ID A0A2C9JE88_BIOGL Unreviewed; 947 AA.
AC A0A2C9JE88;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN Name=106054973 {ECO:0000313|EnsemblMetazoa:BGLB001318-PE};
OS Biomphalaria glabrata (Bloodfluke planorb) (Freshwater snail).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Heterobranchia; Euthyneura; Panpulmonata; Hygrophila; Lymnaeoidea;
OC Planorbidae; Biomphalaria.
OX NCBI_TaxID=6526 {ECO:0000313|EnsemblMetazoa:BGLB001318-PE, ECO:0000313|Proteomes:UP000076420};
RN [1] {ECO:0000313|EnsemblMetazoa:BGLB001318-PE}
RP IDENTIFICATION.
RC STRAIN=BB02 {ECO:0000313|EnsemblMetazoa:BGLB001318-PE};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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 RefSeq; XP_013066520.1; XM_013211066.1.
DR AlphaFoldDB; A0A2C9JE88; -.
DR EnsemblMetazoa; BGLB001318-RE; BGLB001318-PE; BGLB001318.
DR VEuPathDB; VectorBase:BGLB001318; -.
DR OrthoDB; 3085317at2759; -.
DR Proteomes; UP000076420; 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; 2.60.40.1910; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 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; IPR024571; ERAP1-like_C_dom.
DR InterPro; IPR034016; M1_APN-typ.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR11533:SF302; AMINOPEPTIDASE N-LIKE PROTEIN; 1.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364040};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR634016-3};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU364040};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU364040};
KW Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..947
FT /note="Aminopeptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012044798"
FT DOMAIN 71..264
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 299..519
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 602..918
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT REGION 21..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 372
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 371
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 375
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 394
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 456
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 947 AA; 108830 MW; 9DB63A74AA1CE229 CRC64;
MGAVMVAVAV IAAFARPASI QTSNSCKPSP SSEDSSGGST VGPENETPQT YIATNGQVFP
WKDLRLPRTI KPLSYHIFLH PNLSESYFAG WVQMNLHVLE DTNYIVFHSH ELNLSSVTLH
ERQPGGGKEL GRELRVVQEL EYTRNNQYYV RVDSLLRAGL LLQLNVSFRG SLESLSRMSG
FYKSTYTVKE ETRYMASTQF EATFARSAFP CFDEPELKAN FSMSIVRSPQ HISLFNTRLI
ETKLYRDSLW LDVYEDSVKM STYLVAYVIC DFKNISKMTK DNVQVRLFAP EDKIYMGQYA
LNAAVTVLEY YNSFFGIHYP LSKLDLIAVP NFAAGAMENW GLITYRDTSI LYDPAKSTES
TKMWVTLVVA HELAHQWFGN LVTMKWWNDL WLNEGFATYV EYIGADQVDK DFQMMDSFMM
PFSGAQHLDS LITSHPIEVE VQDPAEVDAL FDKISYDKGA CLIRMLQHFI GEDKFKTALS
NYLKSHAYDN AQTQDLWDAM DSVSTNPQGL KVSMVMDTWT KQMGYPVVTV TREQDYLVLK
QDRFLMMDNF ENKSLKSDKS PFNYTWYIPF TYKTSSNPDK SHLVWMKRGS ATEKLPDSSA
IWIKGNVDTY GYYRVNYDKD GWQAIIQQLK TNHSVFSITD KVGLFNDAFS LARTGLISYT
IPLDMTKYLI NESNYFVWEE VLTNMYFVCN QLKLEEELDL LQTFVLSLAQ HLIDELGWAD
TGKHLTKKLR ASMIYLSLTM NYQPVMNEAY RQFIQWTIDK DFHIHSDLRG AVYSTGLKNS
TKEVWDLVME RYLTANIPSE KILLLSSLAA STNSRILQIL LEYSLDDSKV KSQSTTDVLS
SVAANDNGLL VTWRFVRERW DIIFERYGES SFLLSDIIKS VIQPFNSQFD YDEVVAFFKN
RDLGSGKMAL RQALEVVQSH IVWVKRNMQT VKDWLKANVK KSKNKIM
//
