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Database: UniProt
Entry: A0A091VVM7_NIPNI
LinkDB: A0A091VVM7_NIPNI
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ID   A0A091VVM7_NIPNI        Unreviewed;       692 AA.
AC   A0A091VVM7;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=Aminopeptidase Q {ECO:0000313|EMBL:KFR06543.1};
DE   Flags: Fragment;
GN   ORFNames=Y956_00251 {ECO:0000313|EMBL:KFR06543.1};
OS   Nipponia nippon (Crested ibis) (Ibis nippon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Pelecaniformes; Threskiornithidae;
OC   Nipponia.
OX   NCBI_TaxID=128390 {ECO:0000313|EMBL:KFR06543.1, ECO:0000313|Proteomes:UP000053283};
RN   [1] {ECO:0000313|EMBL:KFR06543.1, ECO:0000313|Proteomes:UP000053283}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_Y956 {ECO:0000313|EMBL:KFR06543.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRSR:PIRSR634016-3};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634016-3};
CC   -!- SIMILARITY: Belongs to the peptidase M1 family.
CC       {ECO:0000256|ARBA:ARBA00010136}.
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DR   EMBL; KL411402; KFR06543.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091VVM7; -.
DR   STRING; 128390.A0A091VVM7; -.
DR   MEROPS; M01.026; -.
DR   eggNOG; KOG1046; Eukaryota.
DR   Proteomes; UP000053283; 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:InterPro.
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:SF31; AMINOPEPTIDASE Q; 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:0000313|EMBL:KFR06543.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR634016-3};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053283};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT   DOMAIN          2..75
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          111..352
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
FT   DOMAIN          428..692
FT                   /note="ERAP1-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11838"
FT   ACT_SITE        184
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT   BINDING         183
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   BINDING         187
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   BINDING         219
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   SITE            285
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
FT   NON_TER         692
FT                   /evidence="ECO:0000313|EMBL:KFR06543.1"
SQ   SEQUENCE   692 AA;  80297 MW;  38C5036DD72FC964 CRC64;
     MLIASQLEPT YARRVYPCFD APAMKATFNI RIVHDPSYVA LSNMPAIDVS EMKDENGSLW
     TVTTFNTSLK MSTYLTAFVI CDFDYVTRTE RGNEIRIWAR KEAVKNGYVD YALNITGPIF
     SFLEDLLNVS YPLPKTDLVA LPDFGAGGME NWGLMTFQES SLMYLPSDKL TSRKAMIAII
     VSHELGHQAC EMLRHFFFLF KWFGNLVTMN WWNDLWLNEG LASYFEYLGA TFIEPKLSLD
     KIFYDHVVQP VLREDNEIGV RSLSESEDKI KGSFSLMSLF DSITYNKGAS ITWMLSGFLT
     EKLFIRALTS YLKEFSFSNA NQDDLWTHIQ MVVDAQDEVQ LPASVKQIMD SWTCQNGFPV
     LTLNLTTGTI SQEQFLNKKN ENSTDSYNNT WIIPISWMRN GSSQPLMWLD KSSKVFPEIQ
     VSESEYDWIL LNVNLSGYYR VNYDKLNLKR LARVLESDPK VSRFQLIDDV FALTQFGYIQ
     IETALELTKY LAREDELFIW NVVLLNLVPE NLEGTLKNYE VYPLLKKYLL KRMLPIYHYY
     AGFIRQNVDA LEDDYFAQVY LEKLFATACW MGLQDCLKLS SELYAKWMDN PEYKIPFLIR
     RTVCCYGIAV GSDKEWNFAW EMYNHTNSTK EDKDILLSAM SCAKESWLLY RYLQYGLSDT
     LFSSNCTSII ILYVVTKDIG HRIAWEFVTE NW
//
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