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Q5BGG1

- MAP22_EMENI

UniProt

Q5BGG1 - MAP22_EMENI

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Protein
Methionine aminopeptidase 2-2
Gene
AN0369
Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
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 sitei209 – 2091Substrate By similarity
Metal bindingi230 – 2301Divalent metal cation 1 By similarity
Metal bindingi241 – 2411Divalent metal cation 1 By similarity
Metal bindingi241 – 2411Divalent metal cation 2; catalytic By similarity
Metal bindingi310 – 3101Divalent metal cation 2; catalytic; via tele nitrogen By similarity
Binding sitei318 – 3181Substrate By similarity
Metal bindingi343 – 3431Divalent metal cation 2; catalytic By similarity
Metal bindingi439 – 4391Divalent metal cation 1 By similarity
Metal bindingi439 – 4391Divalent metal cation 2; catalytic By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-HAMAP
  2. metalloaminopeptidase activity Source: UniProtKB-HAMAP
Complete GO annotation...

GO - Biological processi

  1. protein initiator methionine removal Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease

Keywords - Ligandi

Metal-binding

Protein family/group databases

MEROPSiM24.002.

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:AN0369
OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic identifieri227321 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000000560: Chromosome VIII

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 – 458458Methionine aminopeptidase 2-2UniRule annotation
PRO_0000407628Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi162425.CADANIAP00002334.

Structurei

3D structure databases

ProteinModelPortaliQ5BGG1.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0024.
HOGENOMiHOG000226278.
KOiK01265.
OMAiNNCVAHY.
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.

Q5BGG1-1 [UniParc]FASTAAdd to Basket

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MGSKTPERDG HKGQENTTGP VECPLGGMPR GMHLATDGDG TIGDSGDDDD    50
GEAHSTALIN ANANGNQKKK RKSKKKGKKK AAKQSSPPRV PLSQLFLQGK 100
YPIGEVQEYQ PNVENTSRTT AEEVRYKSRS HLEDDSFLND YRKAAEVHRQ 150
VRKWTQERVK PGQGLMEIAE DIDDGVRALL GHAGLEPGDS LKAGLGFPTG 200
LSLNNVVAHY TPNPGQKDII LQSSDVMKVD FGVHINGWIV DSAFTMTFDP 250
VYDNLLAAVK DATNAGLKTA GIDVRISDVS AAIQEAMESY EVEIGGKTFP 300
VKAVRNITGH NIKHYQIHGG KSVPFVKNSD QTKMEEGEIF AIETFGSTGR 350
GYIYDDVGVY GYGKSYDAPR QVSLPLASAR SLYKTINENF GTIVFCRRYL 400
DRLGLQRYLA GMNTLVQHGV VDVYAPLVDI KGSYSAQFEH TVLLRESNKE 450
VISRGDDY 458
Length:458
Mass (Da):50,186
Last modified:May 3, 2011 - v2
Checksum:i79A7211808B75D0E
GO

Sequence cautioni

The sequence EAA65775.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AACD01000006 Genomic DNA. Translation: EAA65775.1. Sequence problems.
BN001308 Genomic DNA. Translation: CBF89626.1.
RefSeqiXP_657973.1. XM_652881.1.

Genome annotation databases

EnsemblFungiiCADANIAT00002334; CADANIAP00002334; CADANIAG00002334.
GeneIDi2876145.
KEGGiani:AN0369.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AACD01000006 Genomic DNA. Translation: EAA65775.1 . Sequence problems.
BN001308 Genomic DNA. Translation: CBF89626.1 .
RefSeqi XP_657973.1. XM_652881.1.

3D structure databases

ProteinModelPortali Q5BGG1.
ModBasei Search...

Protein-protein interaction databases

STRINGi 162425.CADANIAP00002334.

Protein family/group databases

MEROPSi M24.002.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADANIAT00002334 ; CADANIAP00002334 ; CADANIAG00002334 .
GeneIDi 2876145.
KEGGi ani:AN0369.2.

Phylogenomic databases

eggNOGi COG0024.
HOGENOMi HOG000226278.
KOi K01265.
OMAi NNCVAHY.
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

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
  2. "The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
    Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G.
    , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
    Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENOME REANNOTATION.
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.

Entry informationi

Entry nameiMAP22_EMENI
AccessioniPrimary (citable) accession number: Q5BGG1
Secondary accession number(s): C8VTR8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: May 3, 2011
Last modified: June 11, 2014
This is version 66 of the entry and version 2 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

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