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B8M990

- MAP22_TALSN

UniProt

B8M990 - MAP22_TALSN

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Protein
Methionine aminopeptidase 2-2
Gene
TSTA_112180
Organism
Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006) (Penicillium stipitatum)
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 sitei216 – 2161Substrate By similarity
Metal bindingi237 – 2371Divalent metal cation 1 By similarity
Metal bindingi248 – 2481Divalent metal cation 1 By similarity
Metal bindingi248 – 2481Divalent metal cation 2; catalytic By similarity
Metal bindingi317 – 3171Divalent metal cation 2; catalytic; via tele nitrogen By similarity
Binding sitei325 – 3251Substrate By similarity
Metal bindingi350 – 3501Divalent metal cation 2; catalytic By similarity
Metal bindingi445 – 4451Divalent metal cation 1 By similarity
Metal bindingi445 – 4451Divalent 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 2-2 (EC:3.4.11.18)
Short name:
MAP 2-2
Short name:
MetAP 2-2
Alternative name(s):
Peptidase M
Gene namesi
ORF Names:TSTA_112180
OrganismiTalaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006) (Penicillium stipitatum)
Taxonomic identifieri441959 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesTrichocomaceaeTalaromyces
ProteomesiUP000001745: 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 – 464464Methionine aminopeptidase 2-2UniRule annotation
PRO_0000407636Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliB8M990.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi69 – 8517Lys-richUniRule annotation
Add
BLAST

Sequence similaritiesi

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.

B8M990-1 [UniParc]FASTAAdd to Basket

« Hide

MGAKTYEGGD HHEDATNVLS TKSNAVGGKP RGANMLEDGD GEFGSDDDDD    50
GGDGQDSSLA MVNPDDAAKP KKKKRSKKKK NNKKKSGAGA QRQTSPPRVP 100
LSQLFPDGKY PIGQMVEVQD ENLRRTTDEE FRYLSRGTIT DDEALNDYRK 150
AAEVHRQVRR WIHETIQPGS SLTELAVGIE DGVRALLEHQ GLEPGDSLKG 200
GMGFPTGLAL NNCAAHYTPN PGQKDIILKT DDVLKIDFGV HVNGWIVDSA 250
FTVTFDPVYD NLVAAVKDAT NTGLKCAGVD ARVGEIGGFI QEAMESYEVE 300
INGKVYPVKS IRSITGHDIL RYRVHGGKQV PFVKSNDQTK MEEGEVFAIE 350
TFGSTGKGYL RDGPGVYGYS KEPHAGNVHL PLASARALLK TINQNFGTIP 400
FCRRYLDRLG IEKYLLGMNS LISHGIVQMY PPLVDIAGSY TAQFEHTILI 450
NSSGNEIISR GDDY 464
Length:464
Mass (Da):50,618
Last modified:March 3, 2009 - v1
Checksum:i8C7B0975724386EC
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
EQ962655 Genomic DNA. Translation: EED17385.1.
RefSeqiXP_002481377.1. XM_002481332.1.

Genome annotation databases

GeneIDi8098873.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
EQ962655 Genomic DNA. Translation: EED17385.1 .
RefSeqi XP_002481377.1. XM_002481332.1.

3D structure databases

ProteinModelPortali B8M990.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 8098873.

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. "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 nameiMAP22_TALSN
AccessioniPrimary (citable) accession number: B8M990
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: March 3, 2009
Last modified: June 11, 2014
This is version 32 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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