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Database: UniProt
Entry: A6RB90_AJECN
LinkDB: A6RB90_AJECN
Original site: A6RB90_AJECN 
ID   A6RB90_AJECN            Unreviewed;      1134 AA.
AC   A6RB90;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   RecName: Full=26S proteasome regulatory subunit RPN2 {ECO:0000256|PIRNR:PIRNR015947};
GN   ORFNames=HCAG_06228 {ECO:0000313|EMBL:EDN10425.1};
OS   Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS   (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX   NCBI_TaxID=2059318 {ECO:0000313|EMBL:EDN10425.1, ECO:0000313|Proteomes:UP000009297};
RN   [1] {ECO:0000313|Proteomes:UP000009297}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NAm1 / WU24 {ECO:0000313|Proteomes:UP000009297};
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
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   -!- SIMILARITY: Belongs to the proteasome subunit S1 family.
CC       {ECO:0000256|ARBA:ARBA00006308, ECO:0000256|PIRNR:PIRNR015947}.
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DR   EMBL; CH476661; EDN10425.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6RB90; -.
DR   STRING; 339724.A6RB90; -.
DR   VEuPathDB; FungiDB:HCAG_06228; -.
DR   HOGENOM; CLU_002323_0_1_1; -.
DR   OMA; IMFGRQE; -.
DR   OrthoDB; 151732at2759; -.
DR   Proteomes; UP000009297; 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; 2.
DR   PIRSF; PIRSF015947; 26S_Psome_Rpn2; 1.
DR   SUPFAM; SSF48371; ARM repeat; 2.
PE   3: Inferred from homology;
KW   Proteasome {ECO:0000256|ARBA:ARBA00022942, ECO:0000256|PIRNR:PIRNR015947};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009297};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          6..134
FT                   /note="26S proteasome non-ATPase regulatory subunit 1/RPN2
FT                   N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21505"
FT   DOMAIN          197..439
FT                   /note="26S proteasome non-ATPase regulatory subunit 1/RPN2
FT                   N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21505"
FT   DOMAIN          886..1059
FT                   /note="26S proteasome regulatory subunit RPN2 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18004"
FT   REGION          358..403
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          939..1006
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1112..1134
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        378..396
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        941..955
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        970..1006
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1134 AA;  124275 MW;  F559EED4832E15BD CRC64;
     MVGLVSADGL VGFLSEPDPE LKIFALKALD AQVDLLWTEI ADSIDRIEAL YEDESFPERE
     LAALLASKVY YHLQEYNESM VFALGAGKLL NLDHGGEFEE TIISKCIDTF ISISASPKTQ
     NAAQTANKTP RLNTSFPLTT NGATSTSAGL TSPITPFSQS ALPSKSLLSR KDSISLETGG
     EDTGAYPSEL TLVVQRGVQK QLQAVIERLF EQCFREKRYR QVVGIAVEAK NLDVLRAAIL
     RASEDEKKTE ESSRSGEELK EYVLDICMSV VQERAFRNEI LKLILELLNE IPSPDYFSIA
     KCVVYLNEHS MASEILRQLV EKGDPRSLSV AYQISFDLYD NSTQEFLRKV RQEISQLIPA
     SNESESQDTE DDGSAAKETD SLLQNQEGTV NSSNSRRLGS REEKYKLSED AQAALKSIGD
     IIDGVNSIQL NLEFLYRNNK ADIAVLNKIK DSLEARNSIF HNAVTLCNAF MHAGTTHDKF
     FRDNLEWLGK AVNWSKFTAT AALGVIHRGN LTQGQKLLAP YLPKDNIAGV GGSGSVYSQG
     GSLYAFGLIY ANHEGWAVDL IREHFTKATE EVVQHGGALG LGVAGMATGD EGIYNDLKAV
     LETDSALNGE AVGLAMGLVM LGTGNMKALE DMIRYAHDTQ HEKIIRGVAM GMALIMYGRQ
     EAADELINGL LGDPDPTLRY GGIMAIALAY CGTGSNRAVR RLLHVAVSDV SDDVRRVAVL
     SLGFISSAKH QSVPRIVELL SESYNPHVRY GATMALGISC AGTGLDEAVD LLEPMLKDPT
     DFVRQGALIA LAMVLVQQNE TMNPKVGIIR KTMQKMITDR HEDAMAKFGC ALALGIIDAG
     GRNCTISLQT QTGNLNMPGI IGMAVFIQYW YWFPLSHFLS LSFTPTAVIG VDQRLEVPIF
     KFHSNTRPSL FDYPPEQQVK ADEAPEKVKT AVLSTTAQAI RRAQRREKQQ RRESMDIDQT
     PATPKVSTQH LDKMDVDETE VKTEEEGNDR VKEETPTEAP KRKAEKEKVG YELENMSRVL
     PAQLKFLTFP DPRYEPVKRP TGGVVVVLDK TPSEPREIIE LRASRETKLA AAGETIQDRI
     NAAMSALEQP AVAGTFGGAA AAAGVLTAVD EDEEGAEEAP VPNEFDYYSD AAED
//
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