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Protein

Methionine aminopeptidase 2-2

Gene

CHGG_07046

Organism
Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970) (Soil fungus)
Status
Reviewed-Annotation score: 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 Fe2+-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 sitei192 – 1921SubstrateUniRule annotation
Metal bindingi212 – 2121Divalent metal cation 1UniRule annotation
Metal bindingi223 – 2231Divalent metal cation 1UniRule annotation
Metal bindingi223 – 2231Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi292 – 2921Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
Binding sitei300 – 3001SubstrateUniRule annotation
Metal bindingi325 – 3251Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi420 – 4201Divalent metal cation 1UniRule annotation
Metal bindingi420 – 4201Divalent 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 2-2UniRule annotation (EC:3.4.11.18UniRule annotation)
Short name:
MAP 2-2UniRule annotation
Short name:
MetAP 2-2UniRule annotation
Alternative name(s):
Peptidase MUniRule annotation
Gene namesi
ORF Names:CHGG_07046
OrganismiChaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970) (Soil fungus)
Taxonomic identifieri306901 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesChaetomiaceaeChaetomium
ProteomesiUP000001056 Componenti: Unassembled WGS sequence

Subcellular locationi

Cytoplasm 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 – 439439Methionine aminopeptidase 2-2PRO_0000407604Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ2GYA8.
SMRiQ2GYA8. Positions 72-439.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi55 – 617Poly-Lys
Compositional biasi64 – 674Poly-Lys

Sequence similaritiesi

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

Phylogenomic databases

InParanoidiQ2GYA8.
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.

Q2GYA8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAQAPPTDE LSKLSVEDAD NKPQPDASNG NLNHDEDDSE DDAEDASAPA
60 70 80 90 100
AGGAKKKKKR KPRKKKKNPT QQSDPPRVLI SQLFPDKQYP KGEEVEYLNE
110 120 130 140 150
NSYRTTNEEK RHLDNLKSEF LNDYRHAAEA HRQVRQWAAK NIKPGQSLTD
160 170 180 190 200
IANGIEDSVR ALVGHQGLEE GDALIAGMGF PTGLSINHCA AHYTPNAGNK
210 220 230 240 250
MILQQDDVMK IDFGVQVNGN IVDSAFTMAF NPRYDPLLEA VKAATNAGIK
260 270 280 290 300
EAGIDVRLGE IGGVIQEVME SYEVEIDGTT YPVKPIRNLN GHTILPYNIH
310 320 330 340 350
GGKSVPIVKS NDTTKMEEGD VFAIETFGST GGGHVIEDGE VSHYAKRTDA
360 370 380 390 400
PKVDLRLSSA KSLLSVINKN FGTLPWCRRY LDRLGQEKYL LGLNNLVSNG
410 420 430
IVEAYPPLVD KKGSYTAQFE HTILIRPTVK EVISRGDDF
Length:439
Mass (Da):48,244
Last modified:March 21, 2006 - v1
Checksum:iE1E54ED5023BDB67
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH408033 Genomic DNA. Translation: EAQ85793.1.
RefSeqiXP_001224702.1. XM_001224701.1.

Genome annotation databases

GeneIDi4393147.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH408033 Genomic DNA. Translation: EAQ85793.1.
RefSeqiXP_001224702.1. XM_001224701.1.

3D structure databases

ProteinModelPortaliQ2GYA8.
SMRiQ2GYA8. Positions 72-439.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiM24.002.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi4393147.

Phylogenomic databases

InParanoidiQ2GYA8.
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]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970.

Entry informationi

Entry nameiMAP22_CHAGB
AccessioniPrimary (citable) accession number: Q2GYA8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: March 21, 2006
Last modified: January 7, 2015
This is version 54 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.