SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q7S7L7

- MAP2_NEUCR

UniProt

Q7S7L7 - MAP2_NEUCR

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Methionine aminopeptidase 2
Gene
B7H23.090, NCU04306
Organism
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
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 sitei190 – 1901Substrate By similarity
Metal bindingi210 – 2101Divalent metal cation 1 By similarity
Metal bindingi221 – 2211Divalent metal cation 1 By similarity
Metal bindingi221 – 2211Divalent metal cation 2; catalytic By similarity
Metal bindingi290 – 2901Divalent metal cation 2; catalytic; via tele nitrogen By similarity
Binding sitei298 – 2981Substrate By similarity
Metal bindingi323 – 3231Divalent metal cation 2; catalytic By similarity
Metal bindingi418 – 4181Divalent metal cation 1 By similarity
Metal bindingi418 – 4181Divalent 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 involved in protein maturation Source: EnsemblFungi
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 (EC:3.4.11.18)
Short name:
MAP 2
Short name:
MetAP 2
Alternative name(s):
Peptidase M
Gene namesi
ORF Names:B7H23.090, NCU04306
OrganismiNeurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Taxonomic identifieri367110 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeNeurospora
ProteomesiUP000001805: Chromosome 2, Linkage Group V

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 – 437437Methionine aminopeptidase 2UniRule annotation
PRO_0000407658Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi5141.NCU04306.1.

Structurei

3D structure databases

ProteinModelPortaliQ7S7L7.
SMRiQ7S7L7. Positions 69-437.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi53 – 6513Lys-richUniRule annotation
Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0024.
HOGENOMiHOG000226278.
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.

Q7S7L7-1 [UniParc]FASTAAdd to Basket

« Hide

MAAQAAPAEE LSKLSVDETK PAPAAANGND SDAESGDEEA EEGAAAPAAG    50
AAKKKKKRKP KKKKKAPTSQ SEPPRVLVSQ LFPNNQYPKG EEVEYVNDNL 100
NRVTNEEKRH LDNLNQEFLT DYRHAAEVHR QVRQWAQKSI KPGQTLTEIA 150
ENIEDSVRAL TGHSGLEEGD ALIAGMGFPT GLSINHCAAH YTPNAGNKMV 200
LQEDDVMKVD FGVHVNGRIV DSAFTVAFNP RYDPLLEAVK AATNAGIKEA 250
GIDVRVGDIG AAIQEVMESY EVEINGQMLP VKSIRNLNGH TINHYSIHGT 300
KSVPIVKSND QTKMEEGDVF AIETFGSTGN GYVHEEGEVS HYAKRGDAAK 350
VDLRLSSAKS LLNVITKNFG TLPFCRRYID RLGQDKYLLG LNNLVSQGIV 400
EAYPPLVDKK GSYTAQYEHT ILLRPTVKEV ISRGDDF 437
Length:437
Mass (Da):47,731
Last modified:May 3, 2011 - v2
Checksum:iCEEE909DE0816003
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX294026 Genomic DNA. Translation: CAD71035.1.
CM002240 Genomic DNA. Translation: EAA31716.2.
RefSeqiXP_960952.1. XM_955859.1.
UniGeneiNcr.25108.

Genome annotation databases

EnsemblFungiiEFNCRT00000003758; EFNCRP00000003758; EFNCRG00000003754.
GeneIDi3877118.
KEGGincr:NCU04306.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX294026 Genomic DNA. Translation: CAD71035.1 .
CM002240 Genomic DNA. Translation: EAA31716.2 .
RefSeqi XP_960952.1. XM_955859.1.
UniGenei Ncr.25108.

3D structure databases

ProteinModelPortali Q7S7L7.
SMRi Q7S7L7. Positions 69-437.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 5141.NCU04306.1.

Protein family/group databases

MEROPSi M24.002.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii EFNCRT00000003758 ; EFNCRP00000003758 ; EFNCRG00000003754 .
GeneIDi 3877118.
KEGGi ncr:NCU04306.

Phylogenomic databases

eggNOGi COG0024.
HOGENOMi HOG000226278.
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. "What's in the genome of a filamentous fungus? Analysis of the Neurospora genome sequence."
    Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D., Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.
    Nucleic Acids Res. 31:1944-1954(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.
  2. "The genome sequence of the filamentous fungus Neurospora crassa."
    Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D.
    , Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.
    Nature 422:859-868(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.

Entry informationi

Entry nameiMAP2_NEUCR
AccessioniPrimary (citable) accession number: Q7S7L7
Secondary accession number(s): Q871H0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: May 3, 2011
Last modified: May 14, 2014
This is version 79 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

Similar proteinsi