ID A0A0V0XDH0_9BILA Unreviewed; 855 AA.
AC A0A0V0XDH0;
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:KRX85683.1};
GN ORFNames=T06_8104 {ECO:0000313|EMBL:KRX85683.1};
OS Trichinella sp. T6.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX85683.1, ECO:0000313|Proteomes:UP000054673};
RN [1] {ECO:0000313|EMBL:KRX85683.1, ECO:0000313|Proteomes:UP000054673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS34 {ECO:0000313|EMBL:KRX85683.1};
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:KRX85683.1}.
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DR EMBL; JYDK01000001; KRX85683.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0XDH0; -.
DR Proteomes; UP000054673; 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:UP000054673};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Zinc {ECO:0000256|RuleBase:RU361144}.
FT DOMAIN 747..783
FT /note="EB"
FT /evidence="ECO:0000259|Pfam:PF01683"
SQ SEQUENCE 855 AA; 96971 MW; 32373173144D66DA CRC64;
MRRVIEPSLQ LSRKVIIYFC KQQSAAIPSY SQIIFTNGCW LLLNIFITLS SSQRPDDTTR
APPQAIASEN VVNELISRLL SGNGGDISSD LQQNSINIPT VNGGTVNRDD PYWNASDILE
PNSVNDETAA LKFLVDYDKQ AEEVFSKSAE AGWCFLTNMT ANTRKELAEM DKNVVEFLHI
SAKRAKQFNL NSIHNKKAKK QIKNLSQEGI YVLPEKKLEQ FISVQAKINQ VFADGTVCEP
SRPPPCTMPL EPDLQRIMAT SRDVNELYYV WLAWRNAVGP PMKQSYLEMV DLFNEIAKLN
GLKHGGEIWQ NTYGENVNLI NLLEKIYDEV RPLYDQLHAY IRNQLRKQYA SFMHQDGQIP
AHLLGDMSGS NWINLYSDSV PYPEHHPLDV NYHLKSLNYT VEKMVRTAEK LFTSMGFGRL
PKSFWDYSIF VRPNDRDMVC YPAAFDFKNQ KDFRIKMCAQ VTWEDFKQLI RQMTSTYYQI
AYKEQPISFR EAANPAISYA LTNALALSVS SEDFMHSVGI LPDLENSQEK TINYLYNIAL
REVAFIPYGV LADKWRWSLF SGDIDATNMN EKWWEYRMKY QGVKSPARRD SNDFDPGSNY
QIAQNLPFSR QVNVIGYVIQ FQVLKGLCSA IGYQGPLHRC HFFEGKLAGE KLISAMKLGA
SENWTDVLKI LSGSEEISGA AMMEYMEPLI QWLVKTNAET GETIGWNEYP DQFNEAEITL
AKNISKKLPV GDIKNNAHSV SDLEGIAFPG EDCSQGQQCL ADSTCNGTVC VCPPNSVPWY
QTCLPNDPTM VGFGPGGEGF QLDLIKEELV TEESTSSQEE SNDINGSTSS MQWKWLSIFS
GVLFCLVHLK MYTTF
//