ID A0A091CMT6_FUKDA Unreviewed; 885 AA.
AC A0A091CMT6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
DE Flags: Fragment;
GN ORFNames=H920_19416 {ECO:0000313|EMBL:KFO19222.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO19222.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO19222.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO19222.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR634016-3,
CC ECO:0000256|RuleBase:RU364040};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634016-3,
CC ECO:0000256|RuleBase:RU364040};
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136, ECO:0000256|RuleBase:RU364040}.
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DR EMBL; KN125162; KFO19222.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091CMT6; -.
DR STRING; 885580.ENSFDAP00000021747; -.
DR MEROPS; M01.026; -.
DR eggNOG; KOG1046; Eukaryota.
DR Proteomes; UP000028990; Unassembled WGS sequence.
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:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09601; M1_APN-Q_like; 1.
DR Gene3D; 1.25.50.20; -; 1.
DR Gene3D; 3.30.2010.30; -; 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; IPR029264; ARF7EP_C.
DR InterPro; IPR024571; ERAP1-like_C_dom.
DR InterPro; IPR034016; M1_APN-typ.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR PANTHER; PTHR11533:SF31; AMINOPEPTIDASE Q; 1.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR Pfam; PF14949; ARF7EP_C; 1.
DR Pfam; PF11838; ERAP1_C; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR PRINTS; PR00756; ALADIPTASE.
DR SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|RuleBase:RU364040,
KW ECO:0000313|EMBL:KFO19222.1}; Hydrolase {ECO:0000256|RuleBase:RU364040};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR634016-3,
KW ECO:0000256|RuleBase:RU364040};
KW Metalloprotease {ECO:0000256|RuleBase:RU364040};
KW Protease {ECO:0000256|RuleBase:RU364040};
KW Reference proteome {ECO:0000313|Proteomes:UP000028990};
KW Zinc {ECO:0000256|PIRSR:PIRSR634016-3, ECO:0000256|RuleBase:RU364040}.
FT DOMAIN 123..197
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 233..430
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 423..698
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT DOMAIN 769..870
FT /note="ARF7 effector protein C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14949"
FT ACT_SITE 306
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 305
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 309
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 339
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 405
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFO19222.1"
SQ SEQUENCE 885 AA; 101036 MW; A641B88F8B75AEDC CRC64;
HSLFLDHELP EVRGPLSPGA RDAAACRVPV QDMWFSEYME YMVLELGEAL QPGSLYELQL
RFTGPVFKET REGLFLNLYS DQGERSSLST VAVGSERILL WFGDALSPLL RQQCPRGTVS
VSRALIASQM EPTFARSVFP CFDEPALKAT FNITIIHHPS YVALSNMPQL GQSERDVNGS
KWTVTTFYTT PHMPTYLVAL AICDYDQVNR TERGKEIRIW ARKDAIANGN ADFALNITGP
IFSFLEDLFN ISYPLPKADI IALPSFDNQA MENWGLMMFD ESLLLLQPSD QLTVKKDLIS
HIVSHEIGHQ ACAFFPFHFQ KWFGNLVTMN WWNNIWLNEG FASYFEFGVT NYFNPKLPRN
EVFFSNFLHG VLSEDHALVL RAVSMKAENF RETSEINELF DLFTYKKGAS MARMLSSFLN
EHLFISALKA IPVIHRLQLI DDAFSLSRNN YIEIETALDL TKYLAEEDEI IVWHEVLANL
VTRDLVSDVS NYDIYPLLKK YLLKRLKSIW NIYATIIREN VGALQDDYLA LISLEKLFTT
ACGFGLEDCL QLSKELFRKW MSHPENKIPY PIKSVILCYG IASGSDKEWD FLLNIYTNTT
EEVERIQLAY AMCCSKDPWI LNRYMQYAII TSPITFNEMN VIEAVAASEV GRYVAKDFLV
DNWQAVSERY GTQSLVTLIC IIGRTISTDL QIMELSQLHD STTLPLVFMA FPARNSVSLV
PFSTDGVSLK SHRLPIPQPP LQQSYHGHIT WAMELCVCVA STSWQQQIER QLKCLAFQNP
GPQVADFNPE TRQQKKKARM SKMNEYFSVK YKVMKKYDKS GRLICNDVDL CDCLEKNCLG
CFYPCPKCNS NKCGPECRCS RRWVYDAIVT ESGDIVSSLP FNIPD
//
