ID D2VAI3_NAEGR Unreviewed; 682 AA.
AC D2VAI3;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=26S proteasome regulatory subunit S3 {ECO:0000313|EMBL:EFC45961.1};
GN ORFNames=NAEGRDRAFT_79218 {ECO:0000313|EMBL:EFC45961.1};
OS Naegleria gruberi (Amoeba).
OC Eukaryota; Discoba; Heterolobosea; Tetramitia; Eutetramitia;
OC Vahlkampfiidae; Naegleria.
OX NCBI_TaxID=5762 {ECO:0000313|Proteomes:UP000006671};
RN [1] {ECO:0000313|EMBL:EFC45961.1, ECO:0000313|Proteomes:UP000006671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEG-M {ECO:0000313|EMBL:EFC45961.1,
RC ECO:0000313|Proteomes:UP000006671};
RX PubMed=20211133; DOI=10.1016/j.cell.2010.01.032;
RA Fritz-Laylin L.K., Prochnik S.E., Ginger M.L., Dacks J.B., Carpenter M.L.,
RA Field M.C., Kuo A., Paredez A., Chapman J., Pham J., Shu S., Neupane R.,
RA Cipriano M., Mancuso J., Tu H., Salamov A., Lindquist E., Shapiro H.,
RA Lucas S., Grigoriev I.V., Cande W.Z., Fulton C., Rokhsar D.S., Dawson S.C.;
RT "The genome of Naegleria gruberi illuminates early eukaryotic
RT versatility.";
RL Cell 140:631-642(2010).
CC -!- SIMILARITY: Belongs to the proteasome subunit S3 family.
CC {ECO:0000256|ARBA:ARBA00007912}.
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; GG738860; EFC45961.1; -; Genomic_DNA.
DR RefSeq; XP_002678705.1; XM_002678659.1.
DR AlphaFoldDB; D2VAI3; -.
DR STRING; 5762.D2VAI3; -.
DR EnsemblProtists; EFC45961; EFC45961; NAEGRDRAFT_79218.
DR GeneID; 8859154; -.
DR VEuPathDB; AmoebaDB:NAEGRDRAFT_79218; -.
DR eggNOG; KOG2581; Eukaryota.
DR InParanoid; D2VAI3; -.
DR OrthoDB; 514836at2759; -.
DR Proteomes; UP000006671; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Proteasome {ECO:0000313|EMBL:EFC45961.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006671}.
FT DOMAIN 243..451
FT /note="PCI"
FT /evidence="ECO:0000259|PROSITE:PS50250"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 577..679
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 682 AA; 79612 MW; CD3F6A71BCF40FC3 CRC64;
MTIKETTDAE MKESTSPTTT TLSPEEELEL VIKGELKDQL KLIAKSAQQD DLDNDRKQMR
AFRLFYNKLR RQITAKLLVS ILKELKCSHI VSYIEDTIGM QDDEQKPIPE AEIYLWLITI
IFLTDKKEYR RAYTCALDCV KYQQTLEKQQ KSRSVNFLFS KVYFYFSLAH EKLPTISNNE
FRNILLGRLR SCTLSHDNWS QFVILNCLLR SYLQDKLVEQ ANKLLKNVPV DQTIGHVDNS
QLARYFYYKG RIQSIQLEYS EAFNSLQTAL RKAPSAQPIK KSQGTESINP AKRTYGVGRG
FRIHTNKLLI VVSLLMGHIP DRSLFVNTIE ATNDSVTLSQ LKPYYELTQQ VRLGNVNGFE
TIVEKYRDQY IADDNLTLIN RIRQNVIRTG LKSIIKAYSR ISFADVSQKL HLNDVDINDV
QGIIAKAIKD GIIDAKIDES TQSVDTAKNQ DVYQTSEPAD EFDKRIQFCL SCRSQCIKAM
RYREEKKKKP TQQDSEDSLH LDIDELVDEE QTPTTEKNNE NIELEDDEQL ITRATRQQTQ
EYFQKHKISQ IIKQKLNEAF NLNHQDPVEY LFSTKRIQQQ DLKLQQQEKE LKELTKKHDE
ELTALQQSKE ASREALIEQE KQLVDQLEQL RKERKDLEDK IQQTEQQKKV RDENRKYNIE
LLKQRNAELS QENQKLSKEL SV
//
