHD.
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]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1.

Entry informationi

Entry nameiMAP21_ASPCL
AccessioniPrimary (citable) accession number: A1CCP2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 55 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.