ID A0A0G2FH01_9PEZI Unreviewed; 817 AA.
AC A0A0G2FH01;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Putative minor extracellular protease vpr {ECO:0000313|EMBL:KKY33787.1};
GN ORFNames=UCDDA912_g06165 {ECO:0000313|EMBL:KKY33787.1};
OS Diaporthe ampelina.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Diaporthaceae; Diaporthe.
OX NCBI_TaxID=1214573 {ECO:0000313|EMBL:KKY33787.1, ECO:0000313|Proteomes:UP000034680};
RN [1] {ECO:0000313|EMBL:KKY33787.1, ECO:0000313|Proteomes:UP000034680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DA912 {ECO:0000313|EMBL:KKY33787.1};
RA Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT "Distinctive expansion of gene families associated with plant cell wall
RT degradation and secondary metabolism in the genomes of grapevine trunk
RT pathogens.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KKY33787.1, ECO:0000313|Proteomes:UP000034680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DA912 {ECO:0000313|EMBL:KKY33787.1};
RA Morales-Cruz A., Amrine K.C., Cantu D.;
RL Submitted (MAY-2015) 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 -!- 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:KKY33787.1}.
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DR EMBL; LCUC01000226; KKY33787.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G2FH01; -.
DR STRING; 1214573.A0A0G2FH01; -.
DR OrthoDB; 662485at2759; -.
DR Proteomes; UP000034680; 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; cd07489; Peptidases_S8_5; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 2.
DR InterPro; IPR010435; Fn3_5.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
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; 2.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 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:UP000034680};
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..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..817
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002544285"
FT DOMAIN 141..241
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 272..342
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 386..449
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 513..637
FT /note="Fn3-like"
FT /evidence="ECO:0000259|Pfam:PF06280"
FT ACT_SITE 150
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 201
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 430
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 817 AA; 87742 MW; AC1B299D6FD5AC6D CRC64;
MHLLNIAGLL LSALPSSGSA QPFAARQAPK ETNVTASVPR SYIIKYIAGS PKARRDVALA
ADIKVVKDFE TDVFSGASIE TDNHNVDSLL SLAGVVRAWP NKRVALSPVE GLSSIGDAAA
SNYTTHNATG VSKLHDRGIF GQGVKVGVVD SGTWYKHPAL GGGFGPGFKV AGGYDLVGNG
LWPVVIGDKA PDDDPEDQLG HGTHVAGIIA GKNDFWTGVA PEAELYSYKV FAQVDGTDEA
TLIEAFLRAY TDGAGYLPST FYFPSNVTDW PVVPLNFNTT DPADGCQPYP NGTRRLEGVI
PLVRRGTCTF AIKQQNLVAL GAEYILFYNN ESPLVTPGTD DDVGLIGLIT ADAGKAIIET
VQAGGNVTAD FSSNPEQVVG LAYPAGGRPN TFTSWGASND LQIKPDIAAP GGQIFSTYLD
NTYALLSGTS MATPYVAGVA ALYISVHGGR SVHGKDFART LHQRIISSGT SLPWSDGTAT
DYGFAAPVAQ VGNGLVNAFK VVNYTTGISF EKIALNDTKH FSGDHGVTIA NNGGKDVSYK
FSYEAAAGVE TLGWYSFVEP YGGEKRLRSF SELRPTSLPI EISVPADFTL GPGESKTVTV
SFPNPDGLGW NSSALPVYSG KVIVSGNNGE QVSVPYLGLA ADLNAEISPI YRPTYPFTNQ
RDYAYSFNLN ISSQDFPTIY SKLIWGSKEV RWDIYEPGWT EEQWKYPPVP GENGYIGPAT
SHVLADSASY FDPDLYDPDD TFTYPAVDLF RNAQTQNSYH QFWWFGKLGN GSQIELGNYT
MRFATLRPFG DPSVTDGWDI FKTPEIQVTG KYPRRGS
//
