ID A0A125S6H1_9FUNG Unreviewed; 352 AA. AC A0A125S6H1; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 25-MAY-2022, entry version 27. DE RecName: Full=Methionine aminopeptidase {ECO:0000256|RuleBase:RU003653}; DE EC=3.4.11.18 {ECO:0000256|RuleBase:RU003653}; OS Actinomucor elegans. OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina; OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Actinomucor. OX NCBI_TaxID=64647 {ECO:0000313|EMBL:AME15507.1}; RN [1] {ECO:0000313|EMBL:AME15507.1} RP NUCLEOTIDE SEQUENCE. RA Murphy D.; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Cotranslationally removes the N-terminal methionine from CC nascent proteins. The N-terminal methionine is often cleaved when the CC second residue in the primary sequence is small and uncharged (Met- CC Ala-, Cys, Gly, Pro, Ser, Thr, or Val). CC {ECO:0000256|RuleBase:RU003653}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Release of N-terminal amino acids, preferentially methionine, CC from peptides and arylamides.; EC=3.4.11.18; CC Evidence={ECO:0000256|HAMAP-Rule:MF_03174, CC ECO:0000256|RuleBase:RU003653}; CC -!- COFACTOR: CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; CC Evidence={ECO:0000256|HAMAP-Rule:MF_03174, CC ECO:0000256|RuleBase:RU003653}; CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|HAMAP-Rule:MF_03174, CC ECO:0000256|RuleBase:RU003653}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|HAMAP-Rule:MF_03174, CC ECO:0000256|RuleBase:RU003653}; CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; CC Evidence={ECO:0000256|HAMAP-Rule:MF_03174, CC ECO:0000256|RuleBase:RU003653}; CC Note=Binds 2 divalent metal cations per subunit. Has a high-affinity CC and a low affinity metal-binding site. The true nature of the CC physiological cofactor is under debate. The enzyme is active with CC cobalt, zinc, manganese or divalent iron ions. Most likely, methionine CC aminopeptidases function as mononuclear Fe(2+)-metalloproteases under CC physiological conditions, and the catalytically relevant metal-binding CC site has been assigned to the histidine-containing high-affinity site. CC {ECO:0000256|HAMAP-Rule:MF_03174, ECO:0000256|RuleBase:RU003653}; CC -!- SIMILARITY: Belongs to the peptidase M24A family. Methionine CC aminopeptidase type 1 subfamily. {ECO:0000256|HAMAP-Rule:MF_03174}. 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; KP973584; AME15507.1; -; mRNA. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:UniProtKB-UniRule. DR GO; GO:0070084; P:protein initiator methionine removal; IEA:UniProtKB-UniRule. DR CDD; cd01086; MetAP1; 1. DR Gene3D; 3.90.230.10; -; 1. DR HAMAP; MF_01974; MetAP_1; 1. DR InterPro; IPR036005; Creatinase/aminopeptidase-like. DR InterPro; IPR000994; Pept_M24. DR InterPro; IPR001714; Pept_M24_MAP. DR InterPro; IPR002467; Pept_M24A_MAP1. DR InterPro; IPR031615; Zfn-C6H2. DR Pfam; PF00557; Peptidase_M24; 1. DR Pfam; PF15801; zf-C6H2; 1. DR PRINTS; PR00599; MAPEPTIDASE. DR SUPFAM; SSF55920; SSF55920; 1. DR TIGRFAMs; TIGR00500; met_pdase_I; 1. DR PROSITE; PS00680; MAP_1; 1. PE 2: Evidence at transcript level; KW Aminopeptidase {ECO:0000256|HAMAP-Rule:MF_03174, KW ECO:0000256|RuleBase:RU003653}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_03174}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_03174, KW ECO:0000256|RuleBase:RU003653}; KW Protease {ECO:0000256|HAMAP-Rule:MF_03174, ECO:0000256|RuleBase:RU003653}. FT DOMAIN 7..51 FT /note="zf-C6H2" FT /evidence="ECO:0000259|Pfam:PF15801" FT DOMAIN 119..345 FT /note="Peptidase_M24" FT /evidence="ECO:0000259|Pfam:PF00557" FT METAL 200 FT /note="Divalent metal cation 1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03174" FT METAL 211 FT /note="Divalent metal cation 1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03174" FT METAL 211 FT /note="Divalent metal cation 2; catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03174" FT METAL 274 FT /note="Divalent metal cation 2; catalytic; via tele FT nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03174" FT METAL 307 FT /note="Divalent metal cation 2; catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03174" FT METAL 338 FT /note="Divalent metal cation 1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03174" FT METAL 338 FT /note="Divalent metal cation 2; catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03174" FT BINDING 183 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03174" FT BINDING 281 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03174" SQ SEQUENCE 352 AA; 38978 MW; 796F3C95E8BF159C CRC64; MLEKPLCASI ECKNKAHLQC PTCVKLGKNG ESFFCSQDCF KKSWGSHKAV HGDTKSPYDP FKTFKYAGPL RAVYPLSPRR TVPEEISRPD YAESGISRSE LMSRGSDIKV LTPEEIEGAK KACAITREVL ELAAKSIRVG MTTDELDRIV HEATIERGAY PSPLNYNYFP KSCCTSLNEV ICHGIPDQRP LADGDILNID ISCFYQGFHG DTNGTYLVGN VDEAGQKLVN VTRECLEKAI AAVKPGMRYR DFGKIIEDHA TKNGFSVVRA FVGHGIHQLF HCAPNVPHYA NNKAIGVCKP GHIFTIEPMI CEGVHQELMW PDGWTATTKD GKRSAQFEHT LLVTETGVEI LT //