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E3QDQ4

- MAP21_COLGM

UniProt

E3QDQ4 - MAP21_COLGM

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Protein

Methionine aminopeptidase 2-1

Gene
GLRG_04136
Organism
Colletotrichum graminicola (strain M1.001 / M2 / FGSC 10212) (Maize anthracnose fungus) (Glomerella graminicola)
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 sitei214 – 2141Substrate By similarity
Metal bindingi235 – 2351Divalent metal cation 1 By similarity
Metal bindingi246 – 2461Divalent metal cation 1 By similarity
Metal bindingi246 – 2461Divalent metal cation 2; catalytic By similarity
Metal bindingi315 – 3151Divalent metal cation 2; catalytic; via tele nitrogen By similarity
Binding sitei323 – 3231Substrate By similarity
Metal bindingi348 – 3481Divalent metal cation 2; catalytic By similarity
Metal bindingi444 – 4441Divalent metal cation 1 By similarity
Metal bindingi444 – 4441Divalent 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:GLRG_04136
OrganismiColletotrichum graminicola (strain M1.001 / M2 / FGSC 10212) (Maize anthracnose fungus) (Glomerella graminicola)
Taxonomic identifieri645133 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeGlomerellalesGlomerellaceaemitosporic GlomerellaceaeColletotrichum
ProteomesiUP000008782: 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 – 463463Methionine aminopeptidase 2-1UniRule annotationPRO_0000407627Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliE3QDQ4.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi68 – 725Poly-LysUniRule annotation
Compositional biasi75 – 795Poly-LysUniRule annotation

Sequence similaritiesi

Phylogenomic databases

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.

E3QDQ4-1 [UniParc]FASTAAdd to Basket

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MGSKTPEEQI PGGNGGPPST GPSSSGGEPR GTHLSRDGDG SLGDHGDDDD    50
ADEDDVSSRP LRADVEEKKK KKRPKKKKKP AAAKEQSSPP RVPLSDLFPL 100
GEYPAGEDLV YDRVPQPDAN TARTTTAELR YQSRKHLEDP ALLNDYRKAA 150
EVHRQVRHWV QEAVKPGWTL LDIATGIEDG VRSLLANQGI EPGDNLRSGM 200
GFPTGLCLNH ETAHYTPNPG QRDVVLQHGD VMKVDYGVQV NGWIVDSAFT 250
MSFDPTYDNL LAAARDATNS GIKAAGIDVR ICDVSAEIQE AMESYEVEIR 300
GKTYPVKAVR NICAHDIKRY RIHGGKSIPF IRNNDQTKME EGEIFAIETF 350
GTTGRGKLYD DIGVYGYGLL HDAPAQVRLP FASANRLCKT IKEQFGSIVF 400
CRRYLDRLGL DRYLAGLNCL VSHGVLESYA PLADIKGSYT SQFEHTILLR 450
ESSKEIVSRG SDY 463
Length:463
Mass (Da):50,912
Last modified:January 11, 2011 - v1
Checksum:i02C808D4B6DD28F2
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
GG697343 Genomic DNA. Translation: EFQ28992.1.

Genome annotation databases

EnsemblFungiiEFQ28992; EFQ28992; GLRG_04136.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
GG697343 Genomic DNA. Translation: EFQ28992.1 .

3D structure databases

ProteinModelPortali E3QDQ4.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii EFQ28992 ; EFQ28992 ; GLRG_04136 .

Phylogenomic databases

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. "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered by genome and transcriptome analyses."
    O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J., Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J., Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z., Choi J., Crouch J.A.
    , Duvick J.P., Farman M.A., Gan P., Heiman D., Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y., Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U., Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H., Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L., Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K., Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F., van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J., Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E., Ma L.-J., Vaillancourt L.J.
    Nat. Genet. 44:1060-1065(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: M1.001 / M2 / FGSC 10212.

Entry informationi

Entry nameiMAP21_COLGM
AccessioniPrimary (citable) accession number: E3QDQ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: January 11, 2011
Last modified: June 11, 2014
This is version 22 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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