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Q0C838

- MAP21_ASPTN

UniProt

Q0C838 - MAP21_ASPTN

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Protein

Methionine aminopeptidase 2-1

Gene
ATEG_10146
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 sitei210 – 2101Substrate By similarity
Metal bindingi231 – 2311Divalent metal cation 1 By similarity
Metal bindingi242 – 2421Divalent metal cation 1 By similarity
Metal bindingi242 – 2421Divalent metal cation 2; catalytic By similarity
Metal bindingi306 – 3061Divalent metal cation 2; catalytic; via tele nitrogen By similarity
Binding sitei314 – 3141Substrate By similarity
Metal bindingi339 – 3391Divalent metal cation 2; catalytic By similarity
Metal bindingi434 – 4341Divalent metal cation 1 By similarity
Metal bindingi434 – 4341Divalent 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 2-1 (EC:3.4.11.18)
Short name:
MAP 2-1
Short name:
MetAP 2-1
Alternative name(s):
Peptidase M
Gene namesi
ORF Names:ATEG_10146
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 – 453453Methionine aminopeptidase 2-1UniRule annotationPRO_0000407625Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi33178.CADATEAP00000518.

Structurei

3D structure databases

ProteinModelPortaliQ0C838.
SMRiQ0C838. Positions 90-453.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi67 – 8216Lys-richUniRule annotationAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0024.
HOGENOMiHOG000226278.
OMAiRNISAHN.
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.

Q0C838-1 [UniParc]FASTAAdd to Basket

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MGSKTPDGHR QSPDASNSSE LKPASPNPKP SQNGSQSADL DRGVVGEDDD    50
DDDENEEVGV ITTNAEKKKK RKKSKKKNKK SKSGAAPATQ QTTPPRVPLS 100
TLFPSGYPVG ELVPYENTAR TTDEESQYNS RLWDEDLLTD YRQAAEIHRQ 150
VRQYAQAELI KPGASLQSIA EGIEDGVRAL CGHQGLDTGD ALKAGMGFPT 200
GLCLNNIAAH WTPNPGGKDV ILEKSDVLKV DFGVHINGRI VDSAFTVAFD 250
HTYDNLLTAV KEATNTGIMV HVFLDDLVGS EVMESYEVDL AGKTIPVKAI 300
RNITGHDILR YNIHGGKQIP FIKNNNPDKM EEGEVFAIET FGSTGKGVLD 350
DDIGIYGYGR NANVPGSHLR LASAKSLLKT IDANFGSLVF CRRYLERLGV 400
KSYHLGMKNL IDNGIVESYA PLVDVKGSYT AQFEHTILLH SGGKEVISRG 450
EDY 453
Length:453
Mass (Da):49,298
Last modified:October 17, 2006 - v1
Checksum:i7C226C2EE5896EC8
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CH476609 Genomic DNA. Translation: EAU29595.1.
RefSeqiXP_001209448.1. XM_001209448.1.

Genome annotation databases

EnsemblFungiiCADATEAT00000518; CADATEAP00000518; CADATEAG00000518.
GeneIDi4319451.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CH476609 Genomic DNA. Translation: EAU29595.1 .
RefSeqi XP_001209448.1. XM_001209448.1.

3D structure databases

ProteinModelPortali Q0C838.
SMRi Q0C838. Positions 90-453.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 33178.CADATEAP00000518.

Protein family/group databases

MEROPSi M24.002.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADATEAT00000518 ; CADATEAP00000518 ; CADATEAG00000518 .
GeneIDi 4319451.

Phylogenomic databases

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

Entry informationi

Entry nameiMAP21_ASPTN
AccessioniPrimary (citable) accession number: Q0C838
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: October 17, 2006
Last modified: June 11, 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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