ID A0A093PV00_9PASS Unreviewed; 1287 AA.
AC A0A093PV00;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Angiotensin-converting enzyme {ECO:0000256|RuleBase:RU361144};
DE EC=3.4.-.- {ECO:0000256|RuleBase:RU361144};
DE Flags: Fragment;
GN ORFNames=N305_08246 {ECO:0000313|EMBL:KFW80608.1};
OS Manacus vitellinus (golden-collared manakin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Pipridae; Manacus.
OX NCBI_TaxID=328815 {ECO:0000313|EMBL:KFW80608.1, ECO:0000313|Proteomes:UP000053258};
RN [1] {ECO:0000313|EMBL:KFW80608.1, ECO:0000313|Proteomes:UP000053258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N305 {ECO:0000313|EMBL:KFW80608.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-2014) 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 2 Zn(2+) ions per subunit. {ECO:0000256|RuleBase:RU361144};
CC -!- COFACTOR:
CC Name=chloride; Xref=ChEBI:CHEBI:17996;
CC Evidence={ECO:0000256|ARBA:ARBA00001923};
CC -!- SIMILARITY: Belongs to the peptidase M2 family.
CC {ECO:0000256|ARBA:ARBA00008139, ECO:0000256|RuleBase:RU361144}.
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DR EMBL; KL670913; KFW80608.1; -; Genomic_DNA.
DR STRING; 328815.ENSMVIP00005027337; -.
DR MEROPS; M02.001; -.
DR Proteomes; UP000053258; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 2.
DR Gene3D; 1.10.1370.30; -; 1.
DR Gene3D; 1.10.1370.20; Oligoendopeptidase f, C-terminal domain; 1.
DR InterPro; IPR042088; OligoPept_F_C.
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; 2.
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 Membrane {ECO:0000256|SAM:Phobius};
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:UP000053258};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|RuleBase:RU361144}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..1287
FT /note="Angiotensin-converting enzyme"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001886881"
FT TRANSMEM 1247..1271
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFW80608.1"
FT NON_TER 1287
FT /evidence="ECO:0000313|EMBL:KFW80608.1"
SQ SEQUENCE 1287 AA; 147926 MW; A5A9B7D609DEB1C8 CRC64;
SRSAPAAMPP ALGLLLGLSL AGALRAQFEP PQHPGTEEGA ALFASDYNST AELVLFESVS
ASWNYNTNLT AENAALQVQA SLEEQNFTEL WGKRAKELYG NIWSNFTDPQ LRKIIGSIQT
LGPSNLPLDK REQYNTILSD MDKIYSTAKV CLPNGTCWDL EPDLSDIMAM SRSYKKLLYA
WEGWHNTAGN PLRPKYEEFV QLSNEAYSAD GFEDTGSYWR SWYDSDTFED DLESIYNQLE
PLYLNLHAFV RRKLYDYYGP KYVNLRGPIP AHLLGNMWAQ QWNNIYDLMV PYPEKPNLDV
TSAMVQQGWN ATHMFRVSEE FFTSLGLLEM PPEFWEKSML EKPTDGREVV CHASAWDFYN
RKDFRIKQCT SVTMEQLFTV HHEMGHIQYY LQYKDQPVSF RSGANPGFHE AIGDVLSLSV
STPSHLHTIG LLSNATEDEE SNINYLLKMA LEKIAFLPFG YLIDQWRWNV FSGRTPPSRY
NSDWWYLRTK YQGICAPVTR NESNFDPGAK YHIPGNTPYI RYFVSFILQF QFHKALCEAA
GHSGPLHTCD IYRSREAGDK LREVLKAGSS KSWQEVLFNF TGTDKMDAGP LLEYFSPVTT
WLQEQNNKTN EVLGWPDFEW RPPIPEGYPE GIDKITDEAQ AKEFLAEYNS TAEEVWNAYT
EASWAYNTNI TDHNREVMLE KNLAMSKHTL DYGMRARQFD TSDFQDESVT RILKKLSVIE
RAALPEDELM EYNTLLSDME TTYSLAKVCR DDKTCLPLDP DLTDIMATSR DYDELLFAWK
GWRDASGKKM RNDYKRYVEL SNKAAVLNGY TDNGAYWRSL YETSTFEEDL ERLYQQLQPL
YLNLHAYVRR ALYKKYGAEH INLRGPIPAH LLGNMWAQSW SNIFDLVMPF PNATKVDATP
AMKEQGWTAK KMFEESDRFF TSLGLIPMPE EFWNKSMIEK PSDGREVVCH ASAWDFYNRK
DFRIKQCTVV NMDDLITVHH EMGHVQYFLQ YKDQPVSFRD GANPGFHEAV GDVMALSVST
PKHLHSINLL DEVKEDQESD INYLMSIALD KIAFLPFGYL MDQWRWKVFD GRIKDDEYNK
EWWNLRTKYQ GLCPPAPRSE DDFDPGAKFH IPANVPYIRY FVSFVIQFQF HQALCNAAGH
TGALHTCDIY QSTEAGKILG DALKLGFSKP WPEAMQLITG QPNMSAEALM SYFEPLMTWL
EKENEKNGEV LGWPEYSWTP DSATLPPDGS SKTDFLGMSL TKSQASVGAW VLLALALVFL
ITTIFFSVKF FSSRRKAFKS SSEMELK
//
