Q54VU7 (AMP1D_DICDI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Methionine aminopeptidase 1D, mitochondrial
EC=3.4.11.18

Alternative name(s):
Methionyl aminopeptidase type 1D, mitochondrial

Gene names

Name:	metap1d
Synonyms:	map1d
ORF Names:	DDB_G0280127

Organism

Dictyostelium discoideum (Slime mold)

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	404 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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.
Subcellular location	Mitochondrion By similarity.
Sequence similarities	Belongs to the peptidase M24A family.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Transit peptide
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	mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell
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
	Transit peptide	1 – 58	58	Mitochondrion Potential
	Chain	59 – 404	346	Methionine aminopeptidase 1D, mitochondrial		PRO_0000328514
Regions
	Compositional bias	27 – 35	9	Poly-Ser
	Compositional bias	38 – 42	5	Poly-Asn
Sites
	Metal binding	249	1	Cobalt 1 By similarity
	Metal binding	260	1	Cobalt 1 By similarity
	Metal binding	260	1	Cobalt 2 By similarity
	Metal binding	323	1	Cobalt 2 By similarity
	Metal binding	355	1	Cobalt 2 By similarity
	Metal binding	389	1	Cobalt 1 By similarity
	Metal binding	389	1	Cobalt 2 By similarity
	Binding site	232	1	Substrate By similarity
	Binding site	330	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q54VU7 [UniParc]. Last modified May 24, 2005. Version 1. Checksum: AC369296B3E58FD4	FASTA	404	45,549
	10 20 30 40 50 60 MNKILKNIIN KSSINNVFKT SFNGGISSSS SSSSSYLNNN NNIIKSYNVQ QKQQQRYYSS 70 80 90 100 110 120 FEDDLSPKKL KEKILENETE EIRDFVRSQR LTKKTASPLE GMNRKERRKM TTKLYRNPDN 130 140 150 160 170 180 LIRGGIVSPQ PLIPAHIKKP KYVLGEPVID FEIDDPIEIH TAESIEHMRV VGKMAKEVLE 190 200 210 220 230 240 YAGTLVRPGI TTDEIDKLVH QNIIDRGAYP SPLGYKGFPK SICTSINEVL CHGIPDDRPL 250 260 270 280 290 300 EFGDIVKIDV TLYYNGYHGD TCATFPVGEI DSSSKRLIEA TEKALYAAIG EVKDGALFNK 310 320 330 340 350 360 IGKKIQLVAN KYSLSVTPEF TGHGIGQLFH TAPFVFQCAN EFDSVMKEGM IFTIEPVLVE 370 380 390 400 STSPYAEWKM WDDKWTVSSR EGGWSAQFEH TILVTKDGYE ILTK

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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AAFI02000035 Genomic DNA. Translation: EAL67290.1.
RefSeq	XP_641258.1. XM_636166.1.
3D structure databases
HSSP	HSSP built from PDB template 2B3H based on UniProtKB P53582.
ProteinModelPortal	Q54VU7.
ModBase	Search...
Protein-protein interaction databases
STRING	Q54VU7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblProtists	DDB0235404; DDB0235404; DDB_G0280127.
GeneID	8622390.
GenomeReviews	Gene locus metap1d in contig CM000152_GR.
KEGG	ddi:DDB_G0280127.
Organism-specific databases
dictyBase	DDB_G0280127. map1d.
Phylogenomic databases
eggNOG	KOG2738.
GeneTree	EPrGT00050000000956.
HOGENOM	HBG299384.
PhylomeDB	Q54VU7.
Family and domain databases
InterPro	IPR001714. Pept_M24_MAP. IPR000994. Pept_M24_structural-domain. IPR002467. Pept_M24A_MAP1. [Graphical view]
Gene3D	G3DSA:3.90.230.10. Peptidase_M24_cat_core. 1 hit.
KO	K01265.
Pfam	PF00557. Peptidase_M24. 1 hit. [Graphical view]
PRINTS	PR00599. MAPEPTIDASE.
SUPFAM	SSF55920. Peptidase_M24_cat_core. 1 hit.
TIGRFAMs	TIGR00500. Met_pdase_I. 1 hit.
PROSITE	PS00680. MAP_1. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AMP1D_DICDI

Accession

Primary (citable) accession number: Q54VU7

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 8, 2008
Last sequence update:	May 24, 2005
Last modified:	November 16, 2011
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)