ID   A0A0K3CL16_RHOTO        Unreviewed;       672 AA.
AC   A0A0K3CL16;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=Peptidase S8/S53 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   Name=FGENESH: predicted gene_9.357 {ECO:0000313|EMBL:CTR09150.1};
GN   ORFNames=BN2166_0050110 {ECO:0000313|EMBL:CTR09150.1};
OS   Rhodotorula toruloides (Yeast) (Rhodosporidium toruloides).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX   NCBI_TaxID=5286 {ECO:0000313|EMBL:CTR09150.1, ECO:0000313|Proteomes:UP000199069};
RN   [1] {ECO:0000313|EMBL:CTR09150.1, ECO:0000313|Proteomes:UP000199069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Single colony {ECO:0000313|EMBL:CTR09150.1};
RA   Cajimat M.N.B., Milazzo M.L., Fulhorst C.F.;
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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; CWKI01000009; CTR09150.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0K3CL16; -.
DR   STRING; 5286.A0A0K3CL16; -.
DR   OMA; IWNSGNR; -.
DR   Proteomes; UP000199069; Unassembled WGS sequence.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
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; IPR022398; Peptidase_S8_His-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; PS00137; SUBTILASE_HIS; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
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:UP000199069};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}.
FT   DOMAIN          133..230
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000259|Pfam:PF05922"
FT   DOMAIN          320..559
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          632..670
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        18..37
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        322
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        353
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        519
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   672 AA;  71647 MW;  62108C82CC802E25 CRC64;
     MRVEEGRVRC GSADGLLRAS EGDEKSEPGE MGVKQEERVG SRVVVEWFEW SSREEVEDEE
     EEQVEECPAL SEVVRMFVPH ALAAALCTAL AAHALPAASS SDLAPLLTPT LLAIPHEQHE
     HTTPTLAHIV EDSYIVVLDD SLTDHDIHQH HAHVDAVHSH TEHALAQASS AHNRRHGVKH
     RFHVGGKRHS HARSRSARKL KGYSGSFDER TVDQIRAMKG VKYVERDSLV WASDIEKGAP
     WVRSTAHSLT RAGDLPPRPD SARPMVSAKV GRMTGTHADS SLLRNGQGLA RISHRNTLSL
     GNFNRYEYDS QAGEGVDAYV IDTGVNIDHV ELEGRAKWGK TIPNDPDQDL NGHGSHVAGT
     IASAKYGVAK KANIVAVKVL GAGGSGTMSD VVAGVAWAAD SAAEQANLKA QGKNKKHKGS
     VANMSLGGGK SQALDDAVNA AVEDGLHFAV AAGNDNRDAC SYSPAAAEGA ITVGASTISD
     ERAYFSNHGK CVDIFAPGLN ILSIWNSGNR SVNTISGTSM ASPHIAGLAA YMLGSDWAAS
     AALDEALSSS SSQGSFASSL NQFAFGGLKG KPEDHLLSPK ALKKAMLKVA TKGALHDLNP
     GSPNLLSFNN YTAPSSTPPK RGKWRTDSSV ESSLVEAYLE DLKDELDALK SELKDEIEEV
     SGLVRELVEE AF
//