ID   A0A0N0BEI9_9HYME        Unreviewed;       648 AA.
AC   A0A0N0BEI9;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Angiotensin-converting enzyme {ECO:0000256|RuleBase:RU361144};
DE            EC=3.4.-.- {ECO:0000256|RuleBase:RU361144};
DE   Flags: Fragment;
GN   ORFNames=WN51_03245 {ECO:0000313|EMBL:KOX71968.1};
OS   Melipona quadrifasciata.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC   Anthophila; Apidae; Melipona.
OX   NCBI_TaxID=166423 {ECO:0000313|EMBL:KOX71968.1, ECO:0000313|Proteomes:UP000053105};
RN   [1] {ECO:0000313|EMBL:KOX71968.1, ECO:0000313|Proteomes:UP000053105}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0111107301 {ECO:0000313|EMBL:KOX71968.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KOX71968.1};
RA   Pan H., Kapheim K.;
RT   "The genome of Melipona quadrifasciata.";
RL   Submitted (JUL-2015) 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 1 zinc ion per subunit. {ECO:0000256|RuleBase:RU361144};
CC   -!- SIMILARITY: Belongs to the peptidase M2 family.
CC       {ECO:0000256|ARBA:ARBA00008139, ECO:0000256|RuleBase:RU361144}.
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DR   EMBL; KQ435827; KOX71968.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N0BEI9; -.
DR   STRING; 166423.A0A0N0BEI9; -.
DR   OrthoDB; 2898149at2759; -.
DR   Proteomes; UP000053105; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
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; 1.
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; 1.
DR   PRINTS; PR00791; PEPDIPTASEA.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000256|RuleBase:RU361144};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180,
KW   ECO:0000256|RuleBase:RU361144}; Hydrolase {ECO:0000256|RuleBase:RU361144};
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:UP000053105};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|RuleBase:RU361144}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..648
FT                   /note="Angiotensin-converting enzyme"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005844825"
FT   COILED          33..67
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KOX71968.1"
SQ   SEQUENCE   648 AA;  75503 MW;  5A0725B466EC6680 CRC64;
     VTKLQRKFHR LLVAVLVTVA WGIPTPEDTS NAAADSEQDL QRAKQFLEQL NEEYGEWNNK
     YTLANWEYAA NLTEENLAKK LNVSAETARY FKSAWEKVNV YPWKDIKDSG IRRQFKKFSV
     LGRSALPEDR YQEYEKIISD MENIYSTAKI CDYKNRSKCD LALEPELTEL LMKSRDPEEL
     KYIWIEWRKA TGEKVKSLYP KYVELSNLAA TLNNFSDNAA YWLKDYEADD FPEQIETLWQ
     QLKPLYLQLH AYVRRELRKK YGENVVSKDG PIPAHLLGNM WAQTWTNIAD FAIPYPGKQM
     PDVTHAMIKQ GYNATTIFRV AEDFFTSINL TAMPDLFWQR SILEKPKDRE LICHASAWDF
     YDGKDFRIKQ CTRVNMEDLL TAHHEMGHVE YYLQYKDQPN IFKEGANPGF HEAVGDVISL
     SASTPSHLKA IKLLDDDSTD TEANINHLFL KGLEKIVFLP FAYMMDKWRW NVFQGQVTSD
     NYNCNWWDLA EEFQGIEPPV DRSEDDFDPG AKYHIIADVE YMRYFVSFVV QFQFHKALCI
     EAKQYDPQNP NSKLLHECDI YNNKAAGNLL KNMLELGSSK PWQDAMEKIT GQKSMESAGL
     LEYFKPLTDW LTAENKKTNE YIGWKPKARQ CVQTRSELAS FEETEAEE
//