ID   A0A0V0VMT4_9BILA        Unreviewed;       869 AA.
AC   A0A0V0VMT4;
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};
GN   ORFNames=T09_3260 {ECO:0000313|EMBL:KRX64774.1};
OS   Trichinella sp. T9.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX64774.1, ECO:0000313|Proteomes:UP000054681};
RN   [1] {ECO:0000313|EMBL:KRX64774.1, ECO:0000313|Proteomes:UP000054681}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS409 {ECO:0000313|EMBL:KRX64774.1};
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:KRX64774.1}.
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DR   EMBL; JYDN01000021; KRX64774.1; -; Genomic_DNA.
DR   Proteomes; UP000054681; 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; 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:UP000054681};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Zinc {ECO:0000256|RuleBase:RU361144}.
FT   DOMAIN          761..797
FT                   /note="EB"
FT                   /evidence="ECO:0000259|Pfam:PF01683"
SQ   SEQUENCE   869 AA;  98321 MW;  E267AD94208CC723 CRC64;
     MNASLCRSVT MKALIAKRSF ENGQQSAAIP SYSQIIFTNG CWLLLNIFIT LSSSQRPDDT
     TRAPPQAIAS ENVVNELISR LLSGNGGDIS SDLQQNSINI PTVNGGTVNR DDPYWNASDI
     LEPNSVNDET AALKFLVDYD KQAEEVFSKS AEAGWCFLTN MTANTRKELA EMDKTVVEFL
     HISAKRAKQF NLNSIHNKKA KKQIKNLSQE GIYVLPEKKL EQFISVQAKI NQVFADGTVC
     EPSRPPPCTM PLEPDLQRIM ATSRDVNELY YVWLAWRNAV GPPMKQSYLE MVDLFNEIAK
     LNGLKHGGEI WQNTYGENVN LINLLEKIYD EVRPLYDQLH AYIRNQLRKQ YASFMHQDGQ
     IPAHLLVKFS TGDMSGSNWI NLYSDSVPYP EHHPLDVNYH LKSLNYXXXX XNYTVEKMVR
     TAEKLFTSMG FGRLPKSFWD YSIFVRPNDR DMVCYPAAFD FKNQKDFRIK MCAQVTWEDF
     IQLIRQMTST YYQIAYKEQP ISFREAANPA ISYALTNALA LSVSSEDFMH SVGILPDLEN
     SQEKTINYLY NIALREVAFI PYGVLADKWR WSLFSGDIDA TNMNEKWWEY RMKYQGVKSP
     ARRDSNDFDP GSNYQIAQNL PFSRQVNVIG YVIQFQVLKG LCSAIGYQGP LHRCHFFEGK
     LAGEKLISAM KLGASENWTD VLKILSGSEE ISGAAMMEYM EPLIQWLVKT NAETGETIGW
     NEYPDQFNEA EITLAKNISK KLPVGDIKNN AHSVSDLEGI AFPGEDCSQG QQCLADSTCN
     GTVCVCPPNS VPWYQTCLPN DPTMVGFGPG GEGFQLDLIK EELVTEESTS SQEESNDING
     STSSMQWKWL SIFSGVLFCL VHFKMYTTF
//