ID   B3RUA8_TRIAD            Unreviewed;      1127 AA.
AC   B3RUA8;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   24-JAN-2024, entry version 69.
DE   RecName: Full=Angiotensin-converting enzyme {ECO:0000256|RuleBase:RU361144};
DE            EC=3.4.-.- {ECO:0000256|RuleBase:RU361144};
GN   ORFNames=TRIADDRAFT_37492 {ECO:0000313|EMBL:EDV25300.1};
OS   Trichoplax adhaerens (Trichoplax reptans).
OC   Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC   Trichoplax.
OX   NCBI_TaxID=10228 {ECO:0000313|EMBL:EDV25300.1, ECO:0000313|Proteomes:UP000009022};
RN   [1] {ECO:0000313|EMBL:EDV25300.1, ECO:0000313|Proteomes:UP000009022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV25300.1,
RC   ECO:0000313|Proteomes:UP000009022};
RX   PubMed=18719581; DOI=10.1038/nature07191;
RA   Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U.,
RA   Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L.,
RA   Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J.,
RA   Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., Dellaporta S.L.,
RA   Rokhsar D.S.;
RT   "The Trichoplax genome and the nature of placozoans.";
RL   Nature 454:955-960(2008).
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   -!- SIMILARITY: Belongs to the peptidase M2 family.
CC       {ECO:0000256|ARBA:ARBA00008139, ECO:0000256|RuleBase:RU361144}.
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DR   EMBL; DS985244; EDV25300.1; -; Genomic_DNA.
DR   RefSeq; XP_002111333.1; XM_002111297.1.
DR   AlphaFoldDB; B3RUA8; -.
DR   SMR; B3RUA8; -.
DR   STRING; 10228.B3RUA8; -.
DR   MEROPS; M02.004; -.
DR   EnsemblMetazoa; TriadT37492; TriadP37492; TriadG37492.
DR   GeneID; 6753027; -.
DR   KEGG; tad:TRIADDRAFT_37492; -.
DR   CTD; 6753027; -.
DR   eggNOG; KOG3690; Eukaryota.
DR   HOGENOM; CLU_006219_0_0_1; -.
DR   InParanoid; B3RUA8; -.
DR   OMA; DYSDFQD; -.
DR   OrthoDB; 2898149at2759; -.
DR   PhylomeDB; B3RUA8; -.
DR   Proteomes; UP000009022; 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; 2.
DR   Gene3D; 1.10.1370.30; -; 3.
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   Metal-binding {ECO:0000256|RuleBase:RU361144};
KW   Metalloprotease {ECO:0000256|RuleBase:RU361144};
KW   Protease {ECO:0000256|RuleBase:RU361144};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009022};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Zinc {ECO:0000256|RuleBase:RU361144}.
SQ   SEQUENCE   1127 AA;  130419 MW;  2BE4C96A96645726 CRC64;
     MSADVKRQFF FLTLDDSPKD STKLQELLAT IAKMESTYSK GRVCNKTRCY VLNPDLYSII
     GKSRNYDELV FAWKGWRDSV GRNVKRDYMK YVEISNIGAT DNNYADEGAY WRVQYELPDE
     QFFAELEKLW TQMKPFYEQL HGYIRGKLRQ KYGKDKISED GPIPAHLLGN MWAQSWENLY
     DMVVPYPNQP IVDVTSEMVR QNYTVLKMFE LSEEFFLSIG MKKLPEIFWR NSIIEKRKDV
     AMTCHASAWD LSIDYDVRVK MCTNINQGDL ITVHHELGHI QYYLQYWDQP SVYRRGANPG
     FHEAVGDTLA LSVVTPKHLQ NIGLLKQVSS SNEADINYLL SQALDKIAFI PFGYLMDQWR
     WKVFSGEIIP TDYNYNWWEL RNKYQGIVPP ELRSEIDFDP GAKYHIPASV PYIRYFVSYI
     LQFQFQRSLC QAANKTNEPL YLCSIYQSQE AGEKLSEMLS LGRSKPWPEV LKALTGGTGM
     DATAIIDYFK PLNDWLTKYN KDNNFKVGWA GNGTVKQQAI KFVMWYQHEA EKIYHKNTWY
     QWNYSTNLTS HNAKLSAESS INTTAAIVAL RRKGHSLQNV SINSEIDRQL RIATFIPASA
     GSPESEELVG VNNEMDRLYS TGKACNGTTC YSLNPGLDGI LAKSRDYNEL LFAWHGWRNG
     TGPSIKPYYI KYVSLMNTLA KQANYSDAGA RWRSRYGNNS KAFTDNVQKL WLQLKPFYQN
     LHAYVRKRLR EKYGADKVSR TGPVPAHLFG NMWAQSWINI YDMLVPYPKK QILDVTDEMV
     KQNYTVKKIF EVADEFFVSM GLERVPKSFW KNSMLEKPKD RQAICHASAW DFYRGDVRFK
     MCTQINFDDF LTVHHEMGHI QYYLQYGFQP LNYRSGANPA FHEAVGDTIS LSVTTPDHLR
     KVGLLKSSEN DQESAINYLM LQALDKIAFL PFGYLVDQWR WKVFDGSITP ENYNKAWWEL
     RTKYQGIIPP VSRTEEDFDP GAKYHIPGST PYIRYFISYI IQFQFQKALC QAAGNTQPLY
     LCSVYQSKEA GKRLGDMLKL GRSKSWEDAM EAITGQREMD ASAIVEYFKP LDDWLKEQNK
     DEVIGWDTTT TKPQVTTPST GSAGRAFTWS TLFIALFTCL IAFDLRW
//