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Database: UniProt
Entry: G4TD50_SERID
LinkDB: G4TD50_SERID
Original site: G4TD50_SERID 
ID   G4TD50_SERID            Unreviewed;       445 AA.
AC   G4TD50;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   SubName: Full=Probable RPT3-26S proteasome regulatory subunit {ECO:0000313|EMBL:CCA69223.1};
GN   ORFNames=PIIN_03123 {ECO:0000313|EMBL:CCA69223.1};
OS   Serendipita indica (strain DSM 11827) (Root endophyte fungus)
OS   (Piriformospora indica).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Sebacinales; Serendipitaceae; Serendipita.
OX   NCBI_TaxID=1109443 {ECO:0000313|EMBL:CCA69223.1, ECO:0000313|Proteomes:UP000007148};
RN   [1] {ECO:0000313|EMBL:CCA69223.1, ECO:0000313|Proteomes:UP000007148}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11827 {ECO:0000313|EMBL:CCA69223.1,
RC   ECO:0000313|Proteomes:UP000007148};
RX   PubMed=22022265; DOI=10.1371/journal.ppat.1002290;
RA   Zuccaro A., Lahrmann U., Guldener U., Langen G., Pfiffi S., Biedenkopf D.,
RA   Wong P., Samans B., Grimm C., Basiewicz M., Murat C., Martin F.,
RA   Kogel K.H.;
RT   "Endophytic Life Strategies Decoded by Genome and Transcriptome Analyses of
RT   the Mutualistic Root Symbiont Piriformospora indica.";
RL   PLoS Pathog. 7:e1002290-e1002290(2011).
CC   -!- SIMILARITY: Belongs to the AAA ATPase family.
CC       {ECO:0000256|ARBA:ARBA00006914, ECO:0000256|RuleBase:RU003651}.
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:CCA69223.1}.
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DR   EMBL; CAFZ01000050; CCA69223.1; -; Genomic_DNA.
DR   AlphaFoldDB; G4TD50; -.
DR   STRING; 1109443.G4TD50; -.
DR   eggNOG; KOG0727; Eukaryota.
DR   HOGENOM; CLU_000688_2_0_1; -.
DR   InParanoid; G4TD50; -.
DR   OMA; QDIGGMD; -.
DR   OrthoDB; 5477077at2759; -.
DR   Proteomes; UP000007148; 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, ECO:0000313|EMBL:CCA69223.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007148}.
FT   DOMAIN          192..331
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
SQ   SEQUENCE   445 AA;  50318 MW;  2469F88D2F1BC27E CRC64;
     MDEIGIEIHA EEPTFESVVT EKAALYQEMQ EDDYYIKYKK LSRHLEMLDI QETYIKDEQA
     NLKRELVRAQ EEVKRIQSVP LVIGQFLEPI DQHTGIVGST TGSNYVVRIL STLDRELLKP
     SSSVALHRHS NALVDILPPE ADSSISMLGA EQKPDVTYQD VGGMDSQKQE IREAVELPLT
     HFDLYKKIGI DPPRGVLLYG PPGTGKTMLV KAVAHHTTAS FIRVVGSEFV QKYLGEGPRM
     VRDVFRLARE NAPAIIFIDE IDAIATKRFD AQTGADREVQ RILLELLNQM DGFDQGSNVK
     VIMATNRADT LDPALLRPGR LDRKIEFPQP SRREKRLIFQ TITGKMNLSP DLDLEDFVSR
     PDKISSAEIA SICQAAGLQA VRKNRYVILP IDMEEAWKQV VKRNDETLEF CAFIANMDNS
     RIYIALQIDR ALALYGLRVV YLAFM
//
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