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Database: UniProt
Entry: H1UVW1_COLHI
LinkDB: H1UVW1_COLHI
Original site: H1UVW1_COLHI 
ID   H1UVW1_COLHI            Unreviewed;       461 AA.
AC   H1UVW1;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   SubName: Full=26S protease regulatory subunit 6A {ECO:0000313|EMBL:CCF32112.1};
GN   ORFNames=CH063_00758 {ECO:0000313|EMBL:CCF32112.1}, CH63R_00118
GN   {ECO:0000313|EMBL:OBR14938.1};
OS   Colletotrichum higginsianum (strain IMI 349063) (Crucifer anthracnose
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum destructivum species complex.
OX   NCBI_TaxID=759273 {ECO:0000313|EMBL:CCF32112.1, ECO:0000313|Proteomes:UP000007174};
RN   [1] {ECO:0000313|EMBL:CCF32112.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMI 349063 {ECO:0000313|EMBL:CCF32112.1};
RA   Ma L.-J., O'Connell R., van Themaat E.V.L., Stueber K., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A.,
RA   Gujja S., Hansen M., Heiman D., Howarth C., Larimer J., Lui A.,
RA   MacDonald P.J.P., McCowen C., Montmayeur A., Murphy C., Neiman D.,
RA   Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., Stolte C.,
RA   Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The genome sequence of Colletotrichum higginsianum IMI 34906.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000007174}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMI 349063 {ECO:0000313|Proteomes:UP000007174};
RX   PubMed=22885923; DOI=10.1038/ng.2372;
RA   O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA   Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA   Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA   Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA   Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA   Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA   Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA   Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA   Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA   Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA   van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA   Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA   Ma L.-J., Vaillancourt L.J.;
RT   "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT   by genome and transcriptome analyses.";
RL   Nat. Genet. 44:1060-1065(2012).
RN   [3] {ECO:0000313|EMBL:OBR14938.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMI 349063 {ECO:0000313|EMBL:OBR14938.1};
RA   O'Connell R., Zambounis A., Thon M., Dallery J.-F.;
RT   "Resequencing and annotation of the Colletotrichum higginsianum genome.";
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|Proteomes:UP000092177}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMI 349063 {ECO:0000313|Proteomes:UP000092177};
RX   PubMed=28851275; DOI=10.1186/s12864-017-4083-x;
RA   Dallery J.-F., Lapalu N., Zampounis A., Pigne S., Luyten I., Amselem J.,
RA   Wittenberg A.H.J., Zhou S., de Queiroz M.V., Robin G.P., Auger A.,
RA   Hainaut M., Henrissat B., Kim K.-T., Lee Y.-H., Lespinet O., Schwartz D.C.,
RA   Thon M.R., O'Connell R.J.;
RT   "Gapless genome assembly of Colletotrichum higginsianum reveals chromosome
RT   structure and association of transposable elements with secondary
RT   metabolite gene clusters.";
RL   BMC Genomics 18:667-667(2017).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       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; CACQ02000324; CCF32112.1; -; Genomic_DNA.
DR   EMBL; LTAN01000001; OBR14938.1; -; Genomic_DNA.
DR   RefSeq; XP_018163455.1; XM_018295093.1.
DR   STRING; 759273.H1UVW1; -.
DR   EnsemblFungi; CCF32112; CCF32112; CH063_00758.
DR   GeneID; 28859200; -.
DR   KEGG; chig:CH63R_00118; -.
DR   VEuPathDB; FungiDB:CH63R_00118; -.
DR   eggNOG; KOG0652; Eukaryota.
DR   HOGENOM; CLU_000688_2_4_1; -.
DR   OrthoDB; 1707207at2759; -.
DR   Proteomes; UP000007174; Unassembled WGS sequence.
DR   Proteomes; UP000092177; Chromosome 1.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0008540; C:proteasome regulatory particle, base subcomplex; IEA:EnsemblFungi.
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:0045899; P:positive regulation of RNA polymerase II transcription preinitiation complex assembly; IEA:EnsemblFungi.
DR   GO; GO:0070682; P:proteasome regulatory particle assembly; IEA:EnsemblFungi.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:EnsemblFungi.
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:SF7; 26S PROTEASOME REGULATORY SUBUNIT 6A; 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:CCF32112.1};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW   Protease {ECO:0000313|EMBL:CCF32112.1};
KW   Proteasome {ECO:0000256|ARBA:ARBA00022942}.
FT   DOMAIN          241..380
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..38
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   461 AA;  51296 MW;  DA55909B06F7FFDA CRC64;
     MSTLEELDDL DRHDKNDKRD DGDKDNKDNK KPAGEGDADM KDAEEEEDIL DDEILNLSTQ
     DIQTRKRLLE NDSRIMRSEL QRLTHEKATM GEKIKENHDK IANNRQLPYL VGNVVELLDL
     DPTAESLEEG ANIDLDATRV GKSAVIKTST RQTIFLPLIG LVDPTTLKPG DLIGVNKDSY
     LILDTLPAEY DSRVKAMEVD EKPTEKYTDV GGLDKQIEEL VEAIVWPMKE AERFKKIGIK
     APKGALMYGP PGTGKTLLAR ACAAQTDATF LKLAGPQLVQ MFIGDGAKLV RDCFALAKEK
     APAIIFIDEL DAVGTKRFDS EKSGDREVQR TMLELLNQLD GFASDDRIKV LAATNRVDVL
     DPALLRSGRL DRKIEFPLPN EEARAQILKI HSRKMKVDPA VNWGELARST DEFGGAMLKA
     VCVEAGMIAL RMGKNKISHE HYVDAIAEVQ AKKKDTVNFY A
//
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