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A1CH02

- MAP22_ASPCL

UniProt

A1CH02 - MAP22_ASPCL

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Protein

Methionine aminopeptidase 2-2

Gene
ACLA_046220
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 sitei197 – 1971Substrate By similarity
Metal bindingi217 – 2171Divalent metal cation 1 By similarity
Metal bindingi228 – 2281Divalent metal cation 1 By similarity
Metal bindingi228 – 2281Divalent metal cation 2; catalytic By similarity
Metal bindingi297 – 2971Divalent metal cation 2; catalytic; via tele nitrogen By similarity
Binding sitei305 – 3051Substrate By similarity
Metal bindingi330 – 3301Divalent metal cation 2; catalytic By similarity
Metal bindingi425 – 4251Divalent metal cation 1 By similarity
Metal bindingi425 – 4251Divalent 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

Protein family/group databases

MEROPSiM24.002.

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:ACLA_046220
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 – 435435Methionine aminopeptidase 2-2UniRule annotationPRO_0000407598Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi5057.CADACLAP00004837.

Structurei

3D structure databases

ProteinModelPortaliA1CH02.
SMRiA1CH02. Positions 75-430.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi60 – 7112Poly-LysUniRule 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.

A1CH02-1 [UniParc]FASTAAdd to Basket

« Hide

MAAQTTEKLQ KLDLNGQSGD AKADAPAAGQ AEAGEAEEDS DDEKDDGNAA    50
PEAGAGGAAK KKKRKSKKKK KGGAKVQSSP PRVPVSNLFP NNQYPEGEIV 100
EYTNENSYRT TNEEKRYLDR MNNDFLQEYR QAAEVHRQVR QYAQKNIKPG 150
QTLTEIAEGI EDAVRALTGH QGLEEGDNLK GGMGFPCGLS INHCAAHYTP 200
NAGNKMVLQQ GDVMKVDFGA QINGRIVDSA FTMTFDPVYD PLLEAVKDAT 250
NTGIREAGID VRMSDIGAAI QEAMESYEIE LNGTMYPVKC IRNLNGHNID 300
QHVIHGGKSV PIVKGGDQTK MEEGETFAIE TFGSTGKGYV REDMETSHYA 350
LVPDAPSVPL RLSSAKNLLN VINKNFGTLP FCRRYLDRLG QDKYLLGLNN 400
LVSSGIVQDY PPLCDIKGSY TAQFEHVQIP SHSHP 435
Length:435
Mass (Da):47,491
Last modified:January 23, 2007 - v1
Checksum:i2D152BB644700084
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DS027054 Genomic DNA. Translation: EAW10157.1.
RefSeqiXP_001271583.1. XM_001271582.1.

Genome annotation databases

EnsemblFungiiCADACLAT00004938; CADACLAP00004837; CADACLAG00004938.
GeneIDi4704294.
KEGGiact:ACLA_046220.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DS027054 Genomic DNA. Translation: EAW10157.1 .
RefSeqi XP_001271583.1. XM_001271582.1.

3D structure databases

ProteinModelPortali A1CH02.
SMRi A1CH02. Positions 75-430.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 5057.CADACLAP00004837.

Protein family/group databases

MEROPSi M24.002.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADACLAT00004938 ; CADACLAP00004837 ; CADACLAG00004938 .
GeneIDi 4704294.
KEGGi act:ACLA_046220.

Phylogenomic databases

eggNOGi COG0024.
HOGENOMi HOG000226278.
KOi K01265.
OMAi IQICEEL.
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 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1.

Entry informationi

Entry nameiMAP22_ASPCL
AccessioniPrimary (citable) accession number: A1CH02
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: January 23, 2007
Last modified: May 14, 2014
This is version 48 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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