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Database: UniProt
Entry: A0A1Y1VXD7_9FUNG
LinkDB: A0A1Y1VXD7_9FUNG
Original site: A0A1Y1VXD7_9FUNG 
ID   A0A1Y1VXD7_9FUNG        Unreviewed;       968 AA.
AC   A0A1Y1VXD7;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Subtilisin-like protein {ECO:0000313|EMBL:ORX65947.1};
GN   ORFNames=DL89DRAFT_260625 {ECO:0000313|EMBL:ORX65947.1};
OS   Linderina pennispora.
OC   Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC   Kickxellomycetes; Kickxellales; Kickxellaceae; Linderina.
OX   NCBI_TaxID=61395 {ECO:0000313|EMBL:ORX65947.1, ECO:0000313|Proteomes:UP000193922};
RN   [1] {ECO:0000313|EMBL:ORX65947.1, ECO:0000313|Proteomes:UP000193922}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12442 {ECO:0000313|EMBL:ORX65947.1,
RC   ECO:0000313|Proteomes:UP000193922};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA   Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA   Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA   Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (JUL-2016) 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:ORX65947.1}.
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DR   EMBL; MCFD01000019; ORX65947.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y1VXD7; -.
DR   STRING; 61395.A0A1Y1VXD7; -.
DR   OrthoDB; 662485at2759; -.
DR   Proteomes; UP000193922; Unassembled WGS sequence.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008240; F:tripeptidyl-peptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.20.25.690; -; 1.
DR   Gene3D; 2.60.40.3170; -; 1.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   InterPro; IPR048383; TPPII_Ig-like-1.
DR   InterPro; IPR022229; TPPII_Ig-like-2.
DR   InterPro; IPR046940; TPPII_Ig-like_sf.
DR   PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR   PANTHER; PTHR43806:SF14; TRIPEPTIDYL-PEPTIDASE 2; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   Pfam; PF12580; TPPII; 1.
DR   Pfam; PF21223; TPPII_Ig-like-1; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
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:UP000193922};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}.
FT   DOMAIN          36..484
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   DOMAIN          501..577
FT                   /note="Tripeptidyl-peptidase II first Ig-like"
FT                   /evidence="ECO:0000259|Pfam:PF21223"
FT   DOMAIN          670..810
FT                   /note="Tripeptidyl peptidase II second Ig-like"
FT                   /evidence="ECO:0000259|Pfam:PF12580"
FT   REGION          873..915
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        875..915
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        45
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        253
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        439
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   968 AA;  105483 MW;  91F77D985F0518DD CRC64;
     MSGNKTPHTQ FPTHGLLPRA DTQAGDFVRK HPHYDGRGTI VAVLDTGIAP MAMGLHTTTD
     GKRKVLDYVD CTGSGDVRLQ APRTNADELV GATGRKLKVN SKWKNPTGEW RVGAKRLYEI
     TPDILKEDIK KERQAVFWLT ALPRGLATSR PPKDEDAELK HELEAQREVL KDFGAKYEDP
     GPVLDILVFH DGKQWRAAID TQETGDFTGV EALGAYKLTG DIGKLAKRNL FYYTLNFYEE
     GKVLSIVANV GSHSTHVAGI IGAHHPDEPQ NDGVAPGAQL LSLMIGDHRV SSLETGTGLT
     RAANAIIEHG ADLANMSYGE PSATANSGQW VQLLRKEVIK KHRCIFVSSA GNEGPALSTA
     GAPGGASDDI IGVGAYVGYE QIKAEYTMYD TVKDTVFTWS SRGPTADGSR GVDIYAPGSA
     ITSYPTYTLQ RLHLANGTSM SSPNLCGCLA LLVSAWKHEF GKEGEPKVSP YRIKNAMMAT
     AKQFGDELAG WAGAVGSGVE LESQLKFEYE QRVILSTSES WIKVPEAVYV SSEGRSFDAR
     VDPTSLERGR LHVAEILGFD SRNVDRGAIF RIPVTITKPS EVGASGCVRF PALRFQPTEV
     VRRFIDVPRV QLAPQTRFTQ YELNTHVTIG HSTYAENGGL AEQSYTKTMK VLGGCTLEPV
     SRVDLVAAVR PEYGIKVTAT LDTLRRALRP AVSSITPLTL ERDTHPEAGT AIQQLILDYK
     YSTSANGVSI TPRLTGIDSL IYEAWTDNVA LLVFDAKKQR VGAHFGYPRP ITLRRKGDYL
     IRVQIRHRSA KDLGGAEAVS IPVEFALASV FTKTVSNVRN SSKSIQLNNI MPVFLKTFAV
     NPPKDTVPGD ILRGSLSASP NTADLLLEYV VPSKANEEKQ PDESSTKSSS KKQGDSKKKE
     AEESQADKDR KAMQEAMRNL KIEWVKKAQD PDVRTELIRQ LEAEQANDTQ VLACAAGVAG
     LRAQDTAD
//
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