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C4Y1F8

- MAP2_CLAL4

UniProt

C4Y1F8 - MAP2_CLAL4

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Protein

Methionine aminopeptidase 2

Gene
MAP2, CLUG_02040
Organism
Clavispora lusitaniae (strain ATCC 42720) (Yeast) (Candida lusitaniae)
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 sitei188 – 1881Substrate By similarity
Metal bindingi208 – 2081Divalent metal cation 1 By similarity
Metal bindingi219 – 2191Divalent metal cation 1 By similarity
Metal bindingi219 – 2191Divalent metal cation 2; catalytic By similarity
Metal bindingi288 – 2881Divalent metal cation 2; catalytic; via tele nitrogen By similarity
Binding sitei296 – 2961Substrate By similarity
Metal bindingi321 – 3211Divalent metal cation 2; catalytic By similarity
Metal bindingi416 – 4161Divalent metal cation 1 By similarity
Metal bindingi416 – 4161Divalent 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 (EC:3.4.11.18)
Short name:
MAP 2
Short name:
MetAP 2
Alternative name(s):
Peptidase M
Gene namesi
Name:MAP2
ORF Names:CLUG_02040
OrganismiClavispora lusitaniae (strain ATCC 42720) (Yeast) (Candida lusitaniae)
Taxonomic identifieri306902 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesMetschnikowiaceaeClavispora
ProteomesiUP000007703: 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 – 435435Methionine aminopeptidase 2UniRule annotationPRO_0000407649Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliC4Y1F8.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi66 – 7611Poly-LysUniRule annotationAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

KOiK01265.
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.

C4Y1F8-1 [UniParc]FASTAAdd to Basket

« Hide

MASAQTGTEM SPHHVTRTYK HENFLSFIST MSEKETVETT QEPKQVVEPT    50
QELEELAIDG DQAAAKKKKS KKKKKKAVSL DKTYADGVFP EGQWMEYPLE 100
VNSYRTTDEE KRYLDRQQNN HWQDFRKGAE VHRRVRQKAQ QQIKPGMTML 150
EIADLIENSI RTYTGNDHTL KQGIGFPTGL SLNHVAAHYT PNSNDKVVLK 200
YEDVMKVDIG VHVNGHIVDS AFTLTFDDKY DNLLTAVREA TYTGVKEAGI 250
DVRLNDIGAA VQEVMESYEV ELDGKTYPVK CIRNLNGHNI GDYVIHSGKT 300
VPIVANGDMT KMEEGETFAI ETFGTTGKGY VIPQGECSHY ALNQDIDGVK 350
LPSERAKSLV KSIKDNFGTL PWCRRYLERA GEDKYLLALN QLVRAGVVED 400
YPPLVDTSGS YTAQYEHTIL LHPHKKEVVS KGDDY 435
Length:435
Mass (Da):49,011
Last modified:July 28, 2009 - v1
Checksum:iAE5C51425D0A0E77
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CH408077 Genomic DNA. Translation: EEQ37917.1.
RefSeqiXP_002618581.1. XM_002618535.1.

Genome annotation databases

GeneIDi8498874.
KEGGiclu:CLUG_02040.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CH408077 Genomic DNA. Translation: EEQ37917.1 .
RefSeqi XP_002618581.1. XM_002618535.1.

3D structure databases

ProteinModelPortali C4Y1F8.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 8498874.
KEGGi clu:CLUG_02040.

Phylogenomic databases

KOi K01265.
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: ATCC 42720.

Entry informationi

Entry nameiMAP2_CLAL4
AccessioniPrimary (citable) accession number: C4Y1F8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: July 28, 2009
Last modified: May 14, 2014
This is version 31 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

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