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C5FF46

- MAP22_ARTOC

UniProt

C5FF46 - MAP22_ARTOC

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Protein
Methionine aminopeptidase 2-2
Gene
MCYG_01318
Organism
Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis)
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 bindingi333 – 3331Divalent metal cation 2; catalytic By similarity
Metal bindingi428 – 4281Divalent metal cation 1 By similarity
Metal bindingi428 – 4281Divalent 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

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:MCYG_01318
OrganismiArthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis)
Taxonomic identifieri554155 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesArthrodermataceaeArthroderma
ProteomesiUP000002035: 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 – 447447Methionine aminopeptidase 2-2UniRule annotation
PRO_0000407597Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliC5FF46.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi59 – 7416Lys-richUniRule annotation
Add
BLAST

Sequence similaritiesi

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]
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.

C5FF46-1 [UniParc]FASTAAdd to Basket

« Hide

MAAQTAPELA KLDLNKNSGS AEANVVSNGG SDKDDAENEG DSDDDKDEAG    50
GSAEVNTEKK KKKKRSKKKK KAAKVQSSPP RIPLTTLFPN NAFPEGEIVE 100
YLNDNSYRTT NEEKRHLDRM NNDFLTEYRQ AAEIHRQVRQ YAQKELIKPG 150
ATLTDIAEGI EDGVRHLTGH MGLEEGDSLI AGMGFPTGLN INHCAAHYSP 200
NAGNKVVLQH GDVMKVDFGV HVNGRIVDSA FTVAFDPVFD PLLTAVKEAT 250
NTGIKEAGID VRMSDIGAAI QETMESYELE INGTSYPIKA VRNLNGHTIG 300
QYEIHGGVNG KSVPIVKGGD QTKMEEGETY AIETFGSTGK GYVRDDMETS 350
HYAKVPNAPS VPLRLSSAKN LYSLINKNFG TLPFCRRYLD RLGQEKYLLG 400
LNNLVSSGLV DAYPPLCDVK GSYTAQFEHT ILLRPNVKEV ISRGDDY 447
Length:447
Mass (Da):48,883
Last modified:July 28, 2009 - v1
Checksum:i4C2792252B598045
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DS995701 Genomic DNA. Translation: EEQ28430.1.
RefSeqiXP_002851214.1. XM_002851168.1.

Genome annotation databases

GeneIDi9228835.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DS995701 Genomic DNA. Translation: EEQ28430.1 .
RefSeqi XP_002851214.1. XM_002851168.1.

3D structure databases

ProteinModelPortali C5FF46.
ModBasei Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 9228835.

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 ]
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 MYA-4605 / CBS 113480.

Entry informationi

Entry nameiMAP22_ARTOC
AccessioniPrimary (citable) accession number: C5FF46
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: July 28, 2009
Last modified: May 14, 2014
This is version 35 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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