ID   PRS6B_HELAN             Reviewed;         414 AA.
AC   P85200;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 1.
DT   03-AUG-2022, entry version 31.
DE   RecName: Full=26S proteasome regulatory subunit 6B homolog {ECO:0000250|UniProtKB:P54778};
OS   Helianthus annuus (Common sunflower).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC   Heliantheae alliance; Heliantheae; Helianthus.
OX   NCBI_TaxID=4232;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-277.
RC   STRAIN=cv. ANN1312 {ECO:0000269|Ref.1};
RA   Michelmore R.W., Knapp S., Rieseberg L., Bradford K., Kesseli R., Boore J.,
RA   Kozik A., Matvienko M., Lavelle D., Lai Z.;
RT   "Sunflower (Helianthus annuus) ESTs (set 2) from the compositae genome
RT   project http://compgenomics.ucdavis.edu/.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 208-414.
RC   STRAIN=cv. RHA801 {ECO:0000269|Ref.2};
RA   Kozik A., Michelmore R.W., Knapp S., Matvienko M., Rieseberg L., Lin H.,
RA   van Damme M., Lavelle D., Chevalier P., Ziegle J., Ellison P., Kolkman J.,
RA   Slabaugh M.S., Livingston K., Zhou Y., Lai Z., Church S., Jackson L.,
RA   Bradford K.;
RT   "Lettuce and sunflower ESTs from the compositae genome project
RT   http://compgenomics.ucdavis.edu/.";
RL   Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000305}
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND INDUCTION.
RA   Garcia J.S., Souza G.H.M.F., Eberlin M.N., Arruda M.A.Z.;
RT   "Evaluation of metal-ion stress in sunflower (Heliantus annus L.) leaves
RT   through proteomic changes.";
RL   Metallomics 1:107-113(2009).
CC   -!- FUNCTION: The 26S proteasome is involved in the ATP-dependent
CC       degradation of ubiquitinated proteins. The regulatory (or ATPase)
CC       complex confers ATP dependency and substrate specificity to the 26S
CC       complex (By similarity). {ECO:0000250|UniProtKB:P43686}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P43686}. Nucleus
CC       {ECO:0000250|UniProtKB:P43686}.
CC   -!- INDUCTION: Down-regulated in response to mixed metal ion contamination
CC       (cadmium, copper, lead and zinc), but not in response to zinc ion
CC       contamination. {ECO:0000269|Ref.3}.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000255}.
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DR   EMBL; DY920613; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BQ915537; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; P85200; -.
DR   SMR; P85200; -.
DR   PRIDE; P85200; -.
DR   EnsemblPlants; mRNA:HanXRQr2_Chr08g0346931; mRNA:HanXRQr2_Chr08g0346931; HanXRQr2_Chr08g0346931.
DR   Gramene; mRNA:HanXRQr2_Chr08g0346931; mRNA:HanXRQr2_Chr08g0346931; HanXRQr2_Chr08g0346931.
DR   OMA; VDNDHAI; -.
DR   OrthoDB; 571919at2759; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
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; IEA:InterPro.
DR   GO; GO:0030163; P:protein catabolic process; IEA:InterPro.
DR   Gene3D; 2.40.50.140; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR005937; 26S_Psome_P45-like.
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_C.
DR   InterPro; IPR035256; PSMC4.
DR   PANTHER; PTHR23073:SF120; PTHR23073:SF120; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF17862; AAA_lid_3; 1.
DR   Pfam; PF16450; Prot_ATP_ID_OB; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01242; 26Sp45; 1.
DR   PROSITE; PS00674; AAA; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Coiled coil; Cytoplasm; Nucleotide-binding; Nucleus;
KW   Proteasome.
FT   CHAIN           1..414
FT                   /note="26S proteasome regulatory subunit 6B homolog"
FT                   /id="PRO_0000397228"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          55..81
FT                   /evidence="ECO:0000255"
FT   BINDING         202..209
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   414 AA;  46652 MW;  9077A7DF34C9E1BD CRC64;
     MAATMVLDPK PSSTPPPTLP NPYTTDSQST DSEDDLYTRL KTLDRQIEFI DIQEEYVKDE
     LKNLKREQLR SQEEVKRIQS VPLVIGQFME MIDQNNGIVG STTGSNYYVR ILSTINRELL
     KPSASVALHR HSNALVDVLP PEADSSISLL SQSEKPDVTY NDIGGCDIQK QEIREAVELP
     LTHHELYKQI GIDPPRGVLL YGPPGTGKTM LAKAVANHTT AAFIRVVGSE FVQKYLGEGP
     RMVRDVFRLA KENAPAIIFI DEVDAIATAR FDAQTGADRE VQRILMELLN QMDGFDQTVN
     VKVIMATNRA DTLDPALLRP GRLDRKIEFP LPDRRQKRLV FQVCTAKMNL SDEVDLEDYV
     SRPDKISAAE ITAICQEAGM HAVRKNRYVI LPKDFEKGYR TNVKKPDTDF DFYK