ID A0A093HJH8_STRCA Unreviewed; 1201 AA.
AC A0A093HJH8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Angiotensin-converting enzyme {ECO:0000256|RuleBase:RU361144};
DE EC=3.4.-.- {ECO:0000256|RuleBase:RU361144};
DE Flags: Fragment;
GN ORFNames=N308_05057 {ECO:0000313|EMBL:KFV81851.1};
OS Struthio camelus australis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Struthioniformes; Struthionidae;
OC Struthio.
OX NCBI_TaxID=441894 {ECO:0000313|EMBL:KFV81851.1, ECO:0000313|Proteomes:UP000053584};
RN [1] {ECO:0000313|EMBL:KFV81851.1, ECO:0000313|Proteomes:UP000053584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N308 {ECO:0000313|EMBL:KFV81851.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-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; KL206368; KFV81851.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093HJH8; -.
DR STRING; 441894.ENSSCUP00000012757; -.
DR MEROPS; M02.004; -.
DR BRENDA; 3.4.15.1; 16960.
DR Proteomes; UP000053584; 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 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:UP000053584};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|RuleBase:RU361144}.
FT TRANSMEM 1161..1185
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFV81851.1"
FT NON_TER 1201
FT /evidence="ECO:0000313|EMBL:KFV81851.1"
SQ SEQUENCE 1201 AA; 139093 MW; 0E2C067594E1DE99 CRC64;
QVEASLVEQN FTEAWGKKAK ELYSNIWSNF SNSQLRKIIG SIQTLGPSNL PLEKREQYNT
ILSDMDKIYS TAKVCQANGT CWELEPDISE IMANSRSYKK LLYAWEGWHN AAGNPLRAMY
QEFVKLSNEA YQMDGFKDTG EYWRSWYDSL TFEDDLEQLY NQLEPLYLNL HAFVRRKLYN
HYGPKYINLK GPIPAHLLGN MWAQQWNNIY DMMIPYPEKP NLDVTNTMVQ QGWNATHMFR
VSEEFFTSLG LLEMPPEFWE KSMLEKPKDG REVVCHASAW DFYNRKDFRI KQCTTVTMEQ
LFTVHHEMGH VQYYLQYKDQ PVSFRSGANP GFHEAIGDVM SLSVSTPSHL KKIGLLSSIT
EDTESSINYL LKMALEKIAF LPFGYLIDQW RWNVFNGRTP PSRYNYDWWY LRTKYQGICS
PVLRNESNFD PGAKYHIPGN TPYIRYFVSF ILQFQFHKAL CQAANHTGPL HTCDIYMSKE
AGAKLRWGQR KVGTLTMDKM DAGALLEYFS PVTEWLQQQN NKTNEVLGWP EFDWRPPIPE
GYPEGIDKIA DEVQAKEFLS EYNRTAEEVW NAYTEASWAY NTNITDHNKD IMLEKNLAMS
KHTLQYGMRA REFDSTDFQD QSVTRILKKL SAIERAALPE DELKEYNTLL SDMETTYSIA
KVCRDNKICH PLDPDLTDIL ASSRDYDELL FAWKGWRDAS GKVIRNKYKR YVTLSNKAAV
LNGYTDNGAF WRSLYETPTF EEDVERLYLQ LQPLYLNLHA YVRRALYKKY GPERVNLKGP
IPAHLLGNMW AQSWSNIFDL VIPFPDATKV DATPAMKKQG WTPRRMFEES DRFFTSLGLI
PMPQEFWDKS MIEKPTDGRE VVCHASAWDF YNRKDFRIKQ CTVVNMDDLI TVHHEMGHVQ
YFLQYMDQPI SFRDGANPGF HEAVGDVMAL SVSTPKHLYS INLLDEVTDN EESNINYLMS
IALDKIAFLP FGYLMDQWRW KVFDGRIKED EYNQQWWNLR LKYQGLCPPV PRSEDDFDPG
AKFHIPANVP YIRYFVSFVI QFQFHQALCK AAGHTGPLHT CDIYQSKAAG SLLGEALKLG
FSKPWPEAME LITGQPNMSA DALMSYFEPL MTWLAKENEK NGDILGWAEY DWTPYAATQA
QGSPDQADFL GMSLASSQAT AGGWVLLALA LIFVVTTIIL GVKLFSFRRK AFKSSSEMEL
K
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