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Q0CL94

- MAP22_ASPTN

UniProt

Q0CL94 - MAP22_ASPTN

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Protein

Methionine aminopeptidase 2-2

Gene
ATEG_05540
Organism
Aspergillus terreus (strain NIH 2624 / FGSC A1156)
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

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:ATEG_05540
OrganismiAspergillus terreus (strain NIH 2624 / FGSC A1156)
Taxonomic identifieri341663 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000007963: 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 2-2UniRule annotationPRO_0000407603Add
BLAST

Proteomic databases

PRIDEiQ0CL94.

Interactioni

Protein-protein interaction databases

STRINGi33178.CADATEAP00004684.

Structurei

3D structure databases

ProteinModelPortaliQ0CL94.
SMRiQ0CL94. Positions 76-445.

Family & Domainsi

Compositional bias

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0024.
HOGENOMiHOG000226278.
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.

Q0CL94-1 [UniParc]FASTAAdd to Basket

« Hide

MAAQASEDLK KLDLNGQAGD SKAAAATAGQ AEAGEAEDDS DDDEVDGNAA    50
PEGAASGAAK KKKKRKPKKK KKGGAKVQSS PPRVPISQLF PNNQYPEGEI 100
VEYKNENSYR TTNEEKRYLD RMNNDFLQEY RQGAEVHRQV RQYAQKNIKP 150
GQTLTEIAEG IEDAVRALTG HQGLEEGDNL KGGMGFPCGL SINHCAAHYT 200
PNAGNKMVLQ QGDVMKVDFG AHLNGRIVDS AFTMAFDPVY DPLLEAVKDA 250
TNTGIREAGI DVRMSDIGAA IQETMESYEV EINGQMHPVK CIRNLNGHNI 300
DQHVIHGGKS VPIVKGGDQT KMEEGEVFAI ETFGSTGKGY VREDMETSHY 350
ALVPNATPVP LRLSSAKNLL NVINKNFGTL PFCRRYLDRL GQDKYLLGLN 400
NLVSSGIVQD YPPLCDIKGS YTAQFEHTIV LRPTVKEVIS RGDDY 445
Length:445
Mass (Da):48,627
Last modified:October 17, 2006 - v1
Checksum:i6F5D7F18DF1AE822
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CH476600 Genomic DNA. Translation: EAU34609.1.
RefSeqiXP_001214718.1. XM_001214718.1.

Genome annotation databases

EnsemblFungiiCADATEAT00004684; CADATEAP00004684; CADATEAG00004684.
GeneIDi4320577.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CH476600 Genomic DNA. Translation: EAU34609.1 .
RefSeqi XP_001214718.1. XM_001214718.1.

3D structure databases

ProteinModelPortali Q0CL94.
SMRi Q0CL94. Positions 76-445.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 33178.CADATEAP00004684.

Protein family/group databases

MEROPSi M24.002.

Proteomic databases

PRIDEi Q0CL94.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADATEAT00004684 ; CADATEAP00004684 ; CADATEAG00004684 .
GeneIDi 4320577.

Phylogenomic databases

eggNOGi COG0024.
HOGENOMi HOG000226278.
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: NIH 2624 / FGSC A1156.

Entry informationi

Entry nameiMAP22_ASPTN
AccessioniPrimary (citable) accession number: Q0CL94
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: October 17, 2006
Last modified: May 14, 2014
This is version 50 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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