ID A0A068S367_9FUNG Unreviewed; 878 AA.
AC A0A068S367;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Peptidase s8 and s53 subtilisin kexin sedolisin {ECO:0000313|EMBL:CDH56430.1};
GN ORFNames=LCOR_07480.1 {ECO:0000313|EMBL:CDH56430.1};
OS Lichtheimia corymbifera JMRC:FSU:9682.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Lichtheimiaceae; Lichtheimia.
OX NCBI_TaxID=1263082 {ECO:0000313|EMBL:CDH56430.1, ECO:0000313|Proteomes:UP000027586};
RN [1] {ECO:0000313|EMBL:CDH56430.1, ECO:0000313|Proteomes:UP000027586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JMRC:FSU:9682 {ECO:0000313|Proteomes:UP000027586};
RA Schwartze V.U., Winter S., Shelest E., Marcet-Houben M., Horn F.,
RA Wehner S., Hoffmann K., Riege K., Sammeth M., Nowrousian M., Valiante V.,
RA Linde J., Jacobsen I.D., Marz M., Brakhage A.A., Gabaldon T., Bocker S.,
RA Voigt K.;
RT "Gene expansion shapes genome architecture in the human pathogen
RT Lichtheimia corymbifera: an evolutionary genomics analysis in the ancient
RT terrestrial Mucorales (Mucoromycotina).";
RL Submitted (AUG-2013) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CDH56430.1}.
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DR EMBL; CBTN010000037; CDH56430.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A068S367; -.
DR STRING; 1263082.A0A068S367; -.
DR VEuPathDB; FungiDB:LCOR_07480.1; -.
DR OrthoDB; 662485at2759; -.
DR Proteomes; UP000027586; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04818; PA_subtilisin_1; 1.
DR CDD; cd07489; Peptidases_S8_5; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR010435; Fn3_5.
DR InterPro; IPR046450; PA_dom_sf.
DR InterPro; IPR003137; PA_domain.
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; IPR034187; Peptidases_S8_5.
DR PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF06280; fn3_5; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52025; PA domain; 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 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:UP000027586};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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..878
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001655458"
FT DOMAIN 137..539
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 343..430
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 577..696
FT /note="Fn3-like"
FT /evidence="ECO:0000259|Pfam:PF06280"
FT ACT_SITE 146
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 195
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 502
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 878 AA; 94842 MW; 0EA134F971CED0D6 CRC64;
MVWLLIFSLL ACTAAVVFAN DSQQQRLFLP NTYVVEFQQP QHDDGLFQRL AEHKIEHHLR
HRYDMMNAIS LSFNTSNDAT RFFNLMRQDI HRTWPVNAVA RPNAKLLHVG KKPATGLFNY
YNNTGVTQLR EELGLTGRNI KVGIIDSGLD YTHPSLGGCF GSQCRVAFGY DFVGDDYTGD
NQPIPDGDPM DCNGHGTHVA GIIGADDKEF QFTGVAPEVT FGAYRIFGCS GSSADDVIMK
AMEQAYFDGM DVINLSLGDL GWAESSTSVL ADVLTLKGMM VVAAAGNEGD KGMFQVGAPS
LGRHALSVAS TDNSVTLAHP IKYNDFQVGY STSSGKPLSV SEGEIVPVSD TFNAPNDACE
PVHSNHLLGK IALIARGGCY FSEKVQNVQA AGAIAAIVYN NNPGLVNPSI NDPTIRIQCG
GISNEQGESL FNMTMANPGV QFELPNEDVQ FEIPTAGTIS SYSSWGLGPD LGVKPDIAAP
GGEIYSTYLI KEGGYATLSG TSMASPHVAG IVALLQQAKG GGRSLHPEEL RATLINTGDP
LSRYQSQAFE SVARQGSGLI NVYKSIHAST RVTPEQIALR DLSRQAPNNE YTFTIHNNGR
MAGDYKITHL PATTVQGYSN GDDMAPLQQP IQLDDPGTQA IVESIYPNEL NIPANEAANV
TVRLRAPADT KAPSVYSGYF KIAKDNDEDN TLFLPYAGLS VELGSLPVLY VNRSMPMVML
DTAGVSSRSP ALIQLQLIHP SPLLLVTAVD AKNTSQSFGI IPGGYWAFLG RNNVHDINDS
ILMAWAGDIA TSPEQAMAEQ STAAAAGLAV MQPKLFRSTK NVDHQLHMAS VQEDSSNNSK
PLPPGTYKLK VMALHAFGDY ENDADYDIWY SDEMYIRN
//
