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.

C5JW60

- MAP21_AJEDS

UniProt

C5JW60 - MAP21_AJEDS

(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 2-1
Gene
BDBG_06837
Organism
Ajellomyces dermatitidis (strain SLH14081) (Blastomyces dermatitidis)
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 sitei196 – 1961Substrate By similarity
Metal bindingi216 – 2161Divalent metal cation 1 By similarity
Metal bindingi227 – 2271Divalent metal cation 1 By similarity
Metal bindingi227 – 2271Divalent metal cation 2; catalytic By similarity
Metal bindingi296 – 2961Divalent metal cation 2; catalytic; via tele nitrogen By similarity
Binding sitei304 – 3041Substrate By similarity
Metal bindingi332 – 3321Divalent metal cation 2; catalytic By similarity
Metal bindingi427 – 4271Divalent metal cation 1 By similarity
Metal bindingi427 – 4271Divalent 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:BDBG_06837
OrganismiAjellomyces dermatitidis (strain SLH14081) (Blastomyces dermatitidis)
Taxonomic identifieri559298 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesAjellomycetaceaeAjellomyces
ProteomesiUP000002038: 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 – 446446Methionine aminopeptidase 2-1UniRule annotation
PRO_0000407595Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliC5JW60.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi58 – 7417Lys-richUniRule annotation
Add
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.

C5JW60-1 [UniParc]FASTAAdd to Basket

« Hide

MAAQVTPELA NLNSKPEGGA PPKQVPVKDV PENEDVESDD DNEGDQGAGE    50
PGSTGAAKKK KKKKPKKKKK GGPKVQTEPP RVILSSIFPN NDYPVGELVE 100
YKDDNAYRTT NEEKRYLDRM NNDFLSEYRY AAEVHRQVRQ YAQKTIKPGQ 150
TLTEIAEGIE DSVRALTGHD GLTEGDNLLG GIAFPTGVNL NHCAAHYSPN 200
AGNKMVLQYE DVMKVDFGVH INGRIVDSAF TVAFDPVYDN LLAAVKDATN 250
TGIREAGIDV RMSDIGAAIQ ETMESYEVEI KGTTYPVKPI RNLNGHTIGQ 300
FEIHGGKNGK SVPIVKGGDQ SKMEEGEVYA IETFGSTGRG YVRDDMETSH 350
YAKVPDAPNV PLRLSSAKNL LNVITKNFGT LPFCRRYLDR LGQDKYLLGL 400
NNLVANGIVD AYPPLCDIKG SYTAQFEHTI LLRPNIKEVI SRGYDY 446
Length:446
Mass (Da):49,025
Last modified:July 28, 2009 - v1
Checksum:iAA100997CC8C860B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
GG657463 Genomic DNA. Translation: EEQ71844.1.
RefSeqiXP_002622719.1. XM_002622673.1.

Genome annotation databases

GeneIDi8502916.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
GG657463 Genomic DNA. Translation: EEQ71844.1 .
RefSeqi XP_002622719.1. XM_002622673.1.

3D structure databases

ProteinModelPortali C5JW60.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 8502916.

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. "The genome sequence of Blastomyces dermatitidis strain SLH14081."
    Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Klein B., Goldman B., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.M., Heiman D.I., Hepburn T.A., Saif S., Shea T.D., Shenoy N., Sykes S.
    , Galagan J.E., Nusbaum C., Birren B.W.
    Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: SLH14081.

Entry informationi

Entry nameiMAP21_AJEDS
AccessioniPrimary (citable) accession number: C5JW60
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: July 28, 2009
Last modified: May 14, 2014
This is version 30 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