ID A0A166DRY2_9AGAM Unreviewed; 503 AA.
AC A0A166DRY2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=PCI-domain-containing protein {ECO:0000313|EMBL:KZV67864.1};
GN ORFNames=PENSPDRAFT_583269 {ECO:0000313|EMBL:KZV67864.1};
OS Peniophora sp. CONT.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Russulales; Peniophoraceae; Peniophora.
OX NCBI_TaxID=1314672 {ECO:0000313|EMBL:KZV67864.1, ECO:0000313|Proteomes:UP000077086};
RN [1] {ECO:0000313|EMBL:KZV67864.1, ECO:0000313|Proteomes:UP000077086}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CONT {ECO:0000313|EMBL:KZV67864.1,
RC ECO:0000313|Proteomes:UP000077086};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- SIMILARITY: Belongs to the proteasome subunit S3 family.
CC {ECO:0000256|ARBA:ARBA00007912}.
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DR EMBL; KV424568; KZV67864.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166DRY2; -.
DR STRING; 1314672.A0A166DRY2; -.
DR InParanoid; A0A166DRY2; -.
DR OrthoDB; 514836at2759; -.
DR Proteomes; UP000077086; Unassembled WGS sequence.
DR GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR GO; GO:0030234; F:enzyme regulator activity; IEA:InterPro.
DR GO; GO:0042176; P:regulation of protein catabolic process; IEA:InterPro.
DR Gene3D; 1.25.40.570; -; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR013586; 26S_Psome_reg_C.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR10758:SF2; 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT 3; 1.
DR PANTHER; PTHR10758; 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT 3/COP9 SIGNALOSOME COMPLEX SUBUNIT 3; 1.
DR Pfam; PF01399; PCI; 1.
DR Pfam; PF08375; Rpn3_C; 1.
DR SMART; SM00753; PAM; 1.
DR SMART; SM00088; PINT; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50250; PCI; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000077086}.
FT DOMAIN 249..429
FT /note="PCI"
FT /evidence="ECO:0000259|PROSITE:PS50250"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 100..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 468..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..486
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..503
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 503 AA; 56306 MW; FA3A4C16E911211B CRC64;
MADVEMKADD TSKTETAEEK KEPTPALTPV AEIKSNASLI ERAVATLEPR FTHRVLRTLT
ALRKRLDDKA LRDAVAEVYP KVDSATKSAL LEWIPASSEG SMDVDAAPST TPASKPVTNE
PAPEVEVYLR LLVVHHLLKS EAGYAKAKEL ANETISVIQR LNRRTMDPIS AKVWYAVERT
YELAGELDSA RPLFLAAQRT ASLRHDDETQ ASLINRLLRS YTTSNLYDQA DKLVSKTTFP
PAASNAQYAR FHYYLGRIKA VKLDYTVAHT NLQQAIRRAP QARVAPGFWQ AVHKLFIVVE
LLMGDIPDRG LFRHPVLEKA LGPYFDIVKA VRTGSLAEFQ TTLATHASAF ESDKTYTLIA
RLRQNVIKTG IRRLSLSYAR ISLRDICVKL HLDSEEDAEY IVGKAIRDGV IEGRILHEKG
WMECQGLKSS YGPEVSEMFS KRIGYCMELH NESVKAMRYP MNAHRKELAD AEDAREREKE
LVKEIAEGEL DEDDGLGGPG PEF
//