ID A0A091KKV2_9GRUI Unreviewed; 552 AA.
AC A0A091KKV2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 08-NOV-2023, entry version 28.
DE SubName: Full=Leucyl-cystinyl aminopeptidase {ECO:0000313|EMBL:KFP41204.1};
DE Flags: Fragment;
GN ORFNames=N324_02906 {ECO:0000313|EMBL:KFP41204.1};
OS Chlamydotis macqueenii (Macqueen's bustard).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Gruiformes; Otididae; Chlamydotis.
OX NCBI_TaxID=187382 {ECO:0000313|EMBL:KFP41204.1, ECO:0000313|Proteomes:UP000053330};
RN [1] {ECO:0000313|EMBL:KFP41204.1, ECO:0000313|Proteomes:UP000053330}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N324 {ECO:0000313|EMBL:KFP41204.1};
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; KK749109; KFP41204.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091KKV2; -.
DR Proteomes; UP000053330; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 1.10.390.10; 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; 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:SF42; LEUCYL-CYSTINYL AMINOPEPTIDASE; 1.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 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:KFP41204.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
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:UP000053330};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 172..357
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 391..550
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT ACT_SITE 464
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 463
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 467
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 486
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 548
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP41204.1"
FT NON_TER 552
FT /evidence="ECO:0000313|EMBL:KFP41204.1"
SQ SEQUENCE 552 AA; 62829 MW; 7138BBC5B449A838 CRC64;
LSSFSDRIQL PRNMIENSMF EEEPDVVDLA KEPCLHPLEP DEVEYEPRSS RLLVRGLGEH
EMDDDEEDYE SSAKLLGMSF MNRSSGLQNN LSVYRKNPNG SCSVPSTRTM VVCTVVLVIA
VSLIMAIYLL PKCIFTKEGC HKKHHTMELI YPLATNGKLF PWAKIRLPPD VVPLHYELVL
QPNLTTLKFA GSVKIVVNIV QVTWKIVLHS SGLNITKATI TSAGGHQAKL VELLEYPLHD
QIAIMAHEAL RVGQNYTVNI EYSSNLSDSY YGFYKISYKD ENSKQRWFAT TQFEPLSARS
AFPCFDEPAF KATFLIKIKR DEKLTTLSNM PKKTTTPVTN GIVQDEFFLS LKMSTYLVAF
VVADLQNITR EINGSLVSIY AIPQHLSQAE YALNTAVKLL EFYEKYFLIN YPLEKLDLVA
VPDFQSGAME NWGLITFRET TLLFDSNTSS ARDKKLITAV IAHELAHQWF GNLVTMEWWN
DLWLNEGFAT FMEYFAMEEI FPELHSDEDF LNLIFKAMMK DSLNSSHPVS ATVQSSEQIE
EMFDALSYIK VT
//
