ID A0A0M4ED06_DROBS Unreviewed; 599 AA.
AC A0A0M4ED06;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Angiotensin-converting enzyme {ECO:0000256|RuleBase:RU361144};
DE EC=3.4.-.- {ECO:0000256|RuleBase:RU361144};
DE Flags: Fragment;
GN ORFNames=Dbus_chr2Lg1695 {ECO:0000313|EMBL:ALC39610.1};
OS Drosophila busckii (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=30019 {ECO:0000313|EMBL:ALC39610.1, ECO:0000313|Proteomes:UP000494163};
RN [1] {ECO:0000313|EMBL:ALC39610.1, ECO:0000313|Proteomes:UP000494163}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Whole larvae {ECO:0000313|EMBL:ALC39610.1};
RA Zhou Q., Bachtrog D.;
RT "Ancestral chromatin configuration constrains chromatin evolution on
RT differentiating sex chromosomes in Drosophila.";
RL Submitted (AUG-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}.
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DR EMBL; CP012523; ALC39610.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M4ED06; -.
DR SMR; A0A0M4ED06; -.
DR STRING; 30019.A0A0M4ED06; -.
DR OMA; KPSKMFE; -.
DR Proteomes; UP000494163; Chromosome 2l 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 Reference proteome {ECO:0000313|Proteomes:UP000494163};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Zinc {ECO:0000256|RuleBase:RU361144}.
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ALC39610.1"
FT NON_TER 599
FT /evidence="ECO:0000313|EMBL:ALC39610.1"
SQ SEQUENCE 599 AA; 69464 MW; FD28AB5CB88C73DD CRC64;
LSQALVKEEI AAKEYLENLN KELALRTNVD TEAAWAYASN INDENEKKRN ENAAELAKFL
KEIAADTQKF NWRSYQSEDI KRQFKFLTKL GYAALSESDY KELLETLSSM ESNYAKVKVC
DFKDAKKCDL ALEPEIEEII TKSRNPEELK YYWREFYDKA GTAVRPQFEK YIELNTKAAH
LNNFTSGAEV WLDEYEDPTF EKQLEAIFAE IRPLYEQVHG YVRYRLRQHY GNEVVSEKGP
LPMHLLGNMW AQQWSDIADI VSPFPDKPLV DVSAEMIKQG YNPLKMFQMG DDFFTSMNLT
KLPKDFWDKS IIEKPTDGRD LICHASAWDF YLQDDVRIKQ CTTVTQSQFF TVHHELGHIQ
YFLQYQHLPF VYRTGANPGF HEAVGDVLSL SVSTPKHLEK VGLLKNYKQD EEQRINNLFL
TALDKIVFLP FAFTMDKYRW SLFRGEVDKS KWNCAFWKLR EEYSGIEPPV VRTEKDFDAP
AKYHVSADVE YLRYLVSFII QFQFYKSACI KAGQYDPKNP ELPLDNCDIY GSAAAGKAFQ
NMLSMGASKP WPDALQAFNG ERTMTGKAIA EYFEPLRVWL EAENKKNKVP IGWTASDSK
//
