ID   A0A0V0YIB9_TRIPS        Unreviewed;       797 AA.
AC   A0A0V0YIB9;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   28-JUN-2023, entry version 17.
DE   RecName: Full=Angiotensin-converting enzyme {ECO:0000256|RuleBase:RU361144};
DE            EC=3.4.-.- {ECO:0000256|RuleBase:RU361144};
DE   Flags: Fragment;
GN   Name=acn-1 {ECO:0000313|EMBL:KRY00073.1};
GN   ORFNames=T4E_12273 {ECO:0000313|EMBL:KRY00073.1};
OS   Trichinella pseudospiralis (Parasitic roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=6337 {ECO:0000313|EMBL:KRY00073.1, ECO:0000313|Proteomes:UP000054815};
RN   [1] {ECO:0000313|EMBL:KRY00073.1, ECO:0000313|Proteomes:UP000054815}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS141 {ECO:0000313|EMBL:KRY00073.1};
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 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}.
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:KRY00073.1}.
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DR   EMBL; JYDU01000010; KRY00073.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0YIB9; -.
DR   Proteomes; UP000054815; 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; IPR006149; EB_dom.
DR   InterPro; IPR001548; Peptidase_M2.
DR   PANTHER; PTHR10514; ANGIOTENSIN-CONVERTING ENZYME; 1.
DR   PANTHER; PTHR10514:SF27; ANGIOTENSIN-CONVERTING ENZYME; 1.
DR   Pfam; PF01683; EB; 1.
DR   Pfam; PF01401; Peptidase_M2; 2.
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:UP000054815};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Zinc {ECO:0000256|RuleBase:RU361144}.
FT   DOMAIN          684..720
FT                   /note="EB"
FT                   /evidence="ECO:0000259|Pfam:PF01683"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KRY00073.1"
SQ   SEQUENCE   797 AA;  89396 MW;  41C04B3C065B2DD0 CRC64;
     LQEGPSKMGK VIIYLCKQQF AAIPSHSQII FTNGCWLLLN VFITLSSSQR PDGTTRAPPP
     AIASENVVNE LISRLLSGNG GDISSDLQQN SINIPTVNGG TVNRDDSYWN ASDILEPNSV
     NDETAALKFL VDYNKQAEEV FSKSAEAGWS FLTNMTANTR KDLAEMDKTV VEFLHISAKR
     AKQFNLNSIH NKKAKKQIKN LSQEGIYVLP EKKLEQFISV QAKINQVFAD GTVCEPSRPP
     PCTMPLEPDL QRIMATSRDV NELYYVWLAW RNAVGPPMKQ SYLEMVNLFN EIAKLNALFF
     TGDMSGSNWI NLYPDSVPYP EHHPLDVNYH LKSLNYTVEK MVRTAEKLFT SMGFGRLPGS
     FWDYSIFVQP NDRDMVCYPA AFDFKNQKDF RIKMCAQVTW EDFIQIVRQM TSTYYQIAYK
     EQPIAFREAA NPAISYALTN ALALSVSSED FMHSVGILPD LENSQEKTIN YLYNIALREV
     AFIPYGVLAD KWRWSLFSGD IDATNMNEKW WEYRMKYQGV KSPARRDNDD FDPGSNYQIA
     QNLPFSRQVN VIGYVIQFQV LKGLCSAIGY QGPLHRCHFF EGKLAGEKLI SAMKLGASEN
     WTDVLKIISG SEEISGAAMM EYMEPLIQWL VKTNAETGET IGWNEYPDQF NEAELTLAKN
     ISKKLPVGDI KNNAHSVSDL EGIAFPGEDC SQGQQCLADS TCNGTVCVCP PNSVPWYQTC
     LPNDPTMVGF GPGGEGFQLD LIKGELVTEE STSSQEESND INGSTSMQWK WLSIFSSVLF
     SSVAEKYLPA AAMQLNS
//