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Q6BVB8

- MAP2_DEBHA

UniProt

Q6BVB8 - MAP2_DEBHA

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Protein

Methionine aminopeptidase 2

Gene

MAP2

Organism
Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii)
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

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.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei172 – 1721SubstrateUniRule annotation
Metal bindingi192 – 1921Divalent metal cation 1UniRule annotation
Metal bindingi203 – 2031Divalent metal cation 1UniRule annotation
Metal bindingi203 – 2031Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi272 – 2721Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
Binding sitei280 – 2801SubstrateUniRule annotation
Metal bindingi305 – 3051Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi400 – 4001Divalent metal cation 1UniRule annotation
Metal bindingi400 – 4001Divalent 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

Protein family/group databases

MEROPSiM24.002.

Names & Taxonomyi

Protein namesi
Recommended name:
Methionine aminopeptidase 2UniRule annotation (EC:3.4.11.18UniRule annotation)
Short name:
MAP 2UniRule annotation
Short name:
MetAP 2UniRule annotation
Alternative name(s):
Peptidase MUniRule annotation
Gene namesi
Name:MAP2UniRule annotation
Ordered Locus Names:DEHA2C03894g
OrganismiDebaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii)
Taxonomic identifieri284592 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeDebaryomyces
ProteomesiUP000000599: Chromosome C

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 – 419419Methionine aminopeptidase 2PRO_0000407651Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi4959.Q6BVB8.

Structurei

3D structure databases

ProteinModelPortaliQ6BVB8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi48 – 6013Lys-richAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0024.
HOGENOMiHOG000226278.
InParanoidiQ6BVB8.
KOiK01265.
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.

Q6BVB8-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSTNSSNPNE VMEKVQDLKI DDSKPKVDSE EQPEAESDGE SATDGAQKKK
60 70 80 90 100
KKKKSKKKKK ITAIDNSYPD GVFPEGEWQE YPLDVNSYRT TSEEKRYLDR
110 120 130 140 150
QQNNHWQDFR KGAEIHRRVR HKAQSSIRPG MNMTEIADLI ENSVRSYANN
160 170 180 190 200
DHTLKAGIGF PTGLSLNHVA AHYTPNAGDK TVLNYEDVMK VDIGVHVNGH
210 220 230 240 250
IVDSAFTLTF DDKYDSLLKA VKEATNTGVK EAGIDVRLND IGEAIQEVME
260 270 280 290 300
SYEMELNGKT YPIKCIRNLN GHNIGDYLIH SGKTVPIVPN GDMTKMEEGE
310 320 330 340 350
TFAIETFGST GNGYVLPQGE CSHYAKNPGT DDIVVPGDKA KSLLNVINEN
360 370 380 390 400
FGTLPWCRRY LDRLGQDKYL LALNQLVRAG IVQDYPPIVD IKGSYTAQFE
410
HTILLHPHKK EVVSRGDDY
Length:419
Mass (Da):46,948
Last modified:November 4, 2008 - v2
Checksum:iFF3366D553F7D758
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR382135 Genomic DNA. Translation: CAG85896.2.
RefSeqiXP_457851.2. XM_457851.1.

Genome annotation databases

GeneIDi2900504.
KEGGidha:DEHA2C03894g.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR382135 Genomic DNA. Translation: CAG85896.2 .
RefSeqi XP_457851.2. XM_457851.1.

3D structure databases

ProteinModelPortali Q6BVB8.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 4959.Q6BVB8.

Protein family/group databases

MEROPSi M24.002.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 2900504.
KEGGi dha:DEHA2C03894g.

Phylogenomic databases

eggNOGi COG0024.
HOGENOMi HOG000226278.
InParanoidi Q6BVB8.
KOi K01265.
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...

Entry informationi

Entry nameiMAP2_DEBHA
AccessioniPrimary (citable) accession number: Q6BVB8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: November 4, 2008
Last modified: October 29, 2014
This is version 70 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