O60085 (AMPM2_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
Peptidase M 2

Gene names

Name:	fma2
Synonyms:	map2
ORF Names:	SPBC14C8.03

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	426 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript 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.
Subcellular location	Cytoplasm Ref.2.
Sequence similarities	Belongs to the peptidase M24A family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Cobalt Metal-binding
Molecular function	Aminopeptidase Hydrolase Protease
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 sequence or structural similarity. Source: GeneDB_Spombe
Cellular component	cytosol Inferred from direct assay. Source: GeneDB_Spombe
Molecular function	aminopeptidase activity Inferred from sequence or structural similarity. Source: GeneDB_Spombe 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 – 426	426	Methionine aminopeptidase 2		PRO_0000311766
Sites
	Metal binding	199	1	Cobalt 1 By similarity
	Metal binding	210	1	Cobalt 1 By similarity
	Metal binding	210	1	Cobalt 2 By similarity
	Metal binding	279	1	Cobalt 2 By similarity
	Metal binding	312	1	Cobalt 2 By similarity
	Metal binding	407	1	Cobalt 1 By similarity
	Metal binding	407	1	Cobalt 2 By similarity
	Binding site	179	1	Substrate By similarity
	Binding site	287	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	O60085 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: E23E56582F7025D3	FASTA	426	47,271
	10 20 30 40 50 60 MTSATTTEAT AKDLQEKLSL KENDVVEDDG KVEENDAAEE GASNGEKKKK KKKKSSKKKK 70 80 90 100 110 120 TPQEQTNPPT VGLSKIFVNK KYPVGEVCDY AEDNLWRTTD EEKRALDRQN FDQYNDLRRA 130 140 150 160 170 180 AEVHRQARQY AQSVIKPGMS MMDVVNTIEN TTRALVEEDG LKSGIGFPTG VSLNHCAAHY 190 200 210 220 230 240 TPNAGDTTIL KEKDVMKVDI GVHVNGRIVD SAFTMSFDPQ YDNLLAAVKA ATNKGIEEAG 250 260 270 280 290 300 IDARLNEIGE AIQEVMESYE VEINGKTHQV KSIRNLCGHN LDPYIIHGGK SVPIVKGGEE 310 320 330 340 350 360 IKMEEGEIFA IETFGSTGRG VVHEDMECSH YAKIPDAGHI PLRLPRAKAL LNTITQNFGT 370 380 390 400 410 420 LPFCRRYLDR IGESKYLLAL NNLVSAGIVQ DYPPLCDIRG SYTAQFEHTI ILHPTQKEVV SRGDDY

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]	"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe." Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M. Nat. Biotechnol. 24:841-847(2006) [PubMed: 16823372] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU329671 Genomic DNA. Translation: CAA18421.1.
PIR	T39431.
RefSeq	NP_595906.1. NM_001021814.1.
3D structure databases
HSSP	HSSP built from PDB template 1KQ0 based on UniProtKB P50579.
ProteinModelPortal	O60085.
SMR	O60085. Positions 65-426.
ModBase	Search...
Protein-protein interaction databases
STRING	O60085.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPBC14C8.03.1; SPBC14C8.03.1:pep; SPBC14C8.03.
GeneID	2539692.
GenomeReviews	Gene locus fma2 in contig CU329671_GR.
KEGG	spo:SPBC14C8.03.
NMPDR	fig|4896.1.peg.1772.
Organism-specific databases
GeneDB_Spombe	SPBC14C8.03.
Phylogenomic databases
eggNOG	fuNOG04088.
GeneTree	EFGT00050000005517.
HOGENOM	HBG318153.
OMA	VKGCYTA.
OrthoDB	EOG4XD70X.
Gene expression databases
ArrayExpress	O60085.
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_SCHPO

Accession

Primary (citable) accession number: O60085

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 13, 2007
Last sequence update:	August 1, 1998
Last modified:	December 14, 2011
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program