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.

E5R4J3

- MAP22_LEPMJ

UniProt

E5R4J3 - MAP22_LEPMJ

(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
Lema_P046670
Organism
Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8) (Blackleg fungus) (Phoma lingam)
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 sitei204 – 2041Substrate By similarity
Metal bindingi224 – 2241Divalent metal cation 1 By similarity
Metal bindingi235 – 2351Divalent metal cation 1 By similarity
Metal bindingi235 – 2351Divalent metal cation 2; catalytic By similarity
Metal bindingi304 – 3041Divalent metal cation 2; catalytic; via tele nitrogen By similarity
Binding sitei312 – 3121Substrate By similarity
Metal bindingi337 – 3371Divalent metal cation 2; catalytic By similarity
Metal bindingi432 – 4321Divalent metal cation 1 By similarity
Metal bindingi432 – 4321Divalent 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:Lema_P046670
OrganismiLeptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8) (Blackleg fungus) (Phoma lingam)
Taxonomic identifieri985895 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaDothideomycetesPleosporomycetidaePleosporalesPleosporineaeLeptosphaeriaceaeLeptosphaeriaLeptosphaeria maculans complex
ProteomesiUP000002668: Whole genome

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 – 451451Methionine aminopeptidase 2-2UniRule annotationPRO_0000407607Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliE5R4J3.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi60 – 667Poly-LysUniRule annotation
Compositional biasi69 – 724Poly-LysUniRule annotation

Sequence similaritiesi

Phylogenomic databases

OMAiIQICEEL.
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.

E5R4J3-1 [UniParc]FASTAAdd to Basket

« Hide

MAAQVEDDVA NLKLDDSTTK PTNGTSQPDS KLSAEAEDSD DDAEGDGNGT    50
GEAGADGAAK KKKKRKPRKK KKAGTSATAG AKSQTSPPRV LISDLFPNDS 100
YPEGEICEYR DENSYRTTNE EKRHLDRMNN DFLTDYRKGA EIHRQVRQWA 150
ANWIKPGMTL TEIAEGIEDS VRALTGHQGL EEGDAQKAGM GFPTGLSINH 200
CAAHYTPNAG NKVVVNYEDV MKVDFGVHIN GRIVDSAFTK TFDPVYDPLV 250
EACKAATNAG IKEAGIDVRM SDIGAAIQEV MESYEVEIGG KMLPVKCIRN 300
LNGHSIGHYT IHGGKTVPIV KGSDQTKMEE GETFAIETFG STGKGYVRDD 350
METSHYALRP DAPKVALRIS SAKSLLASIT KNFGTLPFCR RYLDRLGHDK 400
YLLGLNNLVS SGIVEAYPPL CDIKGSWTAQ SEHTFVLRPT CKEVLSRGDD 450
Y 451
Length:451
Mass (Da):49,158
Last modified:February 8, 2011 - v1
Checksum:i08407BBF6A063CA3
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
FP929083 Genomic DNA. Translation: CBX91961.1.
RefSeqiXP_003835326.1. XM_003835278.1.

Genome annotation databases

EnsemblFungiiCBX91961; CBX91961; LEMA_P046670.1.
GeneIDi13284777.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
FP929083 Genomic DNA. Translation: CBX91961.1 .
RefSeqi XP_003835326.1. XM_003835278.1.

3D structure databases

ProteinModelPortali E5R4J3.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CBX91961 ; CBX91961 ; LEMA_P046670.1 .
GeneIDi 13284777.

Phylogenomic databases

OMAi IQICEEL.
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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8.

Entry informationi

Entry nameiMAP22_LEPMJ
AccessioniPrimary (citable) accession number: E5R4J3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: February 8, 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