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Database: UniProt
Entry: Q45W60_PHACR
LinkDB: Q45W60_PHACR
Original site: Q45W60_PHACR 
ID   Q45W60_PHACR            Unreviewed;       854 AA.
AC   Q45W60;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   SubName: Full=Gag {ECO:0000313|EMBL:AAZ28941.1};
GN   Name=gag {ECO:0000313|EMBL:AAZ28941.1};
OS   Phanerochaete chrysosporium (strain RP-78 / ATCC MYA-4764 / FGSC 9002)
OS   (White-rot fungus) (Sporotrichum pruinosum).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Phanerochaetaceae; Phanerodontia; Phanerodontia chrysosporium.
OX   NCBI_TaxID=273507 {ECO:0000313|EMBL:AAZ28941.1};
RN   [1] {ECO:0000313|EMBL:AAZ28941.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=RP-78 {ECO:0000313|EMBL:AAZ28941.1};
RA   Novikova O., Fursov M., Shutov O., Blinov A.;
RT   "Divergent groups of LTR retrotransposons from Phanerochaete
RT   chrysosporium.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; DQ097842; AAZ28941.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q45W60; -.
DR   SMR; Q45W60; -.
DR   EnsemblFungi; AGR57_12567T0; AGR57_12567T0-p1; AGR57_12567.
DR   VEuPathDB; FungiDB:AGR57_12567; -.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd00303; retropepsin_like; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR025165; DUF4100.
DR   InterPro; IPR001995; Peptidase_A2_cat.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   Pfam; PF13650; Asp_protease_2; 1.
DR   Pfam; PF13352; DUF4100; 1.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS50175; ASP_PROT_RETROV; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 1.
PE   4: Predicted;
KW   Aspartyl protease {ECO:0000256|ARBA:ARBA00022750};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protease {ECO:0000256|ARBA:ARBA00022750}.
FT   DOMAIN          709..748
FT                   /note="Peptidase A2"
FT                   /evidence="ECO:0000259|PROSITE:PS50175"
FT   REGION          1..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          243..329
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          506..579
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          639..663
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..31
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        247..262
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        263..280
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        314..329
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        552..572
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   854 AA;  92850 MW;  EE1B02B08F27421F CRC64;
     MTQSSTGIKK KTVVPPSERV LRERDHRRAN SAPSPESNTR RTMPQAAAAT AAVPLLVQTM
     PLPGAKGAPH FTGKNVRRFV EAIELTGKAA GLSEHEMPPL LLRYSSRDVR ETMAGEGSVM
     NGNDWSKAKG MLIFYYGSRD RDTRRTAEEL RSFSKKSSRK KVGSLRALDR YFCNFSKKAG
     TLVADKLITQ AENDHLFYRG LPSRIRAKIK GRLVTLLSSQ GKALSAKCPP SVQETLAAAR
     GVFDPEDIDF SPGRKSRSED DESSSEDDSS SDESDDSDES DSDDGRKKGK GRGRSPGKRS
     KKSRDRRCSS EVRAKPAPST TTTSQEGGQM KELKDLADSM RQLLAVHVGM SNRPPSTPPT
     LFSPQGAPRS CYMCGKTEGT DLFHRIGMGN CPDTRELIAA GVIQYSPQGG LVYVDGRQLP
     RSPGAGTGGI AGLIRQEIAQ GRGGRDPPPH QSRAAMNLGL YADDQPVLRG GTVAMTVETA
     YAFPTTRAQA KAAGDDPVKY VRIEEEAGPS GARGPAVRKP ADPQGEFTRT RETVDAPPAV
     PHPSNLEGSW RERAGVDQDG RDDEDNRQKG RGTKPFRFTS TVQEQVASST VREQLLDTKV
     TISLREIIAV SPDLQRQFGM LVKTRREYNA KAGEWEVVET EADRSASNDT STTGEPQGDE
     PGVAYLTLQP GEDPHEILGR YTSAVSLGVK KSFARVVPIV EGVFGGEKVK FLLDSGSELN
     LVTRRVWEQT GVPIDEDGKR WSLRGIGGES VSLLGCARDA PVQIGGKNFD HHFFVSTREH
     GDYDGILGQP WLDWFSADVS YNRGGPTNLV AYPSGDKKGA HTSVEICGAY NPRNADRLIL
     TSHAHVEERA AGFQ
//
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