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
//