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
//