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Protein

Methionine aminopeptidase 2-1

Gene

TSTA_071420

Organism
Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006) (Penicillium stipitatum)
Status
Reviewed-Annotation score: 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 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 sitei196 – 1961SubstrateUniRule annotation
Metal bindingi216 – 2161Divalent metal cation 1UniRule annotation
Metal bindingi227 – 2271Divalent metal cation 1UniRule annotation
Metal bindingi227 – 2271Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi296 – 2961Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
Binding sitei304 – 3041SubstrateUniRule annotation
Metal bindingi329 – 3291Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi424 – 4241Divalent metal cation 1UniRule annotation
Metal bindingi424 – 4241Divalent metal cation 2; catalyticUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease

Keywords - Ligandi

Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Methionine aminopeptidase 2-1UniRule annotation (EC:3.4.11.18UniRule annotation)
Short name:
MAP 2-1UniRule annotation
Short name:
MetAP 2-1UniRule annotation
Alternative name(s):
Peptidase MUniRule annotation
Gene namesi
ORF Names:TSTA_071420
OrganismiTalaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006) (Penicillium stipitatum)
Taxonomic identifieri441959 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesTrichocomaceaeTalaromyces
ProteomesiUP000001745 Componenti: Unassembled WGS sequence

Organism-specific databases

EuPathDBiFungiDB:TSTA_071420.

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 443443Methionine aminopeptidase 2-1PRO_0000407614Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliB8LUH2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi58 – 7518Lys-richAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

InParanoidiB8LUH2.
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.

B8LUH2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAQADDELN KLRLNGQNGE AKEQVSASAV DTADNDDSED DEKEEEGGAE
60 70 80 90 100
VAATEAAKKK KKRKPKKKKK GGAKKQSSPP RVPVSELFPN NQYPEGEIVE
110 120 130 140 150
YKDENNYRTT NEEKRYLDRM NNDFLQEYRQ GAEVHRQVRQ YAQKNIKPGQ
160 170 180 190 200
TLTEIAEGIE DAVRALTGHQ GLEEGDNIKG GMGFPCGLSI NHCAAHYTPN
210 220 230 240 250
AGNKMVLQQG DVMKVDFGAH INGRIVDSAF TMTFDPVYDN LLTAVKEATN
260 270 280 290 300
TGIREAGIDV RMSDIGAAIQ EVMESYEVEI NGTTYPVKAI RNLNGHNIDQ
310 320 330 340 350
HVIHGGKSVP IVKGGDQTKM EEGEVFAIET FGSTGKGYVR EDMETSHYAK
360 370 380 390 400
AQDAPNVSLR LSSAKNLLNV INKNFGTLPF CRRYLDRLGQ DKYLLGLNNL
410 420 430 440
VSAGIVQDYP PLCDIKGSYT AQYEHTIVLR PTVKEVISRG DDY
Length:443
Mass (Da):48,965
Last modified:March 3, 2009 - v1
Checksum:i9838CC94CA68A14A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EQ962652 Genomic DNA. Translation: EED23745.1.
RefSeqiXP_002341132.1. XM_002341091.1.

Genome annotation databases

GeneIDi8102525.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EQ962652 Genomic DNA. Translation: EED23745.1.
RefSeqiXP_002341132.1. XM_002341091.1.

3D structure databases

ProteinModelPortaliB8LUH2.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi8102525.

Organism-specific databases

EuPathDBiFungiDB:TSTA_071420.

Phylogenomic databases

InParanoidiB8LUH2.
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]
ProtoNetiSearch...

Publicationsi

  1. "Genome sequence of Talaromyces stipitatus strain ATCC 10500."
    Fedorova N.D., Joardar V.S., Maiti R., Schobel S., Amedeo P., Galens K., Inman J.M., Galinsky K.J., White O.R., Whitty B.R., Wortman J.R., Nierman W.C.
    Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006.

Entry informationi

Entry nameiMAP21_TALSN
AccessioniPrimary (citable) accession number: B8LUH2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: March 3, 2009
Last modified: April 29, 2015
This is version 36 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.