ID   A0A067QH02_ZOONE        Unreviewed;       721 AA.
AC   A0A067QH02;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Angiotensin-converting enzyme {ECO:0000256|RuleBase:RU361144};
DE            EC=3.4.-.- {ECO:0000256|RuleBase:RU361144};
GN   ORFNames=L798_08577 {ECO:0000313|EMBL:KDQ71574.1};
OS   Zootermopsis nevadensis (Dampwood termite).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Polyneoptera; Dictyoptera; Blattodea; Blattoidea; Termitoidae;
OC   Termopsidae; Zootermopsis.
OX   NCBI_TaxID=136037 {ECO:0000313|EMBL:KDQ71574.1, ECO:0000313|Proteomes:UP000027135};
RN   [1] {ECO:0000313|EMBL:KDQ71574.1, ECO:0000313|Proteomes:UP000027135}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Whole organism {ECO:0000313|EMBL:KDQ71574.1};
RX   PubMed=24845553; DOI=10.1038/ncomms4636;
RA   Terrapon N., Li C., Robertson H.M., Ji L., Meng X., Booth W., Chen Z.,
RA   Childers C.P., Glastad K.M., Gokhale K., Gowin J., Gronenberg W.,
RA   Hermansen R.A., Hu H., Hunt B.G., Huylmans A.K., Khalil S.M.,
RA   Mitchell R.D., Munoz-Torres M.C., Mustard J.A., Pan H., Reese J.T.,
RA   Scharf M.E., Sun F., Vogel H., Xiao J., Yang W., Yang Z., Yang Z., Zhou J.,
RA   Zhu J., Brent C.S., Elsik C.G., Goodisman M.A., Liberles D.A., Roe R.M.,
RA   Vargo E.L., Vilcinskas A., Wang J., Bornberg-Bauer E., Korb J., Zhang G.,
RA   Liebig J.;
RT   "Molecular traces of alternative social organization in a termite genome.";
RL   Nat. Commun. 5:3636-3636(2014).
CC   -!- SIMILARITY: Belongs to the peptidase M2 family.
CC       {ECO:0000256|ARBA:ARBA00008139, ECO:0000256|RuleBase:RU361144}.
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DR   EMBL; KK853828; KDQ71574.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A067QH02; -.
DR   EnsemblMetazoa; KDQ71574; KDQ71574; L798_08577.
DR   eggNOG; KOG3690; Eukaryota.
DR   InParanoid; A0A067QH02; -.
DR   Proteomes; UP000027135; 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:SF40; ANGIOTENSIN-CONVERTING ENZYME; 1.
DR   Pfam; PF01401; Peptidase_M2; 3.
DR   PRINTS; PR00791; PEPDIPTASEA.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 2.
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:UP000027135};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Zinc {ECO:0000256|RuleBase:RU361144}.
FT   REGION          254..275
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          694..721
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   721 AA;  83345 MW;  40A0CCF4B4E73E86 CRC64;
     MRFEALNCCE YVDIDIQQPP SEDLKLYLPA SSQGVTMYKP ASTTKMLLLA QLEYVDYQRA
     VWEILNKLTR EQVQEGPIWR QVQFLSVIGP AALPPELLDR YNKLINDMLS VLNGATTCAY
     NEPFRCGLRL EPELTVVMGR SRDWDELQQT WIEWRRLTGQ KMRDLFEQVV ELSNQAAQLN
     HFKNAAEYWL FPYESPTFRY ELEGVWEEVR PLYELLHAYV RRKLRDLYGP DKLSRKAPLP
     AHILGTCQER LRKTLKRPSQ DSRSPGRDLN SGAPVYEVGA LTTRPRRSVS GLKKHSIRLR
     LDSQGFIPYK VEFLPSPQRP DQLWNPPSPL PNGRWTSVAK TRSLPPAFIW YRAYGDMWGQ
     SWSNILDVTI PYPGKNFLDV TTEMVEQGYT PLTMFRLAEE FYVSLNMSVL PPEFWSGSII
     QQQPDRVVIC QPSAWDFCNR RDYRIKMCTE VNMKDFVTVH HEMGHLQYFL HYRHQPKVFR
     DGANPGFHEA VGEAVALSIA TPRHLQDLGL VQSSVDDVPH NINSLFSLAL DKLPFLPFSL
     VMDEWRWDIF EGTITSDQYN CHWWRLSLYI TIEPDDISMC ATIQATLPPY DRARMPDLEV
     SCQQPRQEAA SVAIQVYRCK PTEHNSTIST PLAIDHLFQP HNIKEKFSGI KPPVLRSEID
     FDAGSKYHIA ANVPYIRQNS SYISQVFRKT LRRKKNEGGE QFSIPTKMRG GQNNSPLLPI
     L
//