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Database: UniProt
Entry: A0A3M7Q6Y1_BRAPC
LinkDB: A0A3M7Q6Y1_BRAPC
Original site: A0A3M7Q6Y1_BRAPC 
ID   A0A3M7Q6Y1_BRAPC        Unreviewed;      1614 AA.
AC   A0A3M7Q6Y1;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Aminopeptidase N {ECO:0000313|EMBL:RNA07170.1};
GN   ORFNames=BpHYR1_019646 {ECO:0000313|EMBL:RNA07170.1};
OS   Brachionus plicatilis (Marine rotifer) (Brachionus muelleri).
OC   Eukaryota; Metazoa; Spiralia; Gnathifera; Rotifera; Eurotatoria;
OC   Monogononta; Pseudotrocha; Ploima; Brachionidae; Brachionus.
OX   NCBI_TaxID=10195 {ECO:0000313|EMBL:RNA07170.1, ECO:0000313|Proteomes:UP000276133};
RN   [1] {ECO:0000313|EMBL:RNA07170.1, ECO:0000313|Proteomes:UP000276133}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HYR1 {ECO:0000313|EMBL:RNA07170.1};
RX   PubMed=30375419; DOI=10.1038/s41598-018-34188-y;
RA   Franch-Gras L., Hahn C., Garcia-Roger E.M., Carmona M.J., Serra M.,
RA   Gomez A.;
RT   "Genomic signatures of local adaptation to the degree of environmental
RT   predictability in rotifers.";
RL   Sci. Rep. 8:16051-16051(2018).
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}.
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:RNA07170.1}.
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DR   EMBL; REGN01007135; RNA07170.1; -; Genomic_DNA.
DR   SMR; A0A3M7Q6Y1; -.
DR   STRING; 10195.A0A3M7Q6Y1; -.
DR   Proteomes; UP000276133; 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; 2.
DR   Gene3D; 1.25.50.20; -; 2.
DR   Gene3D; 2.60.40.1910; -; 2.
DR   Gene3D; 1.10.390.10; Neutral Protease Domain 2; 2.
DR   Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 2.
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:SF276; AMINOPEPTIDASE; 1.
DR   PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR   Pfam; PF11838; ERAP1_C; 2.
DR   Pfam; PF01433; Peptidase_M1; 2.
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; 2.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000313|EMBL:RNA07170.1};
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:UP000276133};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT   DOMAIN          74..296
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
FT   DOMAIN          390..695
FT                   /note="ERAP1-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11838"
FT   DOMAIN          737..928
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          966..1189
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
FT   DOMAIN          1277..1593
FT                   /note="ERAP1-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11838"
FT   ACT_SITE        1038
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT   BINDING         1037
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   BINDING         1041
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   BINDING         1060
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   SITE            1122
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ   SEQUENCE   1614 AA;  186314 MW;  B2A7CBE7BA910232 CRC64;
     MSNMPINKTT QIGPKDGYNW TLTEFEETVQ MSTYLVAILV SDFKCKSGVS NSSYSNVDVK
     VCARPNAEDK LDLALNSSVD ILGFFEEYYK VKYPLEKLDH AGVPDFKYGA MENWGLAIYR
     EVYFIFDEKS TQTTEINVVR IIAHEISHMW FGNLVTPKWW DDLWLNEGFA RFAEHVGSDA
     VKKHWRMYDR LFDLLLGVIQ SDSTEETRAV SSDVNTPEEI DANINPTITY GKGSAIVKML
     SYILGDDTFR NGLKNYFETF EYQNVDQSDL WRIMNEQMKL ENKSHGVDLL PVMTSWTKQK
     GHPVVTIKRI NDTHISVKQN RFLTDSTVSG LSDTFWQIPL SFSIEELGSS GQSLTNKINS
     TNLFDKFLWI SNTTEETIIN LNRTLTDSNF LIANLDMAVF CRINYDEKDW KIIAEQLLTN
     TQELSARTRA QLISDVFSLS QALYISPEIA LNHIRYLENE LDYLPWSVFL ERVKYFTGQL
     DSTEIYIPFK KYLQKLVKPY YQKLGWIDNP VTDDWNDRVV RNRLVEFACQ VELADCLSQA
     RSIYNDFIDS GIQINVPSFL YRVAFCSSIE QGNDADFEKL FEKIKNTDSN LKSSMLYGLS
     CSKSTANLNK YLNDQMSSNS VISAIRNVLS KPSGVYVAWN FFKQNWENIY KDGSGISGIV
     SDLVKKLKTQ SDLNDIESFF SDKNLTQGDR ESLNVAKNQL LSNIKWFSQE FNSIKNWTSG
     LNIGNQVNYR LPTNLIPNSY DIKIQPYIGD SWKDKAFTFD GAISINFTCA EPTKKIIFHA
     IDLDLDTDTF TIESTDDNEI EKMFTEDKIT NFIELNLKKE CQKGSDYVLK MNYTGSIIKN
     LYGFYRSSYK NELDETEYLA TTHFQPTDAR RAFPCFDEPA LKASFKLTIM RHKNFSSSIF
     NTPLTKSSPN GDWFEDEFAE TPKMSTYLVA FVVSNFKKIT NQTSKGIEVE VFGRPEKIEN
     GEGDFSLRES QLILDFFENY FNLPYPLAKS SQIGVPDFNA GAMENWGAVI YRETALFYNP
     KTDALVNKQR VSSVVSHELA HQWFGNLVTP DWWNDIWLNE GFASWVEYLG VNYTHPEWNF
     LDLFYVQKLK VMELDSLESS HSVSFDVNDP GEINSLFDKI SYDKGSSIIR MMNAFLTEKT
     FRSGVSDYLK DFAYKNAKQD DLWQYLTNQS YVDGSLDKNL NVKDIMDTWT LKKGYPYVMV
     ERKYAEKEMV LTQKWFLLNP ASKIKDTEEY NNYKWYIPFT FTSLEDPIFD FEKKPTWLEP
     DQKEVKISTQ NIDDESWVIG NLKHSAFMRV NYDQDNWDLL IEQLKANHAV IDPINRATLL
     DDSFNLGRAE IIDQLLFLRI TQYLANEKEN LPFVPAFIGL DYIGNMIAND YFAYNNYKNY
     IINLMNSTYQ SLGWDDVSDD LIDLQISTLQ LMCSFGFEDC ITEARSRFDD WINNDIALPS
     NFKILIYSTV VKYGDEETWL NLYQKAIGIS DNTEKLRIFR GLASSREASL LSIILNSASD
     KNIIRSQDET SVISYVAGSP LGRKLAFDHL EDNWDELFER HGDVSFTLSS LIDSVTKYLN
     TNSYLLRLVN FAERNSNLGV TKKAFEQAIE NVQFNTRWTM KNLNSIKEWL NSNL
//
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