ID A0A0A2L9J7_PENIT Unreviewed; 390 AA.
AC A0A0A2L9J7;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=ATPase, AAA-type, core {ECO:0000313|EMBL:KGO76767.1};
GN ORFNames=PITC_089710 {ECO:0000313|EMBL:KGO76767.1};
OS Penicillium italicum (Blue mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO76767.1, ECO:0000313|Proteomes:UP000030104};
RN [1] {ECO:0000313|EMBL:KGO76767.1, ECO:0000313|Proteomes:UP000030104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHI-1 {ECO:0000313|EMBL:KGO76767.1,
RC ECO:0000313|Proteomes:UP000030104};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
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:KGO76767.1}.
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DR EMBL; JQGA01000238; KGO76767.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2L9J7; -.
DR STRING; 40296.A0A0A2L9J7; -.
DR HOGENOM; CLU_000688_2_2_1; -.
DR OMA; DHEPCVI; -.
DR OrthoDB; 360215at2759; -.
DR PhylomeDB; A0A0A2L9J7; -.
DR Proteomes; UP000030104; Unassembled WGS sequence.
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:SF155; 26S PROTEASOME REGULATORY SUBUNIT 10B; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW Proteasome {ECO:0000256|ARBA:ARBA00022942};
KW Reference proteome {ECO:0000313|Proteomes:UP000030104}.
FT DOMAIN 167..306
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT COILED 20..54
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 390 AA; 43803 MW; F48C6B2A4A7BC9AF CRC64;
MSDPERGQAL EDYKKSLLEL REWEAKLKTL RLGIKDLQRE FDVSEDNIKA LQSVGQIIGE
VLKQLDEERF IVKASSGPRY VVGCRSKVDK SKMKQGTRVA LDMTTLTIMR MLPREVDPMV
YNMSLEDPGS VNFAGIGGLN DQIRELREVI ELPLKNPELF LRVGIKPPKG VLLYGPPGTG
KTLLARAVAS SMETNFLKVV SSAIVDKYIG ESARLIREMF GYAKEHEPCI IFMDEIDAIG
GRRFSEGTSA DREIQRTLME LLNQLDGFDY LGKTKIIMAT NRPDTLDPAL LRAGRLDRKI
EIPLPNEVGR LEILKIHTST VQQEGEIDFE SVVKMSDGLN GADLRNVVTE AGLFAIKDYR
DAINQDDFNK AVRKVAEAKK LEGKLEYQKL
//
