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C5GLJ6

- MAP22_AJEDR

UniProt

C5GLJ6 - MAP22_AJEDR

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Protein

Methionine aminopeptidase 2-2

Gene

BDCG_05228

Organism
Ajellomyces dermatitidis (strain ER-3 / ATCC MYA-2586) (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).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 Fe(2+)-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 sitei216 – 2161SubstrateUniRule annotation
Metal bindingi237 – 2371Divalent metal cation 1UniRule annotation
Metal bindingi248 – 2481Divalent metal cation 1UniRule annotation
Metal bindingi248 – 2481Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi317 – 3171Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
Binding sitei325 – 3251SubstrateUniRule annotation
Metal bindingi350 – 3501Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi445 – 4451Divalent metal cation 1UniRule annotation
Metal bindingi445 – 4451Divalent 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

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:BDCG_05228
OrganismiAjellomyces dermatitidis (strain ER-3 / ATCC MYA-2586) (Blastomyces dermatitidis)
Taxonomic identifieri559297 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesAjellomycetaceaeAjellomyces
ProteomesiUP000002039: Unassembled WGS sequence

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 464464Methionine aminopeptidase 2-2PRO_0000407616Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliC5GLJ6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi71 – 8414Lys-richAdd
BLAST

Sequence similaritiesi

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

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.

C5GLJ6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGSKTPNDHR RGPNESSPHA AIDTINPPKH AAASGLLHGP LEGETEDGED
60 70 80 90 100
EDDDKTGADL KSVGQLNNST KKKNKRKKNK KKKKTLLGGL QTTPPRVALS
110 120 130 140 150
SIFYDQRYPE AEIVGYTTNN DNLQRITAEE FRHLCVVNDM DDEFLNDYRK
160 170 180 190 200
AAEVHRQVRQ YVQTITKPGI AMSQLAQEIE DGVRALTDHQ GIETGDALKA
210 220 230 240 250
GMAFPTGLCL NNIGAHWTPN PGAKEVILQY DDVLKVDFGV HVNGRIVDSA
260 270 280 290 300
YTMAFNPVYD DLLTAVKAAT NTGLKEAGID ARIDCISEAI QEVMESYEVE
310 320 330 340 350
LNRKIIPVKA VRNITGHNIL RYKIHGDKQV PFVKTHTNQR MEEGDIFAIE
360 370 380 390 400
TFGSTGKAYL DDDIGIYGYF CDEHASAAGL HHSSAKSLLK TIKDNFGTLV
410 420 430 440 450
FSRRYLERLG VKSYHLGMRS LVSKGIVQSY APLVDVPGSY VAQFEHTVLL
460
RPNCKEVISR GDDY
Length:464
Mass (Da):51,414
Last modified:July 28, 2009 - v1
Checksum:iE914113CB23390D3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EQ999977 Genomic DNA. Translation: EEQ90108.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EQ999977 Genomic DNA. Translation: EEQ90108.1 .

3D structure databases

ProteinModelPortali C5GLJ6.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

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. "The genome sequence of Blastomyces dermatitidis strain ER-3."
    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: ER-3 / ATCC MYA-2586.

Entry informationi

Entry nameiMAP22_AJEDR
AccessioniPrimary (citable) accession number: C5GLJ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: July 28, 2009
Last modified: November 26, 2014
This is version 34 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