ID   A0A0V0U215_9BILA        Unreviewed;       703 AA.
AC   A0A0V0U215;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   28-JUN-2023, entry version 19.
DE   RecName: Full=Angiotensin-converting enzyme {ECO:0000256|RuleBase:RU361144};
DE            EC=3.4.-.- {ECO:0000256|RuleBase:RU361144};
GN   Name=Ace {ECO:0000313|EMBL:KRX44691.1};
GN   ORFNames=T05_10450 {ECO:0000313|EMBL:KRX44691.1};
OS   Trichinella murrelli.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=144512 {ECO:0000313|EMBL:KRX44691.1, ECO:0000313|Proteomes:UP000055048};
RN   [1] {ECO:0000313|EMBL:KRX44691.1, ECO:0000313|Proteomes:UP000055048}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS417 {ECO:0000313|EMBL:KRX44691.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-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}.
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:KRX44691.1}.
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DR   EMBL; JYDJ01000091; KRX44691.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0U215; -.
DR   STRING; 144512.A0A0V0U215; -.
DR   Proteomes; UP000055048; 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   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   Reference proteome {ECO:0000313|Proteomes:UP000055048};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|RuleBase:RU361144}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..703
FT                   /note="Angiotensin-converting enzyme"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006869822"
FT   REGION          634..667
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        638..654
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   703 AA;  81131 MW;  D15030EE71832D66 CRC64;
     MIPCGIKEHF PLVLLLLMNT LWYATSDEDE EAKLEACLKQ YDEEGRKTMS RVVAIQRNLF
     QDFNDQSVKN FNEISCRAQD WLCNVRHKLQ AVSVENITDE NSKIARTNIL HRTGPCANGS
     LWSAAQTELT RMLRIYNKEI CALNDAAKDC SVKWSLYSDI FNKLANASNP LLLLYIWQEW
     REIENLGQMR ASFATAYGAL KNASIGAGYA DLGDWWRHAY STTENFDVEN ASRTIFYDLL
     PLYEELHAYV KHKLTNRNSL YIPLIGSHLV QSLFGDQWQQ LYRWTRPDKS LPNLDITAVL
     KETYRSVSHM FDEIKKYFSD IGLHGEIICK TSCMYEKPPK KAKLHPICKP TFYDLYDDND
     DWSYTVSMCG QIDSNTMGEM FRLIGQGIYA REYSEQKMYF RQPANAGLFS AIGEAIALSY
     FQPKTLNETY NISISDTELA DVDFLYRQAL LKLPSVMYSY ATDLWRWQLF RSDDVENRDW
     VKMENSWWTT MNKYMGLANP RPSNVNMSDF LVVPEVILFE PHIGSLFSTI FQFQIYEYAC
     EIVNHKDALH KCTFGKKKKI SQLFEQLMNV GSEKEWSLLL SETLHSNLNS SSLLKYFQPL
     HQWLIMENDK TSACRGWYAD EEWPREVLLK LSPKRCKKEP PAPPPPPPTE GPEPVTKPDD
     QLNSADRVGK YTMVSTTIFD TFPLSASDFL KIFSNAGLPD GNP
//