ID A0A094GFJ1_9PEZI Unreviewed; 580 AA.
AC A0A094GFJ1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=PCI domain-containing protein {ECO:0000259|PROSITE:PS50250};
GN ORFNames=V500_01286 {ECO:0000313|EMBL:KFY99758.1};
OS Pseudogymnoascus sp. VKM F-4518 (FW-2643).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420913 {ECO:0000313|EMBL:KFY99758.1, ECO:0000313|Proteomes:UP000029284};
RN [1] {ECO:0000313|EMBL:KFY99758.1, ECO:0000313|Proteomes:UP000029284}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4518 (FW-2643) {ECO:0000313|Proteomes:UP000029284};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the proteasome subunit S3 family.
CC {ECO:0000256|ARBA:ARBA00007912}.
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:KFY99758.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JPKC01000365; KFY99758.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094GFJ1; -.
DR STRING; 1420913.A0A094GFJ1; -.
DR HOGENOM; CLU_019858_1_1_1; -.
DR Proteomes; UP000029284; 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 InterPro; IPR013586; 26S_Psome_reg_C.
DR InterPro; IPR000717; PCI_dom.
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:UP000029284}.
FT DOMAIN 326..506
FT /note="PCI"
FT /evidence="ECO:0000259|PROSITE:PS50250"
FT REGION 1..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 550..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..564
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..580
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 580 AA; 64292 MW; E42CCC19CE468143 CRC64;
MPSKTPHTNG NDPVENGTHD IEMKDDAPAS KKGGKGKKVN QGEDEMTVVV PPSKASKLSA
PPPPDAEGDV AMDEETATSE VEAEVDPIAL TIANIKNDFA LLEKAVALFD ARFTLRALRS
ISTIRKHLSA DILAQVITET YPASSSAAKH LLQALNKEDA TFTRQTAPDM DVDGDVKATA
KNGSKKETKE IIPEIDVFLG ILVQVLFADQ KENEKGAKFS SQLAEQIHSL NRRTLDSLAA
RTYFYFSLFA EQLQPLPPSP NSPVVSLRPA LLAALRTAVL RKDIDTQATV IVLLLRNYLS
TSHITQADLL VSHTKFPENA SNNQVARYLY YLGRIRAIQL RYTEAHEHLT AATRKAPSSP
SAAGFTQTAT KLLLVVELLM GDIPERATFS MASLERALAP YLLLVQAVRV GNLVDFETSI
KQHSDTFRRD GTYTLILRLR QNVIKTGIRM MSLSYSRISL RDICIRLHLG SEESAEYIVA
KAIRDGVIEA TLDRERGFMK SKEIGDVYAT REPGEAFHDR IRACLALHDE SIKAMRFPMN
QHRLELKNAQ EAREREREMA KEIQDGDLDE DDLGGEFEGM
//