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Database: UniProt
Entry: A0A0F8A6I0_9HYPO
LinkDB: A0A0F8A6I0_9HYPO
Original site: A0A0F8A6I0_9HYPO 
ID   A0A0F8A6I0_9HYPO        Unreviewed;       507 AA.
AC   A0A0F8A6I0;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=26S protease regulatory subunit 4-like protein {ECO:0000313|EMBL:KJZ77114.1};
GN   ORFNames=HIM_03435 {ECO:0000313|EMBL:KJZ77114.1};
OS   Hirsutella minnesotensis 3608.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Hirsutella.
OX   NCBI_TaxID=1043627 {ECO:0000313|EMBL:KJZ77114.1, ECO:0000313|Proteomes:UP000054481};
RN   [1] {ECO:0000313|EMBL:KJZ77114.1, ECO:0000313|Proteomes:UP000054481}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3608 {ECO:0000313|EMBL:KJZ77114.1,
RC   ECO:0000313|Proteomes:UP000054481};
RX   PubMed=25359922; DOI=10.1093/gbe/evu241;
RA   Lai Y., Liu K., Zhang X., Zhang X., Li K., Wang N., Shu C., Wu Y., Wang C.,
RA   Bushley K.E., Xiang M., Liu X.;
RT   "Comparative genomics and transcriptomics analyses reveal divergent
RT   lifestyle features of nematode endoparasitic fungus Hirsutella
RT   minnesotensis.";
RL   Genome Biol. Evol. 6:3077-3093(2014).
CC   -!- SUBCELLULAR LOCATION: 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; KQ030508; KJZ77114.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F8A6I0; -.
DR   OrthoDB; 1707207at2759; -.
DR   Proteomes; UP000054481; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0008540; C:proteasome regulatory particle, base subcomplex; IEA:UniProt.
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:SF24; 26S PROTEASOME REGULATORY SUBUNIT 4; 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   Hydrolase {ECO:0000313|EMBL:KJZ77114.1};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW   Protease {ECO:0000313|EMBL:KJZ77114.1};
KW   Proteasome {ECO:0000256|ARBA:ARBA00022942};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054481}.
FT   DOMAIN          227..366
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          1..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          85..115
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          439..507
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..27
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        85..111
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        470..494
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   507 AA;  56033 MW;  CD18D90ED3AF7B30 CRC64;
     MGGGDGRDDK DKKKDKPKYE PPPRPTTRVG RKKRKAGGTS AAAKLPAVYP TSRCKLRLLR
     MQRIHDHLLL EEEYVENQER LRKAKAAKEG SIAGADADDR LADERGRVDD MRGSPMGVGT
     LEELIDDDHA IVSSTTGPEY YVSIMSFVDK DLLEPGASVL LHHKSVSIVG VLTDDTDPIV
     SVMKLDKAPT ESYADIGGLE QQIQEVRESV ELPLLHPELY EEMGIKPPKG VILYGAPGTG
     KTLLAKAVAN QTSATFLRIV GSELIQKYLG DGPRLVRQLF QVAGENAPSI VFIDEIDAIG
     TKRYDSTSGG EREVQRTMLE LLNQLDGFDD RGDVKVIMAT NKIDTLDPAL IRPGRIDRKI
     LFENPDQNTK RKIFTLHTSK MNLGDDVDLE EFISQKDDLS GADIKAICSE AGMMALRERR
     MRVQMADFRS ARERVLRTKQ EGEPEGKKMM FDGGGVVGPR GASQLDDSEG YKSVSKDSDS
     WARALERNIA NHARDEQQLP HATLTAK
//
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