ID A0A1R1PJD3_ZANCU Unreviewed; 504 AA.
AC A0A1R1PJD3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Subtilase-type proteinase psp3 {ECO:0000313|EMBL:OMH81066.1};
GN ORFNames=AX774_g5480 {ECO:0000313|EMBL:OMH81066.1};
OS Zancudomyces culisetae (Gut fungus) (Smittium culisetae).
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Harpellomycetes; Harpellales; Legeriomycetaceae; Zancudomyces.
OX NCBI_TaxID=1213189 {ECO:0000313|EMBL:OMH81066.1, ECO:0000313|Proteomes:UP000188320};
RN [1] {ECO:0000313|Proteomes:UP000188320}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COL-18-3 {ECO:0000313|Proteomes:UP000188320};
RA Wang Y., White M., Kvist S., Moncalvo J.-M.;
RL Submitted (JAN-2017) 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:OMH81066.1}.
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DR EMBL; LSSK01000993; OMH81066.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R1PJD3; -.
DR Proteomes; UP000188320; Unassembled WGS sequence.
DR GO; GO:0110165; C:cellular anatomical entity; IEA:UniProt.
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; 3.40.50.200; 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 PANTHER; PTHR43806:SF11; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
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:UP000188320};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 238..481
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 245
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 278
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 437
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 504 AA; 55057 MW; D88C341D26373A47 CRC64;
MVQPRLAERK VVSKVMDRLD NSTLQQNRAY NIGFSVNEGT GNEEYFDMLK FLISEFSLNN
DTDVSNLKYE EIFVSGNTGN QALQTSKIIS VVLSEVQATK LRSLTFPYIS IVEPDIKVQV
YWGETPSNDD DKLIVAHNTP SSDRKEDFLN IFTNLWDSNR QSSKSVSSDS ENEDLDVSIV
ANDTPVSTLG FSSSPDNWAH ERLPPWNLCR ISKEKFDNPL EYIPYGGTYS YPITEPSKVL
VFVIDSGVNK THSELQDRVI YEESLVATEP ETEDFFGHGT FVSSIITGKM AGVAKNVQLG
SIKVIDRDGL ADVKTIISAF NRVVQLKNST FKDYSILVNL SINADGVSNT LLSAIASANE
QGILTVISAG NNSDDACSYS PSGEPSSITV GAIGFPNDAF FSYSNYGKCV DILAPGQSVL
GASDETISVL SFQSGTSMAA PMVTGVCAQV WQNNPSLSPA EVRKRVLDSA LRGLITDLDE
NTPNLLLWNG YSGPTLLPEM ITDS
//