ID A0A132ABF3_SARSC Unreviewed; 655 AA.
AC A0A132ABF3;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Angiotensin-converting enzyme {ECO:0000256|RuleBase:RU361144};
DE EC=3.4.-.- {ECO:0000256|RuleBase:RU361144};
GN ORFNames=QR98_0068370 {ECO:0000313|EMBL:KPM08321.1};
OS Sarcoptes scabiei (Itch mite) (Acarus scabiei).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Sarcoptiformes; Astigmata; Psoroptidia; Sarcoptoidea;
OC Sarcoptidae; Sarcoptinae; Sarcoptes.
OX NCBI_TaxID=52283 {ECO:0000313|EMBL:KPM08321.1, ECO:0000313|Proteomes:UP000616769};
RN [1] {ECO:0000313|EMBL:KPM08321.1, ECO:0000313|Proteomes:UP000616769}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Arlian Lab {ECO:0000313|EMBL:KPM08321.1};
RX PubMed=26555130; DOI=10.1186/s13071-015-1198-2;
RA Rider S.D.Jr., Morgan M.S., Arlian L.G.;
RT "Draft genome of the scabies mite.";
RL Parasit. Vectors 8:585-585(2015).
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:KPM08321.1}.
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DR EMBL; JXLN01012321; KPM08321.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A132ABF3; -.
DR VEuPathDB; VectorBase:SSCA002861; -.
DR OMA; FERNDFR; -.
DR OrthoDB; 3088988at2759; -.
DR Proteomes; UP000616769; 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}.
SQ SEQUENCE 655 AA; 78209 MW; 308C0F731AADF4D3 CRC64;
MKRQFRYKYF LLGLILLITF FVYIECQSLD DYNEFLEEQN LFLLRERNRI TKAQWSHDSN
ITNFNEINLI EKANAFDEFR KKQAKLVEEY RRTNVTEPLP ESLRRQFDKL GFLGVSVLDE
IDREQWQASL LRMEKIYSSS KIKLDEDEDS NEINDDYRDG LPLQPDLTQI MATSTDEPLL
RKIWQKFRDA TGKRIRDDYL KYIDLGNKAA QKLDKGFESY DDIWVSDWNM ENFREEMERL
INEVMPLYRK IHAYVRFHLN RTYPGVIPKD GTIPAHLLGN MWAQHWSNLL QLIPEMQFFP
DVPSIDGAVN EKLQKNKQII FSYATEFDCE RNVPIIRRIF SQSWNEKYDS NLLESIHFGT
SHRNRNDMVG DDSHASAWDF FERNDFRIKQ CTVKTLEHLL VIHHEMGHIQ YYMNYAGQPT
VFREGANRGF HEAIGDLMAL SVVTPQHLSR IGLLDRKHLE KNLDELNLNY QLRMALDKIV
FLPFSFLVDK WRWDVFRDEH LARHLNQHWW ELRLKYQGIS PPLKRSEYDF DAGAKYHVAA
NVEYMQYFFA HILQFQFYQH LCSYVDGIEK LYECDFYRNK QAGSDLIQML RKGSSEPWQK
ILNDFIGTDK LSLGAIFEYF EPLNRTLSEF IEKNSIEIGW DVESKFNIYI NRFCF
//
