SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

E3QW41

- MAP22_COLGM

UniProt

E3QW41 - MAP22_COLGM

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Methionine aminopeptidase 2-2

Gene
GLRG_10223
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 sitei194 – 1941Substrate By similarity
Metal bindingi214 – 2141Divalent metal cation 1 By similarity
Metal bindingi225 – 2251Divalent metal cation 1 By similarity
Metal bindingi225 – 2251Divalent metal cation 2; catalytic By similarity
Metal bindingi294 – 2941Divalent metal cation 2; catalytic; via tele nitrogen By similarity
Binding sitei302 – 3021Substrate By similarity
Metal bindingi327 – 3271Divalent metal cation 2; catalytic By similarity
Metal bindingi421 – 4211Divalent metal cation 1 By similarity
Metal bindingi421 – 4211Divalent 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 2-2 (EC:3.4.11.18)
Short name:
MAP 2-2
Short name:
MetAP 2-2
Alternative name(s):
Peptidase M
Gene namesi
ORF Names:GLRG_10223
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 – 440440Methionine aminopeptidase 2-2UniRule annotationPRO_0000407605Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliE3QW41.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi57 – 6913Lys-richUniRule annotationAdd
BLAST

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]
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.

E3QW41-1 [UniParc]FASTAAdd to Basket

« Hide

MAAQVPTEAL KELNVGGPAT NDKAANPTEG NGVDHDSDDS DEEGEEVAAP    50
AAGGAAKKKK KNKKKKKKKS PTAQSDPPRV LMSSLFPNKN YPKGQEEEYR 100
DENLYRTTNE EKRHLDNLNN DFLTDYREAA EIHRQVRQWA QKNIKPGQTL 150
TEIAEGIEDG VRALTGHPGI EEGDAYKGGM GFPCGLSLNH CAAHYTPNAG 200
NKMVLSQGDV MKVDFGVHVN GRIVDSAFTM AFEPQYDNLL AAVKDATNAG 250
VKEAGIDVRV GDVGGVIQEV MESYEVEIDG TTYPVKSIRN LNGHTIERWS 300
IHGTKSVPIV KSNDTTKMEE GDVFAVETFG STGNGFVRED MEVSHYAKRG 350
EGHAALRLDS AKRLLNVINK NFGTLPFCRR YLDRLGQDKY LLGLNNLVSS 400
GIVEAYPPLC DKKGSYTAQF EHTILLRPTV KEVISRGDDY 440
Length:440
Mass (Da):48,286
Last modified:January 11, 2011 - v1
Checksum:i7303EE074317C86B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
GG697387 Genomic DNA. Translation: EFQ35079.1.

Genome annotation databases

EnsemblFungiiEFQ35079; EFQ35079; GLRG_10223.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
GG697387 Genomic DNA. Translation: EFQ35079.1 .

3D structure databases

ProteinModelPortali E3QW41.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii EFQ35079 ; EFQ35079 ; GLRG_10223 .

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 ]
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. "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 nameiMAP22_COLGM
AccessioniPrimary (citable) accession number: E3QW41
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: January 11, 2011
Last modified: May 14, 2014
This is version 21 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

Similar proteinsi