O59730 (AMPM1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable methionine aminopeptidase 1
Short name=MAP 1
Short name=MetAP 1
EC=3.4.11.18

Alternative name(s):
Peptidase M 1

Gene names

ORF Names:

SPBC3E7.10

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	379 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	protein initiator methionine removal involved in protein maturation Inferred from sequence or structural similarity. Source: GeneDB_Spombe proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Inferred from direct assay. Source: GeneDB_Spombe nucleolus Inferred from direct assay. Source: GeneDB_Spombe
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 – 379	379	Probable methionine aminopeptidase 1		PRO_0000148972
Sites
	Metal binding	209	1	Cobalt 1 By similarity
	Metal binding	220	1	Cobalt 1 By similarity
	Metal binding	220	1	Cobalt 2 By similarity
	Metal binding	289	1	Cobalt 2 By similarity
	Metal binding	322	1	Cobalt 2 By similarity
	Metal binding	353	1	Cobalt 1 By similarity
	Metal binding	353	1	Cobalt 2 By similarity
	Binding site	192	1	Substrate By similarity
	Binding site	296	1	Substrate By similarity
Amino acid modifications
	Modified residue	373	1	Phosphoserine Ref.2

Sequences

	Sequence		Length	Mass (Da)
	O59730 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: D7A30E2886E3B248	FASTA	379	42,139
	10 20 30 40 50 60 MATEIAKHIC CGIDCNNEAD RLQCPKCLND GVKSYFCGQE CFRNSWNIHK HLHRPPNVEK 70 80 90 100 110 120 REDGTYNPFP KFHFAGSLKP VYPLSPIRKV PPHIKRPDYA KTGVSRSEQI EGRSFKLKRL 130 140 150 160 170 180 TPKEQEGMRK VCRLGREVLD AAAAAVRPGT TTDELDSIVH NACIERDCFP STLNYYAFPK 190 200 210 220 230 240 SVCTSVNEII CHGIPDQRPL EDGDIVNIDV SLYHNGFHGD LNETYYVGDK AKANPDLVCL 250 260 270 280 290 300 VENTRIALDK AIAAVKPGVL FQEFGNIIEK HTNSITEKQI SVVRTYCGHG INQLFHCSPS 310 320 330 340 350 360 IPHYSHNKAP GIARPGMTFT IEPMLTLGPA RDITWPDDWT SSTASGRCSA QFEHTLLVTE 370 TGCEVLTARL PNSPGGPLK

References

[1]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 972 / ATCC 24843.
[2]	"Phosphoproteome analysis of fission yeast." Wilson-Grady J.T., Villen J., Gygi S.P. J. Proteome Res. 7:1088-1097(2008) [PubMed: 18257517] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-373, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU329671 Genomic DNA. Translation: CAA19013.1.
PIR	T40384.
RefSeq	NP_596097.1. NM_001022013.1.
3D structure databases
ProteinModelPortal	O59730.
SMR	O59730. Positions 72-373.
ModBase	Search...
Protein-protein interaction databases
STRING	O59730.
Protein family/group databases
MEROPS	M24.001.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPBC3E7.10.1; SPBC3E7.10.1:pep; SPBC3E7.10.
GeneID	2540928.
KEGG	spo:SPBC3E7.10.
NMPDR	fig|4896.1.peg.1963.
Organism-specific databases
GeneDB_Spombe	SPBC3E7.10.
Phylogenomic databases
eggNOG	fuNOG04170.
GeneTree	EFGT00050000005419.
HOGENOM	HBG299384.
OMA	QEGMRKV.
OrthoDB	EOG4TQQJJ.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-004140-MONOMER.
Gene expression databases
ArrayExpress	O59730.
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. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AMPM1_SCHPO

Accession

Primary (citable) accession number: O59730

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 27, 2001
Last sequence update:	August 1, 1998
Last modified:	December 14, 2011
This is version 91 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program