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B8NA06

- MAP21_ASPFN

UniProt

B8NA06 - MAP21_ASPFN

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Protein

Methionine aminopeptidase 2-1

Gene
AFLA_113020
Organism
Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM 12722 / SRRC 167)
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 sitei198 – 1981Substrate By similarity
Metal bindingi218 – 2181Divalent metal cation 1 By similarity
Metal bindingi229 – 2291Divalent metal cation 1 By similarity
Metal bindingi229 – 2291Divalent metal cation 2; catalytic By similarity
Metal bindingi298 – 2981Divalent metal cation 2; catalytic; via tele nitrogen By similarity
Binding sitei306 – 3061Substrate By similarity
Metal bindingi331 – 3311Divalent metal cation 2; catalytic By similarity
Metal bindingi426 – 4261Divalent metal cation 1 By similarity
Metal bindingi426 – 4261Divalent 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

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:AFLA_113020
OrganismiAspergillus flavus (strain ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM 12722 / SRRC 167)
Taxonomic identifieri332952 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000001875: 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 – 445445Methionine aminopeptidase 2-1UniRule annotationPRO_0000407600Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi5059.CADAFLAP00005036.

Structurei

3D structure databases

ProteinModelPortaliB8NA06.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi60 – 7617Lys-richUniRule 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.

B8NA06-1 [UniParc]FASTAAdd to Basket

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MAAQASEDLQ KLDLNGQGGA AKADAPTAGQ AEAGEAEDDS DDDADEGNAA    50
PEGGANGAAK KKKKRKSKKK KKGGAKVQSE PPRVPLSQLF AGKQYPEGEI 100
VEYKDDNLYR TTNEEKRYLD RMNNDFLQEY RQGAEVHRQV RQYAQKTIKP 150
GQTLTEIAEG IEESVRALTG HQGLEEGDNL KGGMGFPCGL SINHCAAHYT 200
PNAGNKMVLQ QGDVMKVDFG AHINGRIVDS AFTVAFDPVY DPLLEAVKDA 250
TNTGIREAGI DVRMSDIGAA IQEAMESYEV ELNGTMHPVK CIRNLNGHNI 300
DQHVIHGGKS VPIVKGGDQT KMEEGEVFAI ETFGSTGKGY VREDMETSHY 350
ALVPNASPVP LRLSSAKNLL NVINKNFGTL PFCRRYLDRL GQDKYLLGLN 400
NLVSSGIVQD YPPLCDIKGS YTAQYEHTIV LRPNVKEVIS RGDDY 445
Length:445
Mass (Da):48,527
Last modified:March 3, 2009 - v1
Checksum:i83C8106EC333AE1C
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
EQ963475 Genomic DNA. Translation: EED53925.1.
RefSeqiXP_002377171.1. XM_002377130.1.

Genome annotation databases

EnsemblFungiiCADAFLAT00005036; CADAFLAP00005036; CADAFLAG00005036.
GeneIDi7912803.
KEGGiafv:AFLA_113020.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
EQ963475 Genomic DNA. Translation: EED53925.1 .
RefSeqi XP_002377171.1. XM_002377130.1.

3D structure databases

ProteinModelPortali B8NA06.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 5059.CADAFLAP00005036.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADAFLAT00005036 ; CADAFLAP00005036 ; CADAFLAG00005036 .
GeneIDi 7912803.
KEGGi afv:AFLA_113020.

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. "Genome sequence of Aspergillus flavus strain NRRL 3357."
    Payne W.G.A., Dean R.A., Nierman W.C., Amedeo P., Caler E.G.A., Fedorova N.D., Maiti R., Joardar V., Inman J., Galinsky K.J., Yu J., Bhatnagar D., Cleveland T.E.
    Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM 12722 / SRRC 167.

Entry informationi

Entry nameiMAP21_ASPFN
AccessioniPrimary (citable) accession number: B8NA06
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: March 3, 2009
Last modified: May 14, 2014
This is version 36 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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