ID D8PWT6_SCHCM Unreviewed; 412 AA.
AC D8PWT6;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=AAA+ ATPase domain-containing protein {ECO:0000259|SMART:SM00382};
GN ORFNames=SCHCODRAFT_81361 {ECO:0000313|EMBL:EFJ00271.1};
OS Schizophyllum commune (strain H4-8 / FGSC 9210) (Split gill fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Schizophyllaceae; Schizophyllum.
OX NCBI_TaxID=578458 {ECO:0000313|Proteomes:UP000007431};
RN [1] {ECO:0000313|EMBL:EFJ00271.1, ECO:0000313|Proteomes:UP000007431}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H4-8 / FGSC 9210 {ECO:0000313|Proteomes:UP000007431};
RX PubMed=20622885; DOI=10.1038/nbt.1643;
RA Ohm R.A., de Jong J.F., Lugones L.G., Aerts A., Kothe E., Stajich J.E.,
RA de Vries R.P., Record E., Levasseur A., Baker S.E., Bartholomew K.A.,
RA Coutinho P.M., Erdmann S., Fowler T.J., Gathman A.C., Lombard V.,
RA Henrissat B., Knabe N., Kuees U., Lilly W.W., Lindquist E., Lucas S.,
RA Magnuson J.K., Piumi F., Raudaskoski M., Salamov A., Schmutz J.,
RA Schwarze F.W.M.R., vanKuyk P.A., Horton J.S., Grigoriev I.V.,
RA Woesten H.A.B.;
RT "Genome sequence of the model mushroom Schizophyllum commune.";
RL Nat. Biotechnol. 28:957-963(2010).
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
CC {ECO:0000256|ARBA:ARBA00006914, ECO:0000256|RuleBase:RU003651}.
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DR EMBL; GL377303; EFJ00271.1; -; Genomic_DNA.
DR RefSeq; XP_003035173.1; XM_003035127.1.
DR AlphaFoldDB; D8PWT6; -.
DR STRING; 578458.D8PWT6; -.
DR GeneID; 9594373; -.
DR KEGG; scm:SCHCO_02606231; -.
DR VEuPathDB; FungiDB:SCHCODRAFT_02606231; -.
DR eggNOG; KOG0727; Eukaryota.
DR HOGENOM; CLU_000688_2_0_1; -.
DR InParanoid; D8PWT6; -.
DR OMA; QDIGGMD; -.
DR OrthoDB; 5477077at2759; -.
DR Proteomes; UP000007431; Unassembled WGS sequence.
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 CDD; cd19502; RecA-like_PAN_like; 1.
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; 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:SF8; 26S PROTEASOME REGULATORY SUBUNIT 6B; 1.
DR Pfam; PF00004; AAA; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000007431}.
FT DOMAIN 192..331
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 412 AA; 46478 MW; 0445926E5135A72F CRC64;
MDQAGIEIQK TEPTFESVVS EKSQLFQELQ EEDLYIKFKK LTRHLELLDI QESYIKDEQA
NLKRELIRAQ EEVKRIQSVP LVIGQFLEPI DQHTGIVGST TGSNYVVRIM STLDRELLKP
SSSVALHRHS NALVDILPPE ADSSIAMLGV DEKPDVTYSD VGGMDSQKQE IREAVELPLT
HFDLYKKIGI DPPRGVLLYG PPGTGKTMLV KAVAHHTTAA FIRVVGSEFV QKYLGEGPRM
VRDVFRLARE NAPAIIFIDE IDAIATKRFD AQTGADREVQ RILLELLNQM DGFDQGSNVK
VIMATNRADT LDPALLRPGR LDRKIEFPNP SRREKRLIFQ TVTSKMNLGP DVDLEDFVSR
PDKLSSAEIA SIAQAAGLQA VRKNRYVILP VDFEEAWKQT VKRSDETHEF YR
//