ID B7XJ30_ENTBH Unreviewed; 338 AA. AC B7XJ30; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 15-MAR-2017, entry version 48. DE RecName: Full=Methionyl aminopeptidase {ECO:0000256|SAAS:SAAS00684751}; DE EC=3.4.11.18 {ECO:0000256|SAAS:SAAS00684751}; GN ORFNames=EBI_27249 {ECO:0000313|EMBL:EED44036.1}; OS Enterocytozoon bieneusi (strain H348) (Microsporidian parasite). OC Eukaryota; Fungi; Microsporidia; Enterocytozoonidae; Enterocytozoon. OX NCBI_TaxID=481877 {ECO:0000313|EMBL:EED44036.1, ECO:0000313|Proteomes:UP000001742}; RN [1] {ECO:0000313|EMBL:EED44036.1, ECO:0000313|Proteomes:UP000001742} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=H348 {ECO:0000313|EMBL:EED44036.1, RC ECO:0000313|Proteomes:UP000001742}; RX PubMed=18060071; DOI=10.1371/journal.pone.0001277; RA Corradi N., Akiyoshi D.E., Morrison H.G., Feng X., Weiss L.M., RA Tzipori S., Keeling P.J.; RT "Patterns of genome evolution among the microsporidian parasites RT Encephalitozoon cuniculi, Antonospora locustae and Enterocytozoon RT bieneusi."; RL PLoS ONE 2:E1277-E1277(2007). RN [2] {ECO:0000313|EMBL:EED44036.1, ECO:0000313|Proteomes:UP000001742} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=H348 {ECO:0000313|EMBL:EED44036.1, RC ECO:0000313|Proteomes:UP000001742}; RX PubMed=19132089; DOI=10.1371/journal.ppat.1000261; RA Akiyoshi D.E., Morrison H.G., Lei S., Feng X., Zhang Q., Corradi N., RA Mayanja H., Tumwine J.K., Keeling P.J., Weiss L.M., Tzipori S.; RT "Genomic survey of the non-cultivatable opportunistic human pathogen, RT Enterocytozoon bieneusi."; RL PLoS Pathog. 5:E1000261-E1000261(2009). CC -!- FUNCTION: Cotranslationally removes the N-terminal methionine from CC nascent proteins. The N-terminal methionine is often cleaved when CC the second residue in the primary sequence is small and uncharged CC (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). CC {ECO:0000256|SAAS:SAAS00684756}. CC -!- CATALYTIC ACTIVITY: Release of N-terminal amino acids, CC preferentially methionine, from peptides and arylamides. CC {ECO:0000256|SAAS:SAAS00684747}. CC -!- COFACTOR: CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; CC Evidence={ECO:0000256|SAAS:SAAS00684755}; CC -!- COFACTOR: CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; CC Evidence={ECO:0000256|SAAS:SAAS00684757}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|SAAS:SAAS00684758}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|SAAS:SAAS00684761}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|SAAS:SAAS00684748}. CC -!- SIMILARITY: Belongs to the peptidase M24A family. Methionine CC aminopeptidase eukaryotic type 2 subfamily. CC {ECO:0000256|SAAS:SAAS00684752}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EED44036.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; ABGB01000024; EED44036.1; -; Genomic_DNA. DR RefSeq; XP_002650008.1; XM_002649962.1. DR ProteinModelPortal; B7XJ30; -. DR EnsemblFungi; EED44036; EED44036; EBI_27249. DR GeneID; 8641627; -. DR EuPathDB; MicrosporidiaDB:EBI_27249; -. DR InParanoid; B7XJ30; -. DR OrthoDB; EOG092C3NQP; -. DR BRENDA; 3.4.11.18; 12098. DR Proteomes; UP000001742; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008235; F:metalloexopeptidase activity; IEA:InterPro. DR Gene3D; 1.10.10.10; -; 1. DR Gene3D; 3.90.230.10; -; 2. DR InterPro; IPR000994; Pept_M24. DR InterPro; IPR002468; Pept_M24A_MAP2. DR InterPro; IPR018349; Pept_M24A_MAP2_BS. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF00557; Peptidase_M24; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR SUPFAM; SSF55920; SSF55920; 2. DR TIGRFAMs; TIGR00501; met_pdase_II; 1. DR PROSITE; PS01202; MAP_2; 1. PE 3: Inferred from homology; KW Aminopeptidase {ECO:0000256|SAAS:SAAS00684759, KW ECO:0000313|EMBL:EED44036.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001742}; KW Cytoplasm {ECO:0000256|SAAS:SAAS00684754}; KW Hydrolase {ECO:0000256|SAAS:SAAS00684749, KW ECO:0000313|EMBL:EED44036.1}; KW Metal-binding {ECO:0000256|SAAS:SAAS00684750}; KW Protease {ECO:0000256|SAAS:SAAS00684753}; KW Reference proteome {ECO:0000313|Proteomes:UP000001742}. FT DOMAIN 30 326 Peptidase_M24. {ECO:0000259|Pfam: FT PF00557}. SQ SEQUENCE 338 AA; 38121 MW; 8F7642BF024B3E3E CRC64; MILINPVQEK PIEFLDKTLF NTTSDTQLND IMRAAEAHKR IRGNLQKILK PGCSVREIIK YVEDSTRIML HGEKNNGIGF PCGVSLNNVA AHFSLNPWNE DIILTKNDVL KIDFGTHSNG RIVDSAFSVS FDEKYTNLLL ATKEATERGI KVIGIDMAVC EIGKEISEVF KSFEFEENGK MINIKPIWNL NGHSIDQYKI HAGISIPSIN NGDYSRITPG FFAIETFAST GIGEIKDYGE CSHFALASRP TTNKIYDKKN EEILNLIKKE FGTLPFSHQH LLYYTQNAKA AVQLLAARKF IDSYPPLVDI PKSYVAQFEH TLYITEKSKF NISKGDDY //