ID Q38A02_TRYB2 Unreviewed; 408 AA.
AC Q38A02;
DT 22-NOV-2005, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2005, sequence version 1.
DT 27-MAR-2024, entry version 110.
DE SubName: Full=Proteasome regulatory ATPase subunit 6 {ECO:0000313|EMBL:EAN78368.1};
DE EC=3.6.4.8 {ECO:0000313|EMBL:EAN78368.1};
GN ORFNames=Tb10.6k15.0580 {ECO:0000313|EMBL:EAN78368.1};
OS Trypanosoma brucei brucei (strain 927/4 GUTat10.1).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX NCBI_TaxID=185431 {ECO:0000313|EMBL:EAN78368.1, ECO:0000313|Proteomes:UP000008524};
RN [1] {ECO:0000313|EMBL:EAN78368.1, ECO:0000313|Proteomes:UP000008524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=927/4 GUTat10.1 {ECO:0000313|EMBL:EAN78368.1,
RC ECO:0000313|Proteomes:UP000008524};
RX PubMed=16020726; DOI=10.1126/science.1112642;
RA Berriman M., Ghedin E., Hertz-Fowler C., Blandin G., Renauld H.,
RA Bartholomeu D.C., Lennard N.J., Caler E., Hamlin N.E., Haas B., Bohme U.,
RA Hannick L., Aslett M.A., Shallom J., Marcello L., Hou L., Wickstead B.,
RA Alsmark U.C., Arrowsmith C., Atkin R.J., Barron A.J., Bringaud F.,
RA Brooks K., Carrington M., Cherevach I., Chillingworth T.J., Churcher C.,
RA Clark L.N., Corton C.H., Cronin A., Davies R.M., Doggett J., Djikeng A.,
RA Feldblyum T., Field M.C., Fraser A., Goodhead I., Hance Z., Harper D.,
RA Harris B.R., Hauser H., Hostetler J., Ivens A., Jagels K., Johnson D.,
RA Johnson J., Jones K., Kerhornou A.X., Koo H., Larke N., Landfear S.,
RA Larkin C., Leech V., Line A., Lord A., Macleod A., Mooney P.J., Moule S.,
RA Martin D.M., Morgan G.W., Mungall K., Norbertczak H., Ormond D., Pai G.,
RA Peacock C.S., Peterson J., Quail M.A., Rabbinowitsch E., Rajandream M.A.,
RA Reitter C., Salzberg S.L., Sanders M., Schobel S., Sharp S., Simmonds M.,
RA Simpson A.J., Tallon L., Turner C.M., Tait A., Tivey A.R., Van Aken S.,
RA Walker D., Wanless D., Wang S., White B., White O., Whitehead S.,
RA Woodward J., Wortman J., Adams M.D., Embley T.M., Gull K., Ullu E.,
RA Barry J.D., Fairlamb A.H., Opperdoes F., Barrell B.G., Donelson J.E.,
RA Hall N., Fraser C.M., Melville S.E., El-Sayed N.M.;
RT "The genome of the African trypanosome Trypanosoma brucei.";
RL Science 309:416-422(2005).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC 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; CM000208; EAN78368.1; -; Genomic_DNA.
DR RefSeq; XP_823196.1; XM_818103.1.
DR AlphaFoldDB; Q38A02; -.
DR STRING; 185431.Q38A02; -.
DR PaxDb; 5691-EAN78368; -.
DR GeneID; 3662548; -.
DR KEGG; tbr:Tb10.6k15.0580; -.
DR eggNOG; KOG0728; Eukaryota.
DR InParanoid; Q38A02; -.
DR OMA; TANCRVA; -.
DR OrthoDB; 360215at2759; -.
DR Proteomes; UP000008524; Chromosome 10.
DR GO; GO:0005737; C:cytoplasm; IDA:GeneDB.
DR GO; GO:0005654; C:nucleoplasm; IDA:GeneDB.
DR GO; GO:0005838; C:proteasome regulatory particle; IDA:GeneDB.
DR GO; GO:0008540; C:proteasome regulatory particle, base subcomplex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0036402; F:proteasome-activating activity; IBA:GO_Central.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:GeneDB.
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; 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:SF166; 26S PROTEASOME REGULATORY SUBUNIT 8; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000313|EMBL:EAN78368.1};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW Proteasome {ECO:0000256|ARBA:ARBA00022942, ECO:0000313|EMBL:EAN78368.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008524}.
FT DOMAIN 183..323
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT COILED 27..68
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 408 AA; 45730 MW; 3C75C33F2BD5B2CF CRC64;
MATKMVTPTA TASDTDNPVS TYFLQKIQEL RAQEKRLQDN YMRLEAQRNE LNRRVRHLKE
EVQLLQESGS IVADVVRVMS KGKVLVNVSS SQGKLVVDVE KTVNIDDLSR NVRVALRSGT
FAIHYILPTK VDPLVSLMKV ENAGSESTYD EIGGLSRQVK EIKEVIELSV KHPELFEALG
IAQPKGVLLY GPPGTGKTLL ARAVAHHTDC TFIRVSGAEL VQKYIGEGAR LVRELFVMAR
EHSPSIIFMD EIDSIGSTRL ENTGRGGDSE VQRTMLELLN QLDGFESTQS IKVIMATNRV
DILDEALLRP GRIDRKIEFP APDEPARFEI LKIHSRKMNL TRGINLRTVA EKTNQCSGAE
LKAVCTEAGM FALRERRVHI TQEDFELAVA KIMHKDQDKS VSLKKMWK
//
