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Database: UniProt
Entry: C3ZG84_BRAFL
LinkDB: C3ZG84_BRAFL
Original site: C3ZG84_BRAFL 
ID   C3ZG84_BRAFL            Unreviewed;       405 AA.
AC   C3ZG84;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 96.
DE   SubName: Full=Subtilisin-like serine protease Rho m 2.0101 {ECO:0000313|RefSeq:XP_035671522.1};
GN   Name=LOC118412637 {ECO:0000313|RefSeq:XP_035671522.1};
GN   ORFNames=BRAFLDRAFT_118415 {ECO:0000313|EMBL:EEN48405.1};
OS   Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC   Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC   Branchiostomatidae; Branchiostoma.
OX   NCBI_TaxID=7739;
RN   [1] {ECO:0000313|EMBL:EEN48405.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN48405.1};
RC   TISSUE=Testes {ECO:0000313|EMBL:EEN48405.1};
RX   PubMed=18563158; DOI=10.1038/nature06967;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA   Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA   Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA   Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA   Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA   Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA   Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA   Satoh N., Rokhsar D.S.;
RT   "The amphioxus genome and the evolution of the chordate karyotype.";
RL   Nature 453:1064-1071(2008).
RN   [2] {ECO:0000313|RefSeq:XP_035671522.1}
RP   IDENTIFICATION.
RC   STRAIN=S238N-H82 {ECO:0000313|RefSeq:XP_035671522.1};
RC   TISSUE=Testes {ECO:0000313|RefSeq:XP_035671522.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family.
CC       {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240,
CC       ECO:0000256|RuleBase:RU003355}.
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DR   EMBL; GG666617; EEN48405.1; -; Genomic_DNA.
DR   RefSeq; XP_002592394.1; XM_002592348.1.
DR   RefSeq; XP_035671522.1; XM_035815629.1.
DR   KEGG; bfo:118412637; -.
DR   eggNOG; KOG1153; Eukaryota.
DR   InParanoid; C3ZG84; -.
DR   OMA; DNPPSWG; -.
DR   OrthoDB; 5390427at2759; -.
DR   Proteomes; UP000001554; Chromosome 3.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd04077; Peptidases_S8_PCSK9_ProteinaseK_like; 1.
DR   Gene3D; 3.30.70.80; Peptidase S8 propeptide/proteinase inhibitor I9; 1.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   InterPro; IPR034193; PCSK9_ProteinaseK-like.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   InterPro; IPR010259; S8pro/Inhibitor_I9.
DR   InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR   PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR   PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR   Pfam; PF05922; Inhibitor_I9; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00136; SUBTILASE_ASP; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   3: Inferred from homology;
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:UP000001554};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..405
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5041116472"
FT   DOMAIN          36..109
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000259|Pfam:PF05922"
FT   DOMAIN          152..380
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   ACT_SITE        154
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        187
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        342
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   405 AA;  43406 MW;  25F6060D26979E59 CRC64;
     MKSLRVLAVL AAVLGVAMAT APMLRLDSKT AIPNEYIVVL QKNLTNYAVG KHMNSVKTLL
     TGTNDTKILF EHNFRWFKAY SIRTNQKMIR HLAEQPEVRY IEANQVVKAY QAQCQDQLEA
     TWGLVRTVER DLLLDGIYHY QGGDGEGVDA YIIDTGIYTE HSEFGGRAKW GVDTVDTPSP
     ETDENGHGTH VAGTVMSDAW GLAKKATAIA VKVLSRSGSG STAGVIEGVE WTGQQHSGNN
     KKSVANMSLG GGRSDAMNEA VKAVVEAGVV MVVAAGNEGW EACNVSPASE PTAITVGCSD
     NEDDFCFFSN YGTCMDIIAP GQDVTSAWIG GQFADNTISG TSMSAPHIAG IVAKYMSRQS
     SVPSPEEVKD FLQTTSTKDK INQIPSNSDT LNYLGFMDCG GGPDV
//
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