ID A0A166PNC3_9PEZI Unreviewed; 460 AA.
AC A0A166PNC3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=26S proteasome regulatory subunit 6a (26S proteasome subunit P45 family protein) {ECO:0000313|EMBL:KZL66970.1};
GN ORFNames=CT0861_09607 {ECO:0000313|EMBL:KZL66970.1};
OS Colletotrichum tofieldiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum spaethianum species complex.
OX NCBI_TaxID=708197 {ECO:0000313|EMBL:KZL66970.1, ECO:0000313|Proteomes:UP000076552};
RN [1] {ECO:0000313|EMBL:KZL66970.1, ECO:0000313|Proteomes:UP000076552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0861 {ECO:0000313|EMBL:KZL66970.1,
RC ECO:0000313|Proteomes:UP000076552};
RA Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA O'Connell R.J.;
RT "Survival trade-offs in plant roots during colonization by closely related
RT pathogenic and mutualistic fungi.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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:KZL66970.1}.
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DR EMBL; LFIV01000157; KZL66970.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166PNC3; -.
DR STRING; 708197.A0A166PNC3; -.
DR OrthoDB; 1707207at2759; -.
DR Proteomes; UP000076552; Unassembled WGS sequence.
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 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 Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW Proteasome {ECO:0000256|ARBA:ARBA00022942, ECO:0000313|EMBL:KZL66970.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076552}.
FT DOMAIN 240..379
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 460 AA; 51132 MW; 1004DB364DE90EE9 CRC64;
MSTLEELDDL DRHDKNEKRD DGDKDKDNKK PAGDGDADMK DAEEEEDILD DEILNLSTQD
IQTRKRLLEN DSRIMRSELQ RLTHEKATMG EKIKENLDKI ANNRQLPYLV GNVVELLDLD
PTAESSEEGA NIDLDATRVG KSAVIKTSTR QTIFLPLIGL VDPTTLKPGD LIGVNKDSYL
ILDTLPAEYD SRVKAMEVDE KPTEKYTDVG GLDKQIEELV EAIVWPMKEA ERFKKIGIKA
PKGALMYGPP GTGKTLLARA CAAQTDATFL KLAGPQLVQM FIGDGAKLVR DCFALAKEKA
PAIIFIDELD AVGTKRFDSE KSGDREVQRT MLELLNQLDG FASDDRIKVL AATNRVDVLD
PALLRSGRLD RKIEFPLPNE EARAQILKIH SRKMKVDPAV NWGELARSTD EFGGAMLKAV
CVEAGMIALR MGKNKISHEH YVDAIAEVQA KKKDTVNFYA
//
