ID   A0A0N4XTT4_NIPBR        Unreviewed;       671 AA.
AC   A0A0N4XTT4;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Angiotensin-converting enzyme {ECO:0000256|RuleBase:RU361144};
DE            EC=3.4.-.- {ECO:0000256|RuleBase:RU361144};
GN   ORFNames=NBR_LOCUS6045 {ECO:0000313|EMBL:VDL69634.1};
OS   Nippostrongylus brasiliensis (Rat hookworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Heligmosomidae; Nippostrongylus.
OX   NCBI_TaxID=27835 {ECO:0000313|Proteomes:UP000038043, ECO:0000313|WBParaSite:NBR_0000604401-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:NBR_0000604401-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDL69634.1, ECO:0000313|Proteomes:UP000271162}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) 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}.
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DR   EMBL; UYSL01019772; VDL69634.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N4XTT4; -.
DR   STRING; 27835.A0A0N4XTT4; -.
DR   WBParaSite; NBR_0000604401-mRNA-1; NBR_0000604401-mRNA-1; NBR_0000604401.
DR   OMA; IQKFQWR; -.
DR   Proteomes; UP000038043; Unplaced.
DR   Proteomes; UP000271162; 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:UP000271162};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|RuleBase:RU361144}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..671
FT                   /note="Angiotensin-converting enzyme"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5033232443"
FT   REGION          30..112
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   671 AA;  75344 MW;  B163BC620596A865 CRC64;
     MRLRFHRVAF GLWIIACLIG VQMAAESTAN QDKASDTSKE PFEFNDDGES GSQMSGNASV
     PRPEPRASAA AAPASSPKAE PAPIPHPEPE PEPKPEPEPA ASTATHVPEP EPAIKFDNIQ
     SEDYGDVVEL KNQPDDLDTE VIEQLVDRFL NTGSLADKNA PKAANPAAQA LIGSSSYWNT
     DGLKEPGSIK DEATIRSWIQ GYQTEAQKVL KEVAAAGWKY FSHASPGAKQ SLNEAEQVLS
     RFVRATSVQA KQFDMESIAD ADLKRQLAYV SFEGMSALST ADYAAFNQAQ NTLNREASEV
     SVCDFEVPPP CALKKIDLES IFRSENSGKR LSHLWITYLT KLAREKPVYQ KLINLTNKGA
     KANGFTDGGA MWRSAFDLST KNKPPVFDLQ EQIETIYQKI EPLYKQLHSY MRRQIAGIYN
     NPAGLSKNGP IPAHLFGSLD GGDWSAHYEQ TKPYDDQSTL AEDMLFSFHT QNYTTKQMFV
     KAYRYFKSIG FPSLPKTFWI SSHFSRVWSR DMICNPPAAL DMRDGSDYRV KLCAQLGMPD
     FELAHSLMAQ VYYQYLYRGQ PLLYREPASS SISDAIAKVF FHLSTNPHYL YSQKLVPASH
     LDIKDSLVIN KLYKEALESF TKLPFDIVAD KWRYEQFEGK VTPAKVNDRW WELRRILISD
     MLQKRELSHV V
//