ID Q16W80_AEDAE Unreviewed; 602 AA. AC Q16W80; DT 25-JUL-2006, integrated into UniProtKB/TrEMBL. DT 25-JUL-2006, sequence version 1. DT 27-MAR-2024, entry version 98. DE RecName: Full=Angiotensin-converting enzyme {ECO:0000256|RuleBase:RU361144}; DE EC=3.4.-.- {ECO:0000256|RuleBase:RU361144}; DE Flags: Fragment; GN ORFNames=AAEL009310 {ECO:0000313|EMBL:EAT38830.1}; OS Aedes aegypti (Yellowfever mosquito) (Culex aegypti). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae; OC Culicinae; Aedini; Aedes; Stegomyia. OX NCBI_TaxID=7159 {ECO:0000313|EMBL:EAT38830.1, ECO:0000313|Proteomes:UP000682892}; RN [1] {ECO:0000313|EMBL:EAT38830.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Liverpool {ECO:0000313|EMBL:EAT38830.1}; RA Loftus B.J., Nene V.M., Hannick L.I., Bidwell S., Haas B., Amedeo P., RA Orvis J., Wortman J.R., White O.R., Salzberg S., Shumway M., Koo H., RA Zhao Y., Holmes M., Miller J., Schatz M., Pop M., Pai G., Utterback T., RA Rogers Y.-H., Kravitz S., Fraser C.M.; RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EAT38830.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Liverpool {ECO:0000313|EMBL:EAT38830.1}; RX PubMed=17510324; DOI=10.1126/science.1138878; RA Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J., RA Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M., Lobo N.F., RA Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J., Sinkins S.P., RA Hogenkamp D.G., Amedeo P., Arensburger P., Atkinson P.W., Bidwell S.L., RA Biedler J., Birney E., Bruggner R.V., Costas J., Coy M.R., Crabtree J., RA Crawford M., DeBruyn B., DeCaprio D., Eiglmeier K., Eisenstadt E., RA El-Dorry H., Gelbart W.M., Gomes S.L., Hammond M., Hannick L.I., RA Hogan J.R., Holmes M.H., Jaffe D., Johnston S.J., Kennedy R.C., Koo H., RA Kravitz S., Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S., RA Lovin D.D., Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P., RA Mori A., Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J., RA Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W., RA Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O., RA Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D., White O.R., RA Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A., Raikhel A.S., Soares M.B., RA Knudson D.L., Lee N.H., Galagan J., Salzberg S.L., Paulsen I.T., RA Dimopoulos G., Collins F.H., Bruce B., Fraser-Liggett C.M., Severson D.W.; RT "Genome sequence of Aedes aegypti, a major arbovirus vector."; RL Science 316:1718-1723(2007). RN [3] {ECO:0000313|EMBL:EAT38830.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Liverpool {ECO:0000313|EMBL:EAT38830.1}; RG VectorBase; RL Submitted (SEP-2012) 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CH477573; EAT38830.1; -; Genomic_DNA. DR RefSeq; XP_001659916.1; XM_001659866.1. DR AlphaFoldDB; Q16W80; -. DR STRING; 7159.Q16W80; -. DR PaxDb; 7159-AAEL009310-PA; -. DR GeneID; 5571787; -. DR KEGG; aag:5571787; -. DR VEuPathDB; VectorBase:AAEL023559; -. DR eggNOG; KOG3690; Eukaryota. DR OMA; QEWWNFR; -. DR OrthoDB; 2898149at2759; -. DR PhylomeDB; Q16W80; -. DR Proteomes; UP000682892; 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 Gene3D; 1.10.1370.30; -; 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 Signal {ECO:0000256|ARBA:ARBA00022729}; KW Zinc {ECO:0000256|RuleBase:RU361144}. FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:EAT38830.1" FT NON_TER 602 FT /evidence="ECO:0000313|EMBL:EAT38830.1" SQ SEQUENCE 602 AA; 70135 MW; B0AB9183B283BDE8 CRC64; LCHRAASLPQ VVVTNDVLNE EQMKQILQQY DTEVRSYCNR QVQANWNVAT NTENTTFQEE QNKISLEYAK FRTDFYEQYF KDAQVQNYED PKVRKQLTLL KDLGTAALPT SDLEEYNKVM RRMDAAYQLA EVCPYTDQNC APDAEKWTLD PEMEHVMASS NDYDELTYTW RRWREESGKK MRQDYKLYVD YVNQAAKLNG YADYGEMWRA RYDDSDLRGT LERLWKEVEP LYNELHTYVR FKLLDMYGDK MDRNNEKIPA HILGNMWAQS WVNLYDRIKP FPDASLVDVT AKMQELGFNA TKMFEMSDEF YQSLGLPSSA MSYGPKAVIE KQPQKMVCHA SAWDFCDGED FRVKMCTNIN MEDFITVHHE MGHIMYFILY KDQPQLFKTG ATPAFHEAVG DTIALSVATP KHLKLVGLLD EYADSEADNI NALFEMALER VAFLPFGYLI DQWRWDVFSG AVNESEWNSH WWNLREKYQK VYAPVSRSES DFDPGAKYHI PANSQYIAYF LAHILEFQFY RSLCIEAGEY NPSSSSANPL HKCDFYNSKA AGNKLKEGLS LGYSEDWRFA LEKLTGGQDI SGHALLEYFA PLYEFLKEEN AK //