ID H0EH45_GLAL7 Unreviewed; 650 AA.
AC H0EH45;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Putative protease KEX1 {ECO:0000313|EMBL:EHL02186.1};
GN ORFNames=M7I_1780 {ECO:0000313|EMBL:EHL02186.1};
OS Glarea lozoyensis (strain ATCC 74030 / MF5533).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Helotiaceae; Glarea.
OX NCBI_TaxID=1104152 {ECO:0000313|EMBL:EHL02186.1, ECO:0000313|Proteomes:UP000005446};
RN [1] {ECO:0000313|EMBL:EHL02186.1, ECO:0000313|Proteomes:UP000005446}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 74030 / MF5533 {ECO:0000313|Proteomes:UP000005446};
RX PubMed=22302591; DOI=10.1128/EC.05302-11;
RA Youssar L., Gruening B.A., Erxleben A., Guenther S., Huettel W.;
RT "Genome sequence of the fungus Glarea lozoyensis: the first genome sequence
RT of a species from the Helotiaceae family.";
RL Eukaryot. Cell 11:250-250(2012).
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01240}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01240}.
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:EHL02186.1}.
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DR EMBL; AGUE01000032; EHL02186.1; -; Genomic_DNA.
DR AlphaFoldDB; H0EH45; -.
DR HOGENOM; CLU_002976_2_1_1; -.
DR InParanoid; H0EH45; -.
DR Proteomes; UP000005446; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProt.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
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:UniProtKB-KW.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 2.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR002884; P_dom.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR PANTHER; PTHR42884:SF14; NEUROENDOCRINE CONVERTASE 1; 1.
DR PANTHER; PTHR42884; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN-RELATED; 1.
DR Pfam; PF01483; P_proprotein; 1.
DR Pfam; PF00082; Peptidase_S8; 2.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51829; P_HOMO_B; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:EHL02186.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005446};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 500..523
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 259..394
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 421..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 577..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..482
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..598
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 650 AA; 71141 MW; 9F6472CBECABEFAC CRC64;
MEKRGVLPPP PAGYASPVQR QAPPPEDAAV AKQKEVMKAL EISDPIFNEQ WHLYNPVQVG
HDVNVTDVWM QGITGHNATV AIVDDGLDMY SDDLKDNYFQ EGSYDFNDHT EEPKPRLSDD
RHGTRCAGEV ITVGAIDRKG LHPYYSEHCS AQLVVTYSSG SGDAIHTTDV GTNQCYSGHG
GTSAAAPLAA GIFALVLQIR PDLSWRDMQY LVLMTALPID LDTGEWQTTT IGRKFSHTFG
YGKIDTWATI EAAKTFKNVK PQAWYYSPWI HVNQTIPQGD EGLSVSFEVT KQMLQEANLE
RLEHVTVTMN VEHGRRGDIS VDLISPDNLV SHLSVTRRLD NAPEGYVDWT FMSVVHWGEA
GIGKWTIVVK DTMVNEFNGT FTDWHLKLWG ESIDASKAVQ LPLPSDEDDD DHDAIASSTT
TIMASTTPVA PAPSKTSILV NPTDHPDRPT KPTAPVEEEE TAAPTVEPSP TGSPAAATSS
PSTWIPSFVP TFGIGHKARV WILGAVGLIL AFCIGLGIYL FMARRKRLRN NPRDEWEFDL
LEEDEADGLN GAGKTTRGGK GGKRRAGELY DAFAAGSEDE SDGDFDDEGG DEQEKKLYED
DESEGSGSAL RSPSHHVIGD LDSDDEDSIC HSWELGEMVL GVLFCAIGKE
//
