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Database: UniProt
Entry: A0A0D2K8N3_9CHLO
LinkDB: A0A0D2K8N3_9CHLO
Original site: A0A0D2K8N3_9CHLO 
ID   A0A0D2K8N3_9CHLO        Unreviewed;      1012 AA.
AC   A0A0D2K8N3;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=26S proteasome non-ATPase regulatory subunit 1 homolog {ECO:0000256|PIRNR:PIRNR015947};
GN   ORFNames=MNEG_1396 {ECO:0000313|EMBL:KIZ06553.1};
OS   Monoraphidium neglectum.
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Sphaeropleales; Selenastraceae; Monoraphidium.
OX   NCBI_TaxID=145388 {ECO:0000313|EMBL:KIZ06553.1, ECO:0000313|Proteomes:UP000054498};
RN   [1] {ECO:0000313|EMBL:KIZ06553.1, ECO:0000313|Proteomes:UP000054498}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SAG 48.87 {ECO:0000313|EMBL:KIZ06553.1,
RC   ECO:0000313|Proteomes:UP000054498};
RX   PubMed=24373495; DOI=10.1186/1471-2164-14-926;
RA   Bogen C., Al-Dilaimi A., Albersmeier A., Wichmann J., Grundmann M.,
RA   Rupp O., Lauersen K.J., Blifernez-Klassen O., Kalinowski J., Goesmann A.,
RA   Mussgnug J.H., Kruse O.;
RT   "Reconstruction of the lipid metabolism for the microalga Monoraphidium
RT   neglectum from its genome sequence reveals characteristics suitable for
RT   biofuel production.";
RL   BMC Genomics 14:926-926(2013).
CC   -!- FUNCTION: Acts as a regulatory subunit of the 26S proteasome which is
CC       involved in the ATP-dependent degradation of ubiquitinated proteins.
CC       {ECO:0000256|PIRNR:PIRNR015947}.
CC   -!- SUBUNIT: Component of the 19S regulatory particle (RP/PA700) base
CC       subcomplex of the 26S proteasome. The 26S proteasome is composed of a
CC       core protease (CP), known as the 20S proteasome, capped at one or both
CC       ends by the 19S regulatory particle (RP/PA700).
CC       {ECO:0000256|PIRNR:PIRNR015947}.
CC   -!- SIMILARITY: Belongs to the proteasome subunit S1 family.
CC       {ECO:0000256|ARBA:ARBA00006308, ECO:0000256|PIRNR:PIRNR015947}.
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DR   EMBL; KK100357; KIZ06553.1; -; Genomic_DNA.
DR   RefSeq; XP_013905572.1; XM_014050118.1.
DR   AlphaFoldDB; A0A0D2K8N3; -.
DR   STRING; 145388.A0A0D2K8N3; -.
DR   GeneID; 25731474; -.
DR   KEGG; mng:MNEG_1396; -.
DR   OrthoDB; 151732at2759; -.
DR   Proteomes; UP000054498; Unassembled WGS sequence.
DR   GO; GO:0008540; C:proteasome regulatory particle, base subcomplex; IEA:UniProtKB-UniRule.
DR   GO; GO:0030234; F:enzyme regulator activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0042176; P:regulation of protein catabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR   InterPro; IPR016642; 26S_Psome_Rpn2.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR002015; Proteasome/cyclosome_rpt.
DR   InterPro; IPR048570; PSMD1_RPN2_N.
DR   InterPro; IPR040623; RPN2_C.
DR   PANTHER; PTHR10943; 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT; 1.
DR   PANTHER; PTHR10943:SF2; 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT 1; 1.
DR   Pfam; PF13646; HEAT_2; 1.
DR   Pfam; PF01851; PC_rep; 1.
DR   Pfam; PF18004; RPN2_C; 1.
DR   Pfam; PF21505; RPN2_N; 1.
DR   PIRSF; PIRSF015947; 26S_Psome_Rpn2; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
PE   3: Inferred from homology;
KW   Proteasome {ECO:0000256|ARBA:ARBA00022942, ECO:0000256|PIRNR:PIRNR015947};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054498};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          2..348
FT                   /note="26S proteasome non-ATPase regulatory subunit 1/RPN2
FT                   N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21505"
FT   DOMAIN          787..970
FT                   /note="26S proteasome regulatory subunit RPN2 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18004"
FT   REGION          271..316
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          836..926
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          985..1012
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        836..859
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        997..1012
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1012 AA;  106447 MW;  3F8992D5459AF678 CRC64;
     MTSAAGLLTL LEEDNDTLKQ YALVNLDKVV HDFWFQISPS IASVEALYED EAFKKRELAA
     LIASKVFYHL GELDSALTYA LGAGSYFDVN ENSEYVRTLV ARCLDQYFDS RRRQVEGGEE
     SAEVDPRLVA VVERMVETAC QAGQWEQAVG VALEARRLDI LEAVVGRCPD KGSILSYALR
     VTQRLVINRN FRHQVLRLLV RLAEESPSPD WVEVCQCLMF LDDAPRVAAI LGRLVEGSED
     DALVAYQAAF DLVENEMQSF LQAVLDRLPK PPEPATPAPV AAAAPADGAA MDTDGAADAA
     ADANGGAPPE AAAPSVDPAK AERLARLLGI LAGTTPIGLT LEFLYHNNHA DLQVLKNLKA
     SVDARVSVLH SATILANALV HAGTSVDTFL RENLEWLSRA TNWAKFSATA GLGVIHRGQL
     QQGKALLAPY LPRDGAGGSP YSEGGALYAL GLIAANHGAG HRTFLLESLR AAGSPVIQHG
     ACLGLGLACL GTCDEEAFED LKNTLYTDDA VAGEAAGLAM GLLLCGSSSD KAQEMLAYAH
     DTAHEKIIRG LALGLALTGY SREEGADALV EQMSGDQDPI LRWGAMFCLG LAYRGTANNN
     AIARLLHCAV TDVSDDVRRA AVTSLGFVLM GNPEQCPRIV SLLAESFNPH VRYGAALAVG
     IACAGSGGRE AVALLESMVA DSVDFVRQGV YIALALVLLQ QPEGRVEGLR KRLAKAVGDK
     HEETMARMGA SVATGILDAG GRNVTVGLRS RSGYFRRTSV VGLALFTYHW YWHPVAHCLS
     LAFTPSALIG LDASLRTPKL EVNVAARPSL FAYPPPLTVE ASKEVAKVEK AVLSTTAKAR
     ERARKKELEK KDKEGGAAAE PAAKEGPSAM DTDDKAAAAA GSGAAAKEGG GAEGAVKAEG
     EEGGGAGAAS APKKPDEPSS YVLTTPSRMT LQQVRFVSFA PDSRFVPVKR GAPPIGFVVL
     RDTRPGEPVD YAASAAVGGV VGAAGGAAGA GPAAAPVQDA EPPPPAPFEF DG
//
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