ID A0A1B8G7M5_9PEZI Unreviewed; 626 AA.
AC A0A1B8G7M5;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Vesicle formation at the endoplasmic reticulum {ECO:0000313|EMBL:OBT91827.1};
GN Name=SED4 {ECO:0000313|EMBL:OBT91827.1};
GN ORFNames=VE01_10177 {ECO:0000313|EMBL:OBT91827.1};
OS Pseudogymnoascus verrucosus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=342668 {ECO:0000313|EMBL:OBT91827.1, ECO:0000313|Proteomes:UP000091956};
RN [1] {ECO:0000313|EMBL:OBT91827.1, ECO:0000313|Proteomes:UP000091956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 10579 {ECO:0000313|EMBL:OBT91827.1,
RC ECO:0000313|Proteomes:UP000091956};
RA Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT "Comparative genomics of Pseudogymnoascus destructans, the fungus causing
RT white-nose syndrome of bats.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000091956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 10579 {ECO:0000313|Proteomes:UP000091956};
RX PubMed=29295979; DOI=10.1038/s41467-017-02441-z;
RA Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT "Extreme sensitivity to ultraviolet light in the fungal pathogen causing
RT white-nose syndrome of bats.";
RL Nat. Commun. 9:35-35(2018).
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|PROSITE-ProRule:PRU01032};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000256|PROSITE-
CC ProRule:PRU01032};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC {ECO:0000256|ARBA:ARBA00004239}.
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DR EMBL; KV460279; OBT91827.1; -; Genomic_DNA.
DR RefSeq; XP_018125560.1; XM_018279583.1.
DR AlphaFoldDB; A0A1B8G7M5; -.
DR STRING; 342668.A0A1B8G7M5; -.
DR GeneID; 28843563; -.
DR OrthoDB; 1405251at2759; -.
DR Proteomes; UP000091956; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04056; Peptidases_S53; 1.
DR CDD; cd11377; Pro-peptidase_S53; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015366; S53_propep.
DR InterPro; IPR030400; Sedolisin_dom.
DR PANTHER; PTHR14218:SF35; PEPTIDASE S53 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR14218; PROTEASE S8 TRIPEPTIDYL PEPTIDASE I CLN2; 1.
DR Pfam; PF09286; Pro-kuma_activ; 1.
DR SMART; SM00944; Pro-kuma_activ; 1.
DR SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51695; SEDOLISIN; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE-
KW ProRule:PRU01032}; Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01032};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU01032}; Protease {ECO:0000256|PROSITE-ProRule:PRU01032};
KW Reference proteome {ECO:0000313|Proteomes:UP000091956};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01032};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..626
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008608290"
FT DOMAIN 221..614
FT /note="Peptidase S53"
FT /evidence="ECO:0000259|PROSITE:PS51695"
FT ACT_SITE 297
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT ACT_SITE 301
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT ACT_SITE 517
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT BINDING 559
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT BINDING 560
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT BINDING 592
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT BINDING 594
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
SQ SEQUENCE 626 AA; 68006 MW; 64D8041C456043F0 CRC64;
MRAGGIVVGL LSLVGSALAK PAVEVFESVN ELPEGWTQVR TPAPETIVSL RVALEHPNQE
LFEQTLLDVS TPDHPKYGQH LTGAELKYML KPRDDSTESV MTWLASSNVP ASEIKNDGEW
INFRATVAQA EELLSTKFYV YKHNEDNKEM IRTLEYSLPS SVAPHVLTIQ PTTRFSRMMA
QRSTIHDISA MNAVFGVAAT NHKPAPAIPS TELDVKACNA SITPACLRAL YNVGDYQADP
KGKSLFGVAG YLQQYAKIND LNNFIAKYAP YAKGTTFNSV GVNGPNNPQN TTEDDVEANL
DIQYAVAMSY NIPVTYYSTS GLGELVPDLD QPDKATGQNE PYLDFITYLL SLPKDKLPQT
ITTSYGENEQ SVPPKYAKKV CSMFGELGLR GVSVLFSSGD TGVGSACQTN DGKNTTRFLP
IFPAACPWVT SVGGTYQVQP ERAVSFSSGG FSDLFPRPKY QDKAVKGFLR ILGDRWKGLY
NPAGRGFPDV AAQGYRFHVI DELANKTNPD ILVGGTSASA PAFAAIVALL NNARTSRHLP
PLGFLNPWIY SIGHYGLNDV THGGSTGCTG KDIYSKLPTP VVPFASWNAT EGWDPVTGHG
TPDFKKLLEL STPGGGWWGI GREKED
//
