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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).UniRule annotation

Catalytic activityi

Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.UniRule annotation

Cofactori

Co2+UniRule annotation, Zn2+UniRule annotation, Mn2+UniRule annotation, Fe2+UniRule annotationNote: 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 Fe(2+)-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei210 – 2101SubstrateUniRule annotation
Metal bindingi231 – 2311Divalent metal cation 1UniRule annotation
Metal bindingi242 – 2421Divalent metal cation 1UniRule annotation
Metal bindingi242 – 2421Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi306 – 3061Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
Binding sitei314 – 3141SubstrateUniRule annotation
Metal bindingi339 – 3391Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi434 – 4341Divalent metal cation 1UniRule annotation
Metal bindingi434 – 4341Divalent metal cation 2; catalyticUniRule annotation

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 2-1UniRule annotation (EC:3.4.11.18UniRule annotation)
Short name:
MAP 2-1UniRule annotation
Short name:
MetAP 2-1UniRule annotation
Alternative name(s):
Peptidase MUniRule annotation
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 UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 453453Methionine aminopeptidase 2-1PRO_0000407625Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi33178.CADATEAP00000518.

Structurei

3D structure databases

ProteinModelPortaliQ0C838.
SMRiQ0C838. Positions 90-453.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

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

Sequence similaritiesi

Belongs to the peptidase M24A family. Methionine aminopeptidase eukaryotic type 2 subfamily.UniRule annotation

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

« Hide

        10         20         30         40         50
MGSKTPDGHR QSPDASNSSE LKPASPNPKP SQNGSQSADL DRGVVGEDDD
60 70 80 90 100
DDDENEEVGV ITTNAEKKKK RKKSKKKNKK SKSGAAPATQ QTTPPRVPLS
110 120 130 140 150
TLFPSGYPVG ELVPYENTAR TTDEESQYNS RLWDEDLLTD YRQAAEIHRQ
160 170 180 190 200
VRQYAQAELI KPGASLQSIA EGIEDGVRAL CGHQGLDTGD ALKAGMGFPT
210 220 230 240 250
GLCLNNIAAH WTPNPGGKDV ILEKSDVLKV DFGVHINGRI VDSAFTVAFD
260 270 280 290 300
HTYDNLLTAV KEATNTGIMV HVFLDDLVGS EVMESYEVDL AGKTIPVKAI
310 320 330 340 350
RNITGHDILR YNIHGGKQIP FIKNNNPDKM EEGEVFAIET FGSTGKGVLD
360 370 380 390 400
DDIGIYGYGR NANVPGSHLR LASAKSLLKT IDANFGSLVF CRRYLERLGV
410 420 430 440 450
KSYHLGMKNL IDNGIVESYA PLVDVKGSYT AQFEHTILLH SGGKEVISRG

EDY
Length:453
Mass (Da):49,298
Last modified:October 17, 2006 - v1
Checksum:i7C226C2EE5896EC8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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: November 26, 2014
This is version 53 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, Reference 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