ID   A0A0V1DHK6_TRIBR        Unreviewed;       927 AA.
AC   A0A0V1DHK6;
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   Name=Ace {ECO:0000313|EMBL:KRY61047.1};
GN   ORFNames=T03_3802 {ECO:0000313|EMBL:KRY61047.1};
OS   Trichinella britovi (Parasitic roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY61047.1, ECO:0000313|Proteomes:UP000054653};
RN   [1] {ECO:0000313|EMBL:KRY61047.1, ECO:0000313|Proteomes:UP000054653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS120 {ECO:0000313|EMBL:KRY61047.1};
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:KRY61047.1}.
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DR   EMBL; JYDI01000003; KRY61047.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V1DHK6; -.
DR   STRING; 45882.A0A0V1DHK6; -.
DR   Proteomes; UP000054653; 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:UP000054653};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Zinc {ECO:0000256|RuleBase:RU361144}.
FT   DOMAIN          802..838
FT                   /note="EB"
FT                   /evidence="ECO:0000259|Pfam:PF01683"
SQ   SEQUENCE   927 AA;  104826 MW;  9BAB093B2ED6F0E2 CRC64;
     MIVVLLFFTV GRLSIVKYCL WVVAIDSFES FKRCLVMNAS LCRSVTMKAL IAKRSFENGV
     VEKKVIIYFC KQQSAAIPSY SQIIFTNGCW LLLNIFITLS SSQRPDGTTR APPQAIASEN
     VVNELISRLL SGNGGDISSD LQQNSINIPT VNGGTVNRDD PYWNASDILE PNSVNDETAA
     LKFLVDYDKQ AEEVFSKSAE AGWCFLTNMT ANTRKELAEM DKTVVEFLHI SAKRAKQFNL
     NSIHNKKAKK QIKNLSQEGI YVLPEKKLEQ FISVQAKINQ VFADGTVCEP SRPPPCTMPL
     EPDLQRIMAT SRDVNELYYV WLAWRNAVGP PMKQSYLEMV DLFNEIAKLN GLKHGGEIWQ
     NTYGENVNLI NLLEKIYDEV RPLYDQLHAY IRNQLRKQYA SFMHQDGQIP AHLLVKFSTG
     DMSGSNWINL YSDSVPYPEH HPLDVNYHLK SLNYTVEKMV RTAEKLFTSM GFGRLPKSFW
     DYSIFVRPND RDMVCYPAAF DFKNQKDFRI KMCAQVTWED FIQLIRQMTS TYYQIAYKEQ
     PISFREAANP AISYALTNAL ALSVSSEDFM HSVGILPDLE NSQEKTINYL YNIALREVAF
     IPYGVLADKW RWSLFSGDID ATNMNEKWWE YRMKYQGVKS PARRDSNDFD PGSNYQIAQN
     LPFSRQVNVI GYVIQFQVLK GLCSAIGYQG PLHRCHFFEG KLAGEKLISA MKLGASENWT
     DVLKILSGSE EISGAAMMEY MEPLIQWLVK TNAETGETIG WNEYPDQFNE AEITLAKNIS
     KKLPVGDIKN NAHSVSDLEG IAFPGEDCSQ GQQCLADSTC NGTVCVCPPN SVPWYQTCLP
     NDPTMVGFGP GGEGFQLDLI KEELVTEEST SSQEESNDIN GSTSSMQWKW LSIFSASVAE
     KYLPADTGCS YAAEQLCDDF SLYYNHQ
//