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
//