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A1CYM1

- MAP22_NEOFI

UniProt

A1CYM1 - MAP22_NEOFI

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Protein

Methionine aminopeptidase 2-2

Gene
NFIA_034070
Organism
Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / FGSC A1164 / NRRL 181) (Aspergillus fischerianus)
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 sitei215 – 2151Substrate By similarity
Metal bindingi236 – 2361Divalent metal cation 1 By similarity
Metal bindingi247 – 2471Divalent metal cation 1 By similarity
Metal bindingi247 – 2471Divalent metal cation 2; catalytic By similarity
Metal bindingi316 – 3161Divalent metal cation 2; catalytic; via tele nitrogen By similarity
Binding sitei324 – 3241Substrate By similarity
Metal bindingi349 – 3491Divalent metal cation 2; catalytic By similarity
Metal bindingi444 – 4441Divalent metal cation 1 By similarity
Metal bindingi444 – 4441Divalent 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:NFIA_034070
OrganismiNeosartorya fischeri (strain ATCC 1020 / DSM 3700 / FGSC A1164 / NRRL 181) (Aspergillus fischerianus)
Taxonomic identifieri331117 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeNeosartorya
ProteomesiUP000006702: 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 – 463463Methionine aminopeptidase 2-2UniRule annotationPRO_0000407639Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi36630.CADNFIAP00003719.

Structurei

3D structure databases

ProteinModelPortaliA1CYM1.
SMRiA1CYM1. Positions 95-463.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi69 – 8517Lys-richUniRule annotationAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0024.
HOGENOMiHOG000226278.
KOiK01265.
OMAiNNCVAHY.
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.

A1CYM1-1 [UniParc]FASTAAdd to Basket

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MGSKSPEGHW QAPHASNSNE LKPANPDPQT SQNGSGSADL DRGVIGDDDD    50
DDEDAEENGV NTETPNVEKK KKRKKSNKKK KKKTKSGTLS VTELKQTSPP 100
RVLVSTLFPS EYPVGELVPY DCTTRTTDEE SRYNSRLWDD DFLPDYRQAA 150
EIHRQVRQYA QKELIKPGAT LLSIAEGIED GVRALSGHQG LEPGDFFKAG 200
MGFPTGLCLN HIAAHWTPNP REKDVILDKG DVLKVDFGVH VNGRIVDSAF 250
TVAFDDKYDN LLTAVREATN TGIKHAGVDA RMSDIGAAIQ EVMESYEVEI 300
DGKVFPVKAI RNITGHDILR YHIHGGKQIP FIKNNNQDKM EEGEVYAIET 350
FGSTGRGFLD DDVGVYGYGR NENMSGANLR LSSAKSLLKT IDANFGSIVF 400
SRRYLERLGV KNYLLGMKNL VDNGIVECYS PLVDVKGSYT AQFEHTILLH 450
SGGKEVISRG DDY 463
Length:463
Mass (Da):51,127
Last modified:January 23, 2007 - v1
Checksum:iC015237E375845F8
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DS027686 Genomic DNA. Translation: EAW23841.1.
RefSeqiXP_001265738.1. XM_001265737.1.

Genome annotation databases

EnsemblFungiiCADNFIAT00003808; CADNFIAP00003719; CADNFIAG00003808.
GeneIDi4592397.
KEGGinfi:NFIA_034070.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DS027686 Genomic DNA. Translation: EAW23841.1 .
RefSeqi XP_001265738.1. XM_001265737.1.

3D structure databases

ProteinModelPortali A1CYM1.
SMRi A1CYM1. Positions 95-463.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 36630.CADNFIAP00003719.

Protein family/group databases

MEROPSi M24.002.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADNFIAT00003808 ; CADNFIAP00003719 ; CADNFIAG00003808 .
GeneIDi 4592397.
KEGGi nfi:NFIA_034070.

Phylogenomic databases

eggNOGi COG0024.
HOGENOMi HOG000226278.
KOi K01265.
OMAi NNCVAHY.
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 1020 / DSM 3700 / FGSC A1164 / NRRL 181.

Entry informationi

Entry nameiMAP22_NEOFI
AccessioniPrimary (citable) accession number: A1CYM1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 51 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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