ID   A0A091S2P1_NESNO        Unreviewed;      1229 AA.
AC   A0A091S2P1;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Angiotensin-converting enzyme {ECO:0000256|RuleBase:RU361144};
DE            EC=3.4.-.- {ECO:0000256|RuleBase:RU361144};
DE   Flags: Fragment;
GN   ORFNames=N333_13026 {ECO:0000313|EMBL:KFQ49686.1};
OS   Nestor notabilis (Kea).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Psittaciformes; Psittacidae; Nestor.
OX   NCBI_TaxID=176057 {ECO:0000313|EMBL:KFQ49686.1, ECO:0000313|Proteomes:UP000053840};
RN   [1] {ECO:0000313|EMBL:KFQ49686.1, ECO:0000313|Proteomes:UP000053840}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N333 {ECO:0000313|EMBL:KFQ49686.1};
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|RuleBase:RU361144};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|RuleBase:RU361144};
CC   -!- COFACTOR:
CC       Name=chloride; Xref=ChEBI:CHEBI:17996;
CC         Evidence={ECO:0000256|ARBA:ARBA00001923};
CC   -!- SIMILARITY: Belongs to the peptidase M2 family.
CC       {ECO:0000256|ARBA:ARBA00008139, ECO:0000256|RuleBase:RU361144}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KK939626; KFQ49686.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091S2P1; -.
DR   MEROPS; M02.004; -.
DR   Proteomes; UP000053840; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008241; F:peptidyl-dipeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd06461; M2_ACE; 2.
DR   Gene3D; 1.10.1370.30; -; 2.
DR   InterPro; IPR001548; Peptidase_M2.
DR   PANTHER; PTHR10514; ANGIOTENSIN-CONVERTING ENZYME; 1.
DR   PANTHER; PTHR10514:SF27; ANGIOTENSIN-CONVERTING ENZYME; 1.
DR   Pfam; PF01401; Peptidase_M2; 2.
DR   PRINTS; PR00791; PEPDIPTASEA.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 2.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000256|RuleBase:RU361144};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180,
KW   ECO:0000256|RuleBase:RU361144}; Hydrolase {ECO:0000256|RuleBase:RU361144};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|RuleBase:RU361144};
KW   Metalloprotease {ECO:0000256|RuleBase:RU361144};
KW   Protease {ECO:0000256|RuleBase:RU361144};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053840};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|RuleBase:RU361144}.
FT   TRANSMEM        1189..1210
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFQ49686.1"
FT   NON_TER         1229
FT                   /evidence="ECO:0000313|EMBL:KFQ49686.1"
SQ   SEQUENCE   1229 AA;  142110 MW;  3EF40F309BB192DC CRC64;
     SPRWWHVPGL TPGPHVAEQV EASLEEQEFM EVWGKKAKEL YGSIWSNFSD TQLRKIISSI
     QTLGPSNLPL DKREQYNTIL SDMDKIYSTA KVCLANSTCW ELEPDISDIM ATSRSYKKLL
     YAWEGWHNAA GNPLRAKYEE FVQLSNEAYQ MDGFEDTGSY WRSWYDSASF EDDLEHLYNQ
     VEPLYLNLHA FVRRKLYDRY GSKYINLKGP IPAHLLGNMW AQQWNNIYDL MIPYPDKPNL
     DVTSTMVQQG WNATHMFRVS EEFFTSLGLL EMPPEFWDKS MLEKPADGRE VVCHASAWDF
     YNRKDFRIKQ CTTVTMEQLF TVHHEMGHIQ YYLQYKDQPV SFRSGANPGF HEAIGDVMSL
     SVSTPSHLKE IGLLNSAAED TESNINYLLK MALEKIAFLP FGYLIDQWRW NVFSGRTPPS
     RYNYDWWYLR TKYQGICAPI SRNESNFDPG AKYHIPGNTP YIRYFVSFIL QFQFHKVLCQ
     AANHSGPLHT CDIYMSKEAG DKLREVLKAG SSKSWQEILF NLTGTDKMDA GALLEYFSPV
     TEWLQEQNNK TNEVLGWPEF DWRPPIPEGY PEGIDKISDE AQAKEFLAEY NSTAEAVWNA
     YTEASWAYNT NITDHNKEIM LEKNLAMSRH TLEYGMRARQ FDPSDFQDQS VTRILRKLSV
     IERAALPEDE LKEYNTLLSD METTYSIAKV CRENKTCHPL DPDLTDIMAT SRDYDELLFV
     WKGWRDASGK QIKNNYKRYV ELSNKAAVLN GYSDNGAFWR SLYETSTFEE DLERLYLQLQ
     PLYLNLHAYV RRALYRKYGG EHINLKGPIP AHLLGNMWAQ SWSNIFDLVM PFPDATKVDA
     TPAMKQQGWT PKRMFEESDR FFTSLGLIPM PEEFWDKSMI EKPADGREVV CHASAWDFYN
     RKDFRIKQCT VVNMDDLITV HHEMGHVQYF LQYMDQPISF RDGANPGFHE AVGDVMALSV
     STPKHLHSIN LLDQVTDNTE SDINYLMSIA LDKIAFLPFG YLMDQWRWKV FDGRIKEDEY
     NQEWWNLRLK YQGLCPPTPR SEDDFDPGAK FHIPANVPYI RYFVSFVIQF QFHQALCAAA
     KHTGPLHTCD IYQSKEAGNI LGEALKLGFS KPWPEAMELI TGQPNMSADA LMSYFEPLMT
     WLVNENEKNE EVLGWPEYSW TPYTATTAQA GSSRTDFLGM SLASNQATAG SWVLLALALV
     FLITTIYLGV KFSSARRKTF KSSSEMELK
//