ID   A0A1I8JMM1_9PLAT        Unreviewed;       538 AA.
AC   A0A1I8JMM1;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   28-JUN-2023, entry version 18.
DE   RecName: Full=Angiotensin-converting enzyme {ECO:0000256|RuleBase:RU361144};
DE            EC=3.4.-.- {ECO:0000256|RuleBase:RU361144};
OS   Macrostomum lignano.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC   Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX   NCBI_TaxID=282301 {ECO:0000313|Proteomes:UP000095280, ECO:0000313|WBParaSite:maker-uti_cns_0049239-snap-gene-0.6-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:maker-uti_cns_0049239-snap-gene-0.6-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (NOV-2016) to UniProtKB.
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   AlphaFoldDB; A0A1I8JMM1; -.
DR   WBParaSite; maker-uti_cns_0049239-snap-gene-0.6-mRNA-1; maker-uti_cns_0049239-snap-gene-0.6-mRNA-1; maker-uti_cns_0049239-snap-gene-0.6.
DR   Proteomes; UP000095280; Unplaced.
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; -; 1.
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   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   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Zinc {ECO:0000256|RuleBase:RU361144}.
SQ   SEQUENCE   538 AA;  61579 MW;  79D96C97F0A92BE0 CRC64;
     YGQLSTQMSG IYSTAQVPHP DTGKMMQLDP DITDALADPN ESERVKRALW QGWRDASGKR
     MRQNYTDFVT MGNLMIREAG YSNIAQYWQS WYEPRPGQNF TDMMAKLWDV ALPFYQQLHA
     YVRRKLRDKY GAELFPETGH IPAHLLGNMW AQSWFNVEKL TTPFPDLSTV DITEKMNKLG
     WNATKMFRVS EEFFTSIGLD PMTDTFWEKS VLTRLPDVKM VCHASAWDFY TNKGDFRIKQ
     CTSITTNYLG TTHHEMGHVQ YYQQYEKQPV LYRRGANPGF HEAVGDTLEL AVMTPGHLHK
     IGLLDEIIES KDYYLNYLFQ MALQKAAFIP FGYLIDLWRW QASEGRLAPE KYNEGWWKLR
     CGLQGVSSPV PRSEDDFDPG AKYHVPNNTP YIRYFVSHFL QFQLYEALCN ISGHNGPLYK
     CDFYQNKQAG DALKKFLAHG SSLHWEDVLL ELTDTTELRA DSLVRYFAEL NEFLTEENKK
     SGERVGWDAD CPSADWYTTT TSAPETTTLA AGRAATSGTV GLWAAVGAAA LARRLLAV
//