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Database: UniProt
Entry: A0A151K257_9HYME
LinkDB: A0A151K257_9HYME
Original site: A0A151K257_9HYME 
ID   A0A151K257_9HYME        Unreviewed;       724 AA.
AC   A0A151K257;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN   ORFNames=ALC62_03835 {ECO:0000313|EMBL:KYN50206.1};
OS   Cyphomyrmex costatus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Cyphomyrmex.
OX   NCBI_TaxID=456900 {ECO:0000313|EMBL:KYN50206.1, ECO:0000313|Proteomes:UP000078542};
RN   [1] {ECO:0000313|EMBL:KYN50206.1, ECO:0000313|Proteomes:UP000078542}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MS0001 {ECO:0000313|EMBL:KYN50206.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KYN50206.1};
RA   Nygaard S., Hu H., Boomsma J., Zhang G.;
RT   "Cyphomyrmex costatus WGS genome.";
RL   Submitted (MAR-2016) 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   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004609};
CC       Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004589}; Lipid-anchor, GPI-anchor
CC       {ECO:0000256|ARBA:ARBA00004589}.
CC   -!- SIMILARITY: Belongs to the peptidase M1 family.
CC       {ECO:0000256|ARBA:ARBA00010136, ECO:0000256|RuleBase:RU364040}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KYN50206.1}.
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DR   EMBL; LKEX01012869; KYN50206.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A151K257; -.
DR   STRING; 456900.A0A151K257; -.
DR   Proteomes; UP000078542; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0098552; C:side of 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: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; 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:SF291; AMINOPEPTIDASE-RELATED; 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   ECO:0000313|EMBL:KYN50206.1};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00022622};
KW   GPI-anchor {ECO:0000256|ARBA:ARBA00022622};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364040};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
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   Reference proteome {ECO:0000313|Proteomes:UP000078542};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           16..724
FT                   /note="Aminopeptidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012181565"
FT   DOMAIN          38..228
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          263..483
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
FT   DOMAIN          571..719
FT                   /note="ERAP1-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11838"
FT   ACT_SITE        332
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT   BINDING         331
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   BINDING         335
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   BINDING         354
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   SITE            416
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ   SEQUENCE   724 AA;  84043 MW;  30EECBCEB5BB1A3C CRC64;
     MIILKLLLNI GLILATRTIS SLGNNVKIID RLPNNTIPVH YDINITPYLE EGNFTFYGES
     NVKIKIRYIT STISLHSREL KINETATKVI KDKDTTYRPL KHIHDNQTNI LSIIFIGIIT
     PGPYILHMEF AGNLLPVSQR RGFIKFSYIN DKENNTKWLA VTNFEPNGAR LMLPCWDEPA
     LKATFDISVK HSQKYGVLSN MPIREQFLEQ DGMLRTNFHT TPLMSTYIVA IAMSEFVRVP
     NANETINMWC KSSLTSKVTF SHSVAEKVVE FLIEYTNSSQ KVPKMDHILI PNFVVGGMEN
     WGLITYRESG IIYDNSDPIY QKTEAALVVA HELAHQWFGN LVTPSWWPYL WLSEGFASFF
     ESYTIDKIFK DWRRMDLFVI QTMQQCFLKD TGLLNSVTLK IGNTLDEKSL FSTEVYKKAP
     VLLRMLHNTI TAEVFRKGLI TYLATHQFST ATPDDLWSAM QSALDESDVP HEGYRIKEVM
     DTWMNQERYP FVHVERNYET GEVTISQSCV RQHGETEMKT TKWWIPITFA TQSNLDFSNT
     VPRYWLRPDQ HNISFIINPN DWIIVNLQLT GYVEDPNDDH ITKLTRLYAL QMACFFGHEE
     CKKMSALKLS EYLANHEIHK IPSFMYCTGM MTASRTTWDK MLELYLNKEI HLKEQDYDKR
     LLWGLSCAEN PNIVKDYLNM AARNTSLFPN TDHSFIFNFI IRKHVNNDII LDYILNNFMI
     LKPM
//
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