ID A0A3N2QAA5_9PEZI Unreviewed; 458 AA.
AC A0A3N2QAA5;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Proteasome regulatory particle subunit Rpt2 {ECO:0000313|EMBL:ROT43680.1};
GN ORFNames=SODALDRAFT_305873 {ECO:0000313|EMBL:ROT43680.1};
OS Sodiomyces alkalinus F11.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Sodiomyces.
OX NCBI_TaxID=1314773 {ECO:0000313|EMBL:ROT43680.1, ECO:0000313|Proteomes:UP000272025};
RN [1] {ECO:0000313|EMBL:ROT43680.1, ECO:0000313|Proteomes:UP000272025}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F11 {ECO:0000313|EMBL:ROT43680.1,
RC ECO:0000313|Proteomes:UP000272025};
RX PubMed=30368956; DOI=10.1111/mec.14912;
RA Grum-Grzhimaylo A.A., Falkoski D.L., van den Heuvel J.,
RA Valero-Jimenez C.A., Min B., Choi I.G., Lipzen A., Daum C.G., Aanen D.K.,
RA Tsang A., Henrissat B., Bilanenko E.N., de Vries R.P., van Kan J.A.L.,
RA Grigoriev I.V., Debets A.J.M.;
RT "The obligate alkalophilic soda-lake fungus Sodiomyces alkalinus has
RT shifted to a protein diet.";
RL Mol. Ecol. 27:4808-4819(2018).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
CC {ECO:0000256|ARBA:ARBA00006914, ECO:0000256|RuleBase:RU003651}.
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DR EMBL; ML119051; ROT43680.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N2QAA5; -.
DR STRING; 1314773.A0A3N2QAA5; -.
DR OrthoDB; 1707207at2759; -.
DR Proteomes; UP000272025; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0008540; C:proteasome regulatory particle, base subcomplex; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR032501; Prot_ATP_ID_OB_2nd.
DR PANTHER; PTHR23073; 26S PROTEASOME REGULATORY SUBUNIT; 1.
DR PANTHER; PTHR23073:SF24; 26S PROTEASOME REGULATORY SUBUNIT 4; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF16450; Prot_ATP_ID_OB_C; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00674; AAA; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU003651};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW Proteasome {ECO:0000256|ARBA:ARBA00022942, ECO:0000313|EMBL:ROT43680.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000272025}.
FT DOMAIN 236..375
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 458 AA; 50892 MW; A01BFF63101A0272 CRC64;
MGQNQSGMGG GGEGREDKDK KKQKPKYEPP PRPTTRVGRK KRKAGGTSAA AKLPAVFPTS
RCKLRLLRMQ RIHDHLILEE EYVENQERLR KAKAAKEGSS VNPENELDRL ADERSRVDDM
RGSPMGVGTL EEMIDDDHAI VSSTTGPEYY VSIMSFVDKD LLEPGASVLL HHKSVSVVGV
LTDDTDPLVS VMKLDKAPTE SYADIGGLEN QIQEVRESVE LPLLHPELYE EMGIKPPKGV
ILYGAPGTGK TLLAKAVANQ TSATFLRIVG SELIQKYLGD GPRLVRQLFQ VAAENAPSIV
FIDEIDAIGT KRYESTSGGE REIQRTMLEL LNQLDGFDDR GDVKVIMATN KIETLDPALI
RPGRIDRKIL FENPDQNTKR KIFTLHTSKM SLNPDVDLEE FISAKDDLSG ADIKAICSEA
GLMALRERRM RVQMADFRAA RERVLRTKQE SEPEGLYL
//
