ID A0A2T9YD43_9FUNG Unreviewed; 331 AA.
AC A0A2T9YD43;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Peptidase S1 domain-containing protein {ECO:0000259|PROSITE:PS50240};
GN ORFNames=BB560_006218 {ECO:0000313|EMBL:PVU90260.1};
OS Smittium megazygosporum.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Harpellomycetes; Harpellales; Legeriomycetaceae; Smittium.
OX NCBI_TaxID=133381 {ECO:0000313|EMBL:PVU90260.1, ECO:0000313|Proteomes:UP000245609};
RN [1] {ECO:0000313|EMBL:PVU90260.1, ECO:0000313|Proteomes:UP000245609}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC-DP-2 {ECO:0000313|EMBL:PVU90260.1,
RC ECO:0000313|Proteomes:UP000245609};
RX PubMed=29764946;
RA Wang Y., Stata M., Wang W., Stajich J.E., White M.M., Moncalvo J.M.;
RT "Comparative Genomics Reveals the Core Gene Toolbox for the Fungus-Insect
RT Symbiosis.";
RL MBio 9:e00636-e00618(2018).
CC -!- SIMILARITY: Belongs to the peptidase S1 family.
CC {ECO:0000256|ARBA:ARBA00007664}.
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:PVU90260.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MBFS01002974; PVU90260.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T9YD43; -.
DR STRING; 133381.A0A2T9YD43; -.
DR Proteomes; UP000245609; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR PANTHER; PTHR24276:SF100; AT20289P-RELATED; 1.
DR PANTHER; PTHR24276; POLYSERASE-RELATED; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000245609};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 48..300
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
SQ SEQUENCE 331 AA; 36506 MW; D2BE82D2E325F543 CRC64;
MRDIKIFKLS AAFVVGICVI ANLVALLITI KNYTPLENKN VSSESARIIG GVSSKSNEFP
FAAVVKISHE KFIYTCGSTI LSDKFLVTAA HCVYIQSQKI RPNNTRIGLG SRNIKEVKVL
EPLRFHVHPK YIADKNVTIF TFSCVQKKKL KESLTFGPGL QTAKIDLRKI EENTEVTALG
WGITSNESTL PSQELMETSL FIQKPQECSK VRPNFTSNNL DYICAANGVQ GKDTCYGDSG
APIIRTQKPL NAYSVLGLTS YGDIIGNVDM LKKPKCADPK GFGFYTHIGY YIYFISNVTG
IPFETLALDS AAENSQIITE FDTETKADVL S
//
