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Database: UniProt
Entry: A0A093JQ16_STRCA
LinkDB: A0A093JQ16_STRCA
Original site: A0A093JQ16_STRCA 
ID   A0A093JQ16_STRCA        Unreviewed;       544 AA.
AC   A0A093JQ16;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Neuroendocrine convertase 2 {ECO:0000313|EMBL:KFV80769.1};
DE   Flags: Fragment;
GN   ORFNames=N308_11881 {ECO:0000313|EMBL:KFV80769.1};
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:KFV80769.1, ECO:0000313|Proteomes:UP000053584};
RN   [1] {ECO:0000313|EMBL:KFV80769.1, ECO:0000313|Proteomes:UP000053584}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N308 {ECO:0000313|EMBL:KFV80769.1};
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, ECO:0000256|RuleBase:RU003355}.
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DR   EMBL; KL206273; KFV80769.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093JQ16; -.
DR   STRING; 441894.ENSSCUP00000015099; -.
DR   MEROPS; S08.073; -.
DR   Proteomes; UP000053584; Unassembled WGS sequence.
DR   GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016486; P:peptide hormone processing; IEA:UniProt.
DR   CDD; cd04059; Peptidases_S8_Protein_convertases_Kexins_Furin-like; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 3.40.50.200; 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; IPR023827; Peptidase_S8_Asp-AS.
DR   InterPro; IPR022398; Peptidase_S8_His-AS.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   PANTHER; PTHR42884:SF13; NEUROENDOCRINE CONVERTASE 2; 1.
DR   PANTHER; PTHR42884; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN-RELATED; 1.
DR   Pfam; PF01483; P_proprotein; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51829; P_HOMO_B; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00136; SUBTILASE_ASP; 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};
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}.
FT   DOMAIN          368..504
FT                   /note="P/Homo B"
FT                   /evidence="ECO:0000259|PROSITE:PS51829"
FT   ACT_SITE        74
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        115
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        291
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFV80769.1"
FT   NON_TER         544
FT                   /evidence="ECO:0000313|EMBL:KFV80769.1"
SQ   SEQUENCE   544 AA;  59915 MW;  8EAA33E1DEB19AF2 CRC64;
     QVKKAVQQEG FSRRKRGYRD INDIDINMND PLFTKQWYLI NTGQADGTPG LDLNVAEAWE
     LGYTGKGVTI GIMDDGIDYL HPDLASNYNA KASYDFSSND PYPYPRYTDD WFNSHGTRCA
     GEVSAAANNN ICGVGVAYNS KVAGIRMLDQ PFMTDIIEAS SISHMPQVID IYSASWGPTD
     NGKTVDGPRE LTLQAMADGV NKGRGGKGSI YVWASGDGGS YDDCNCDGYA SSMWTISINS
     AINDGRTALY DESCSSTLAS TFSNGRKRNP EAGVATTDLY GNCTLRHSGT SAAAPEAAGV
     FALALEANLD LTWRDMQHLT VLTSKRNQLH DEVHQWRRNG VGLEFNHLFG YGVLDAGAMV
     KMAKDWKTVP ERFHCVGGSI QEPEKIPSSG KLVLTLTTDA CEGKENFVRY LEHVQAVITV
     NSTRRGDLNI NMTSPMGTKS ILLSRRPRDD DSKVGFDKWP FMTTHTWGED PRGTWALEIG
     FVGGVPQRGV LKEWTLMLHG TQSAPYIDQI VKDYQSKLAM SKKEELEEEL DEAVERSLKS
     ILSK
//
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