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A1CCP2

- MAP21_ASPCL

UniProt

A1CCP2 - MAP21_ASPCL

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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: 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 sitei230 – 2301Substrate By similarity
Metal bindingi251 – 2511Divalent metal cation 1 By similarity
Metal bindingi262 – 2621Divalent metal cation 1 By similarity
Metal bindingi262 – 2621Divalent metal cation 2; catalytic By similarity
Metal bindingi331 – 3311Divalent metal cation 2; catalytic; via tele nitrogen By similarity
Binding sitei339 – 3391Substrate By similarity
Metal bindingi364 – 3641Divalent metal cation 2; catalytic By similarity
Metal bindingi459 – 4591Divalent metal cation 1 By similarity
Metal bindingi459 – 4591Divalent metal cation 2; catalytic By similarity

GO - Molecular functioni

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

GO - Biological processi

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

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 – 478478Methionine aminopeptidase 2-1UniRule annotation
PRO_0000407620Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi5057.CADACLAP00005778.

Structurei

3D structure databases

ProteinModelPortaliA1CCP2.
SMRiA1CCP2. Positions 110-478.

Family & Domainsi

Compositional bias

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0024.
HOGENOMiHOG000226278.
KOiK01265.
OMAiRNISAHN.
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

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MGSKSPEGHN QAPHGAPNAL DKPANPAVKA QNGSGSADLD RGTISNDDDD    50
ADDDEKETQI NGSSNAGRIY LFPSRPAKFQ HRPTDTPSTP EKKKKKRKRS 100
KKKAKPTEAK QTSPPRVPLS TLFPSGYPVG ELVADDRTSR VTDEETRYNS 150
RLWDDGFLAD YRQAAEIHRQ VRQYAQRELI KPGATLSSIA DGIEDGVRAL 200
SGHQGLETGD GLNAGMGFPT GLCVNHVAAH WTPNPGAKEV VLEKSDVLKV 250
DFGVHVNGRI VDSAFTVAFD PVYDNLLEAV KEATNTGIAH AGIDARVSDI 300
GAAIQEVMES YELEIAGKSV PVKAIRNITG HNILRYHIHG GKQVPFIKNN 350
RRDKMEEGEV FAIETFGSTG KGYLDDDFGI YGYGRNEHVP ATGLRLASAR 400
SLVKTIDANF GSLVFSRRYL ERLGVKSYHL AMKNLIDNGI VESYAPLVDV 450
KGSYTAQFEH TILLHSGGKE VISRGDDY 478
Length:478
Mass (Da):52,088
Last modified:January 23, 2007 - v1
Checksum:i2AEF66AA80F97A18
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
DS027050 Genomic DNA. Translation: EAW12299.1 .
RefSeqi XP_001273725.1. XM_001273724.1.

3D structure databases

ProteinModelPortali A1CCP2.
SMRi A1CCP2. Positions 110-478.
ModBasei Search...

Protein-protein interaction databases

STRINGi 5057.CADACLAP00005778.

Protein family/group databases

MEROPSi M24.002.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADACLAT00005915 ; CADACLAP00005778 ; CADACLAG00005915 .
GeneIDi 4706022.
KEGGi act:ACLA_062640.

Phylogenomic databases

eggNOGi COG0024.
HOGENOMi HOG000226278.
KOi K01265.
OMAi RNISAHN.
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. 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: June 11, 2014
This is version 49 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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