ID A0A0A2JRJ0_PENEN Unreviewed; 890 AA.
AC A0A0A2JRJ0;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=ATPase, AAA-type, core {ECO:0000313|EMBL:KGO57238.1};
GN ORFNames=PEX2_002120 {ECO:0000313|EMBL:KGO57238.1};
OS Penicillium expansum (Blue mold rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=27334 {ECO:0000313|EMBL:KGO57238.1, ECO:0000313|Proteomes:UP000030143};
RN [1] {ECO:0000313|EMBL:KGO57238.1, ECO:0000313|Proteomes:UP000030143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-8 {ECO:0000313|EMBL:KGO57238.1,
RC ECO:0000313|Proteomes:UP000030143};
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 CbxX/CfxQ family.
CC {ECO:0000256|ARBA:ARBA00010378}.
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:KGO57238.1}.
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DR EMBL; JQFZ01000150; KGO57238.1; -; Genomic_DNA.
DR RefSeq; XP_016598926.1; XM_016737490.1.
DR AlphaFoldDB; A0A0A2JRJ0; -.
DR STRING; 27334.A0A0A2JRJ0; -.
DR GeneID; 27672909; -.
DR HOGENOM; CLU_006450_0_0_1; -.
DR OrthoDB; 2211448at2759; -.
DR Proteomes; UP000030143; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR CDD; cd00009; AAA; 2.
DR Gene3D; 1.10.8.60; -; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041627; AAA_lid_6.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR000641; CbxX/CfxQ.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR43392; AAA-TYPE ATPASE FAMILY PROTEIN / ANKYRIN REPEAT FAMILY PROTEIN; 1.
DR PANTHER; PTHR43392:SF2; AAA-TYPE ATPASE FAMILY PROTEIN _ ANKYRIN REPEAT FAMILY PROTEIN; 1.
DR Pfam; PF00004; AAA; 3.
DR Pfam; PF17866; AAA_lid_6; 2.
DR PRINTS; PR00819; CBXCFQXSUPER.
DR SMART; SM00382; AAA; 3.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 3.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000030143}.
FT DOMAIN 143..275
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 404..544
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 678..815
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 890 AA; 99351 MW; 96C2DCC9C4EA2572 CRC64;
MCMSQSNQPD QQVPISPALE NSEISTDPKC LFLTPEASKS SGSSLNLSTS AENLIGECGN
SLEERLTLDP MPFVPQPLVN NPFDQAPQNA DAEWRKRKQR GETSEVIDEL MNYQGMQAVK
ETFLAVKSHV DICKKQGRDP KLDRYNIVFQ GNPGTGKTTV ARLYAKLLHE IGILDCDYVK
ETSGVILAAR DTLYLKRKLK RMLFNGGVLF IDEAYQLVSP HADIQGKRAL DLILKTMEDN
IGRLVVIFTG HKEEMEAFFE HQPGLPGRIP NIDSQYHGQM KVEGGFDGLA MRIAIQRLAE
SSNSRSFGNT RTVDNLSTQI SRRQSQRLCQ MATSNPQNDP DYLLFTQDDI IGPEPLKAGN
NSAAMTHLQS LVGIDNVKKY VQSMVRLMQA NYQRELRGIK PRRLPLNQLF VGQPGTGKTT
VARLYGSILA DLGILSRGDV VLKTPADFIG DCVGKSERLT QKILDASVGK VLVIDEAYML
DPGDPGREQD RFKTGVLDTI VANIQGSPNE DRCIIMVGYE DRITDMFHHA NPGLRRRFNI
NNMCRFENYN ISQLDQILSL KMREQDLTCT PEARKVAHDI LQRASTRPSF ANASEVESCL
AQAKANFEAR LNSQELEDVL FDDTLQAHDF DKDLDRTKLD CRDLLEGEVQ ESVIQKFISY
QTRFHAAKQR GLDVGFLVPT RFIFKGPPGT GKRTTAQAMG RFFYNIELLP TDEVLQYSTV
DFVGEYVGST PPKTRKLLAK ALGKVVFIDN VDRLGAGHYE TEAVNEIVHF LNQRAHDGKI
VVILAGGNAE INSLFSKHSN LAGPFPEEME FNGLSAKTCI SLLDRKLRSK GIDIEPTLQS
AGIDCHDLKL EMLFEKMQYL SDWRNSHDGN YLANEILGKS LESMGSGNAL
//