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Database: UniProt
Entry: A0A0M0JGG4_9EUKA
LinkDB: A0A0M0JGG4_9EUKA
Original site: A0A0M0JGG4_9EUKA 
ID   A0A0M0JGG4_9EUKA        Unreviewed;       400 AA.
AC   A0A0M0JGG4;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=26s protease regulatory subunit 8-like a-like protein {ECO:0000313|EMBL:KOO25333.1};
GN   ORFNames=Ctob_004201 {ECO:0000313|EMBL:KOO25333.1};
OS   Chrysochromulina tobinii.
OC   Eukaryota; Haptista; Haptophyta; Prymnesiophyceae; Prymnesiales;
OC   Chrysochromulinaceae; Chrysochromulina.
OX   NCBI_TaxID=1460289 {ECO:0000313|EMBL:KOO25333.1, ECO:0000313|Proteomes:UP000037460};
RN   [1] {ECO:0000313|Proteomes:UP000037460}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CCMP291 {ECO:0000313|Proteomes:UP000037460};
RX   PubMed=26397803; DOI=10.1371/journal.pgen.1005469;
RA   Hovde B.T., Deodato C.R., Hunsperger H.M., Ryken S.A., Yost W., Jha R.K.,
RA   Patterson J., Monnat R.J. Jr., Barlow S.B., Starkenburg S.R.,
RA   Cattolico R.A.;
RT   "Genome Sequence and Transcriptome Analyses of Chrysochromulina tobin:
RT   Metabolic Tools for Enhanced Algal Fitness in the Prominent Order
RT   Prymnesiales (Haptophyceae).";
RL   PLoS Genet. 11:e1005469-e1005469(2015).
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:KOO25333.1}.
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DR   EMBL; JWZX01002989; KOO25333.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M0JGG4; -.
DR   OrthoDB; 360215at2759; -.
DR   Proteomes; UP000037460; Unassembled WGS sequence.
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:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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:SF155; 26S PROTEASOME REGULATORY SUBUNIT 10B; 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:KOO25333.1};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW   Protease {ECO:0000313|EMBL:KOO25333.1};
KW   Proteasome {ECO:0000256|ARBA:ARBA00022942};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037460}.
FT   DOMAIN          176..315
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   COILED          22..56
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   400 AA;  44717 MW;  FEA94FE3DC8A2423 CRC64;
     MAKVAAPTSA SGGIQNYYAA KIEELEVIVR ERTQNLRRLE AQRNELNSMV RHLREELSLL
     QEPGSYVGEL VAIMGRKKVL VKVHPEGKYV VDIDKSIDIG KLNVNDRVAL RNDSYALHLV
     LPSKVDPLVS LMKVEKVPDS TYDMVGGCDK QIKEIKEVIE LPIKHPELFE SLGIAQPKGV
     LMYGPPGTGK TLLARAVAHH TDCTFIRVSG GELVQKYIGE GSRMVRELFV MAREHAPSII
     FMDEIDSIGG ARQDGESGGD SEVQRTMLEL LNQLDGFEAT NQIKVVMATN RIDILDQALL
     RPGRIDRKIE FPNPNEDARL DILTIHSRKM NLTRGIDLRK IAKSMHEASG AETKAVCTEA
     GMFALRERRV HVTQDDFEMA VAKVMKKDSE KNTSLKKLWK
//
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