ID A0A125S6H1_9FUNG Unreviewed; 352 AA. AC A0A125S6H1; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 05-OCT-2016, entry version 6. DE RecName: Full=Methionine aminopeptidase 1 {ECO:0000256|HAMAP-Rule:MF_03174}; DE Short=MAP 1 {ECO:0000256|HAMAP-Rule:MF_03174}; DE Short=MetAP 1 {ECO:0000256|HAMAP-Rule:MF_03174}; DE EC=3.4.11.18 {ECO:0000256|HAMAP-Rule:MF_03174}; DE AltName: Full=Peptidase M 1 {ECO:0000256|HAMAP-Rule:MF_03174}; OS Actinomucor elegans. OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycotina; Mucorales; OC 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 CC the second residue in the primary sequence is small and uncharged CC (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). {ECO:0000256|HAMAP- CC Rule:MF_03174}. CC -!- FUNCTION: Removes the N-terminal methionine from nascent proteins. CC The N-terminal methionine is often cleaved when the second residue CC in the primary sequence is small and uncharged (Met-Ala-, Cys, CC Gly, Pro, Ser, Thr, or Val). {ECO:0000256|RuleBase:RU003653}. CC -!- CATALYTIC ACTIVITY: Release of N-terminal amino acids, CC preferentially methionine, from peptides and arylamides. CC {ECO:0000256|HAMAP-Rule:MF_03174, ECO:0000256|RuleBase:RU003653}. CC -!- COFACTOR: CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000256|HAMAP- CC Rule:MF_03174, ECO:0000256|RuleBase:RU003653}; CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP- CC Rule:MF_03174, ECO:0000256|RuleBase:RU003653}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|HAMAP- CC Rule:MF_03174, ECO:0000256|RuleBase:RU003653}; CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000256|HAMAP- CC Rule:MF_03174, ECO:0000256|RuleBase:RU003653}; CC Note=Binds 2 divalent metal cations per subunit. Has a high- CC affinity and a low affinity metal-binding site. The true nature of CC the physiological cofactor is under debate. The enzyme is active CC with cobalt, zinc, manganese or divalent iron ions. Most likely, CC methionine aminopeptidases function as mononuclear Fe(2+)- CC metalloproteases under physiological conditions, and the CC catalytically relevant metal-binding site has been assigned to the CC histidine-containing high-affinity site. {ECO:0000256|HAMAP- CC Rule:MF_03174, ECO:0000256|RuleBase:RU003653}; CC -!- SUBUNIT: Associates with the 60S ribosomal subunit of the 80S CC translational complex. {ECO:0000256|HAMAP-Rule:MF_03174}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03174}. CC -!- SIMILARITY: Belongs to the peptidase M24A family. Methionine CC aminopeptidase type 1 subfamily. {ECO:0000256|HAMAP- CC 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:0022626; C:cytosolic ribosome; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0070084; P:protein initiator methionine removal; IEA:UniProtKB-HAMAP. DR CDD; cd01086; MetAP1; 1. DR Gene3D; 3.90.230.10; -; 1. DR HAMAP; MF_01974; MetAP_1; 1. DR InterPro; IPR001714; Pept_M24_MAP. DR InterPro; IPR000994; Pept_M24_structural-domain. 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, ECO:0000313|EMBL:AME15507.1}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03174}; 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, KW ECO:0000256|RuleBase:RU003653}. FT DOMAIN 7 51 zf-C6H2. {ECO:0000259|Pfam:PF15801}. FT DOMAIN 119 345 Peptidase_M24. {ECO:0000259|Pfam: FT PF00557}. FT REGION 7 51 Zinc finger-like; important for proper FT ribosome association. {ECO:0000256|HAMAP- FT Rule:MF_03174}. FT METAL 200 200 Divalent metal cation 1. FT {ECO:0000256|HAMAP-Rule:MF_03174}. FT METAL 211 211 Divalent metal cation 1. FT {ECO:0000256|HAMAP-Rule:MF_03174}. FT METAL 211 211 Divalent metal cation 2; catalytic. FT {ECO:0000256|HAMAP-Rule:MF_03174}. FT METAL 274 274 Divalent metal cation 2; catalytic; via FT tele nitrogen. {ECO:0000256|HAMAP-Rule: FT MF_03174}. FT METAL 307 307 Divalent metal cation 2; catalytic. FT {ECO:0000256|HAMAP-Rule:MF_03174}. FT METAL 338 338 Divalent metal cation 1. FT {ECO:0000256|HAMAP-Rule:MF_03174}. FT METAL 338 338 Divalent metal cation 2; catalytic. FT {ECO:0000256|HAMAP-Rule:MF_03174}. FT BINDING 183 183 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_03174}. FT BINDING 281 281 Substrate. {ECO:0000256|HAMAP-Rule: FT 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 //