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Database: UniProt
Entry: A0A093H8E1_STRCA
LinkDB: A0A093H8E1_STRCA
Original site: A0A093H8E1_STRCA 
ID   A0A093H8E1_STRCA        Unreviewed;       745 AA.
AC   A0A093H8E1;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   08-NOV-2023, entry version 30.
DE   SubName: Full=Proprotein convertase subtilisin/kexin type 7 {ECO:0000313|EMBL:KFV78843.1};
DE   Flags: Fragment;
GN   ORFNames=N308_03406 {ECO:0000313|EMBL:KFV78843.1};
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:KFV78843.1, ECO:0000313|Proteomes:UP000053584};
RN   [1] {ECO:0000313|EMBL:KFV78843.1, ECO:0000313|Proteomes:UP000053584}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N308 {ECO:0000313|EMBL:KFV78843.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC       ProRule:PRU01240}.
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DR   EMBL; KL206088; KFV78843.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093H8E1; -.
DR   STRING; 441894.ENSSCUP00000014284; -.
DR   Proteomes; UP000053584; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd04059; Peptidases_S8_Protein_convertases_Kexins_Furin-like; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 3.30.70.850; Peptidase S8, pro-domain; 1.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR034182; Kexin/furin.
DR   InterPro; IPR002884; P_dom.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR022398; Peptidase_S8_His-AS.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   InterPro; IPR032815; S8_pro-domain.
DR   InterPro; IPR038466; S8_pro-domain_sf.
DR   PANTHER; PTHR42884:SF28; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN TYPE 7; 1.
DR   PANTHER; PTHR42884; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN-RELATED; 1.
DR   Pfam; PF01483; P_proprotein; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   Pfam; PF16470; S8_pro-domain; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51829; P_HOMO_B; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00137; SUBTILASE_HIS; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   3: Inferred from homology;
KW   Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Membrane {ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000053584};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        670..689
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          486..623
FT                   /note="P/Homo B"
FT                   /evidence="ECO:0000259|PROSITE:PS51829"
FT   REGION          199..233
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        192
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        233
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        411
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   NON_TER         745
FT                   /evidence="ECO:0000313|EMBL:KFV78843.1"
SQ   SEQUENCE   745 AA;  82873 MW;  6C3B847A2D084CFE CRC64;
     MPHWRWRVPL WSAAMEATLC IHTCLWLSAA WIPLILPHGL ARATELAAGT DSRGTAHRHG
     KLAWAVNLDV PEEELEQRAE ELARTAGLVN MGRIGELKGH YLFTYQPDGH PAPEPEAIRR
     SVEALFAQHD SVRWHSEQKL LKRSKRSLHF NDPKYPQQWH LNNRKSPGKD INVTGVWERN
     VTGHGVTVVV VDDGVEHTIK DIQPNYSPEG SYDLNSNDPD PMPHPDEENG NHHGTRCAGE
     IAAVPNNSFC TVGVAYGSRI AGIRVLDGPL TDSMEAIAFN KHYQINDIYS CSWGPDDDGK
     TVDGPHQLGK AALQHGVIAG RRGFGSIFVV ASGNGGQHSD NCNYDGYANS IYTVTIGAVD
     ETGSMPFYAE ECASMLAVTF SGGDKMMRSI VTTDWDLQKG TGCTEGHTGT SAAAPLAAGM
     IALMLQVRPC LTWRDVQHII VFTATKYQDR HAKWDINQAG FSHSHQHGFG LLNAWRLVNA
     AKIWESVPYL ASYISPVLKE GKSIPLLPQE LEVTWNVTTT DLELSGMRTL EHVAVTVTIT
     HPRRGNLEIR LFCPSGMMSL IGTTRSMDSD PNGFADWTFS TVRCWGEEAQ GTYRLVIRDT
     RDESLRAGTL REWQLTLYGS SWSPAEMKER QRLLEEAMSG QYLNSNFSLP CPPGLEIPEE
     QRYTITANTL KTLLLLGCFA VFWTFYYMLE VCLTRNHMGL DLTCHGSTAC KWYQQGGKHR
     ALENGLEMES VPLYGEKDAE DIEIE
//
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