ID G9KLL4_MUSPF Unreviewed; 544 AA. AC G9KLL4; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 22-FEB-2023, entry version 44. DE SubName: Full=Arginyl aminopeptidase {ECO:0000313|EMBL:AES05793.1}; DE Flags: Fragment; OS Mustela putorius furo (European domestic ferret) (Mustela furo). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Mustelidae; Mustelinae; OC Mustela. OX NCBI_TaxID=9669 {ECO:0000313|EMBL:AES05793.1}; RN [1] {ECO:0000313|EMBL:AES05793.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Lungs {ECO:0000313|EMBL:AES05793.1}; RX PubMed=23236062; DOI=10.1128/JVI.02476-12; RA Leon A.J., Banner D., Xu L., Ran L., Peng Z., Yi K., Chen C., Xu F., RA Huang J., Zhao Z., Lin Z., Huang S.H., Fang Y., Kelvin A.A., Ross T.M., RA Farooqui A., Kelvin D.J.; RT "Sequencing, annotation, and characterization of the influenza ferret RT infectome."; RL J. Virol. 87:1957-1966(2013). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR634015-3}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634015-3}; CC -!- SIMILARITY: Belongs to the peptidase M1 family. CC {ECO:0000256|ARBA:ARBA00010136}. 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; JP017195; AES05793.1; -; mRNA. DR AlphaFoldDB; G9KLL4; -. DR MEROPS; M01.014; -. DR HOGENOM; CLU_014505_2_1_1; -. DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW. DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR CDD; cd09599; M1_LTA4H; 1. DR Gene3D; 3.30.2010.30; -; 1. DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1. DR Gene3D; 1.25.40.320; Peptidase M1, leukotriene A4 hydrolase/aminopeptidase C-terminal domain; 1. DR Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 1. DR InterPro; IPR045357; Aminopeptidase_N-like_N. DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR038502; M1_LTA-4_hydro/amino_C_sf. DR InterPro; IPR034015; M1_LTA4H. DR InterPro; IPR001930; Peptidase_M1. DR InterPro; IPR015211; Peptidase_M1_C. DR InterPro; IPR014782; Peptidase_M1_dom. DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf. DR PANTHER; PTHR45726:SF1; AMINOPEPTIDASE B; 1. DR PANTHER; PTHR45726; LEUKOTRIENE A-4 HYDROLASE; 1. DR Pfam; PF09127; Leuk-A4-hydro_C; 1. DR Pfam; PF01433; Peptidase_M1; 1. DR Pfam; PF17900; Peptidase_M1_N; 1. DR PRINTS; PR00756; ALADIPTASE. DR SMART; SM01263; Leuk-A4-hydro_C; 1. DR SUPFAM; SSF48371; ARM repeat; 1. DR SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1. DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1. PE 2: Evidence at transcript level; KW Aminopeptidase {ECO:0000313|EMBL:AES05793.1}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR634015-3}; KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049}; KW Protease {ECO:0000256|ARBA:ARBA00022670}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634015-3}. FT DOMAIN 397..542 FT /note="Peptidase M1 leukotriene A4 hydrolase/aminopeptidase FT C-terminal" FT /evidence="ECO:0000259|SMART:SM01263" FT ACT_SITE 223 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR634015-1" FT ACT_SITE 311 FT /note="Proton donor" FT /evidence="ECO:0000256|PIRSR:PIRSR634015-1" FT BINDING 66..68 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR634015-2" FT BINDING 193..198 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR634015-2" FT BINDING 222 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PIRSR:PIRSR634015-3" FT BINDING 226 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PIRSR:PIRSR634015-3" FT BINDING 245 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PIRSR:PIRSR634015-3" FT BINDING 497..499 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR634015-2" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AES05793.1" FT NON_TER 544 FT /evidence="ECO:0000313|EMBL:AES05793.1" SQ SEQUENCE 544 AA; 61561 MW; 0D8C5EB702B67021 CRC64; PAEPVPFHTQ PFSHYGQALC VALPQPCLAG ERFQVLLTYR VGEGPGVCWL SPEQTAGKKK PFVYTQGQAV LNRAFFPCFD TPAVKCTYSA HVEVPDGFTA VMSANTWEKK GPNKFFFEMC HPIPSYLIAL AIGDLVSAEV GPRSRVWAEP CLIDAAKEEY NGVIEEFLAT GEKLFGPYVW GRYDLLFMPP SFPFGGMENP CLTFVTPCLL AGDRSLADVI IHEISHSWFG NLVTNANWGE FWLNEGFTMY AQRRISTVLF GSAYTCLEAA TGRALLRQHM DITGEENPLN KLRVKIEPGV DPDDTYNETP YEKGFCFVSY LAHLVGDQDQ FDSFLKAYVN EFKFQSIVAE DFLEFYLEYF PELKKKRVES IPGFEFDRWL NVPGWPPYLP DLSPGDSLMK PAEELAQLWE TEELDMKAIE AVAISTWKTY QLVYFLDKIL QKSPLPPGNV KKLGETYPKI SNSQNAELRL RWGHIVLKND YQEDFWKVKE FLQSQGKQKY TLPLYHAMMA GSKVAQTLAK ETFAATAPQL HSNVVNYVQQ IVAP //