Q55C21 (AMPM2_DICDI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Methionine aminopeptidase 2
Short name=MAP 2
Short name=MetAP 2
EC=3.4.11.18

Alternative name(s):
Peptidase M 2

Gene names

Name:	metap2
ORF Names:	DDB_G0270264

Organism

Dictyostelium discoideum (Slime mold)

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	436 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Removes the amino-terminal methionine from nascent proteins By similarity.
Catalytic activity	Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.
Cofactor	Binds 2 cobalt ions per subunit. The true nature of the physiological cofactor is under debate. The enzyme is also active with zinc, manganese or divalent iron ions By similarity.
Sequence similarities	Belongs to the peptidase M24A family.

Ontologies

Keywords
Ligand	Cobalt Metal-binding
Molecular function	Aminopeptidase Hydrolase Protease
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cellular process Inferred from electronic annotation. Source: InterPro proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	phagocytic vesicle Inferred from direct assay. Source: dictyBase
Molecular function	aminopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW metalloexopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 436	436	Methionine aminopeptidase 2		PRO_0000328464
Regions
	Compositional bias	16 – 20	5	Poly-Glu
	Compositional bias	44 – 55	12	Poly-Lys
Sites
	Metal binding	211	1	Cobalt 1 By similarity
	Metal binding	222	1	Cobalt 1 By similarity
	Metal binding	222	1	Cobalt 2 By similarity
	Metal binding	291	1	Cobalt 2 By similarity
	Metal binding	324	1	Cobalt 2 By similarity
	Metal binding	417	1	Cobalt 1 By similarity
	Metal binding	417	1	Cobalt 2 By similarity
	Binding site	191	1	Substrate By similarity
	Binding site	299	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q55C21 [UniParc]. Last modified July 28, 2009. Version 3. Checksum: 586AE79EF89454CF	FASTA	436	48,561
	10 20 30 40 50 60 MSEIQPKTEV PPKTVEEEEE SDDEEDNTKV TEGGNPTGGE GAAKKKKKKN KKKKKAAPVA 70 80 90 100 110 120 SAADIIDSKP IPSGLVQTNP PTIPVSKQFS NGVYPMGEIQ EYRDSNSYRT TSEEKRLEER 130 140 150 160 170 180 IHANIYNDVR RAAEVHRQVR KYVQGIVKPG LGLTELVESL ENASRTLIEA DGLKAGIAFP 190 200 210 220 230 240 TGVSLNHIAA HFTPNTGDKT VLKKDDVLKI DFGTHVNGYI IDCAFTVTFD EKYDKLKDAV 250 260 270 280 290 300 REATNTGIYH AGIDARLGEI GAAIQEVMES HEIELNGKTY PIRSIRNLNG HSIRPYVIHG 310 320 330 340 350 360 GKTVPIVRGG EMTKMEEGEF YAIETFGSTG RAQVIEDLEC SHYMKTDYQT TVRLPKAKQL 370 380 390 400 410 420 LQYINKNYDT LCFCRRWLDR AGEDKHILAL NNLCDLGIIQ RHAPLVDSKG SYVAQYEHTL 430 LLKPTAKEVL SRGDDY

References

[1]

"The genome of the social amoeba Dictyostelium discoideum." Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A. Nature 435:43-57(2005) [PubMed: 15875012] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AAFI02000005 Genomic DNA. Translation: EAL72482.3.
RefSeq	XP_646660.3. XM_641568.3.
3D structure databases
HSSP	HSSP built from PDB template 1KQ0 based on UniProtKB P50579.
ProteinModelPortal	Q55C21.
ModBase	Search...
Protein-protein interaction databases
STRING	Q55C21.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblProtists	DDB0304991; DDB0304991; DDB_G0270264.
GeneID	8617632.
GenomeReviews	Gene locus metap2 in contig CM000150_GR.
KEGG	ddi:DDB_G0270264.
Organism-specific databases
dictyBase	DDB_G0270264. metap2.
Phylogenomic databases
eggNOG	KOG2775.
GeneTree	EPrGT00050000004088.
HOGENOM	HBG318153.
OMA	VKGCYTA.
ProtClustDB	PTZ00053.
Family and domain databases
InterPro	IPR001714. Pept_M24_MAP. IPR000994. Pept_M24_structural-domain. IPR002468. Pept_M24A_MAP2. IPR018349. Pept_M24A_MAP2_BS. IPR011991. WHTH_trsnscrt_rep_DNA-bd. [Graphical view]
Gene3D	G3DSA:3.90.230.10. Peptidase_M24_cat_core. 2 hits. G3DSA:1.10.10.10. Wing_hlx_DNA_bd. 1 hit.
KO	K01265.
PANTHER	PTHR10804:SF9. Pept_M24A_MAP2. 1 hit.
Pfam	PF00557. Peptidase_M24. 1 hit. [Graphical view]
PRINTS	PR00599. MAPEPTIDASE.
SUPFAM	SSF55920. Peptidase_M24_cat_core. 1 hit.
TIGRFAMs	TIGR00501. Met_pdase_II. 1 hit.
PROSITE	PS01202. MAP_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AMPM2_DICDI

Accession

Primary (citable) accession number: Q55C21

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 8, 2008
Last sequence update:	July 28, 2009
Last modified:	December 14, 2011
This is version 53 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)