ID A0A109WMQ1_9FUNG Unreviewed; 507 AA. AC A0A109WMQ1; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 14-DEC-2022, entry version 13. DE SubName: Full=Leucine aminopeptidase 3 {ECO:0000313|EMBL:AME15498.1}; OS Actinomucor elegans. OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina; OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Actinomucor. OX NCBI_TaxID=64647 {ECO:0000313|EMBL:AME15498.1}; RN [1] {ECO:0000313|EMBL:AME15498.1} RP NUCLEOTIDE SEQUENCE. RA Murphy D.; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=Release of N-terminal proline from a peptide.; EC=3.4.11.5; CC Evidence={ECO:0000256|ARBA:ARBA00001585}; CC -!- CATALYTIC ACTIVITY: CC Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa CC is preferably Leu, but may be other amino acids including Pro CC although not Arg or Lys, and Yaa may be Pro. Amino acid amides and CC methyl esters are also readily hydrolyzed, but rates on arylamides CC are exceedingly low.; EC=3.4.11.1; CC Evidence={ECO:0000256|ARBA:ARBA00000135}; CC -!- SIMILARITY: Belongs to the peptidase M17 family. CC {ECO:0000256|ARBA:ARBA00009528}. 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; KP973575; AME15498.1; -; mRNA. DR AlphaFoldDB; A0A109WMQ1; -. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro. DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR CDD; cd00433; Peptidase_M17; 1. DR Gene3D; 3.40.220.10; -; 1. DR HAMAP; MF_00181; Cytosol_peptidase_M17; 1. DR InterPro; IPR011356; Leucine_aapep/pepB. DR InterPro; IPR043472; Macro_dom-like. DR InterPro; IPR000819; Peptidase_M17_C. DR InterPro; IPR023042; Peptidase_M17_leu_NH2_pept. DR InterPro; IPR008283; Peptidase_M17_N. DR PANTHER; PTHR11963; LEUCINE AMINOPEPTIDASE-RELATED; 1. DR Pfam; PF00883; Peptidase_M17; 1. DR Pfam; PF02789; Peptidase_M17_N; 1. DR PRINTS; PR00481; LAMNOPPTDASE. DR SUPFAM; SSF52949; Macro domain-like; 1. DR PROSITE; PS00631; CYTOSOL_AP; 1. PE 2: Evidence at transcript level; KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438, KW ECO:0000313|EMBL:AME15498.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Protease {ECO:0000256|ARBA:ARBA00022670}. FT DOMAIN 351..358 FT /note="CYTOSOL_AP" FT /evidence="ECO:0000259|PROSITE:PS00631" SQ SEQUENCE 507 AA; 55479 MW; 55CCD98E83B64E68 CRC64; MLSPLTHNTF RTASRFHARR FFSNKQGFDS LVVGAYTSKN QPVLTTQQVS KATRDRIQSQ LVQSQFKKTG DVRVFYDIDG IKQVAVVSLG DNTFKNEHEE QERVRMATAV GIQTLQNQGA KYTGVDVSVD IQGAAEGAVL AQFSFDKLKQ KTEEDSGDKV VEPYLVEENN SIQKAWQVGQ IYGASQNVAR MLMTTPANLM TPKLFAEEVA YLLAGLENVD IEVHDEEWVK RQKMNAFLSV SKGSAQPLRF LEVHYKGAKD KNEKPYGFVG KGITFDSGGI SLKPSANMAL MKGDMGGAAT VAGAMYGICK MQLPVNIVAI IPLCENMPSG AATKPGDVVK AMNGKSIEVL NTDAEGRMIL ADALHYTSSR FQPKHIIDLA TLTGAMDVAL GQVYAGVFTN SDTLWQQLEK AGESVSDPFW RMPIHDDYVK EMKQSLVADL SNVGSRRSGG SCAAAGFLKE FVDKDIPWAH IDIAGVMDCH ATKGHHIKGM SGRPTRALIE LMKSVQQ //