ID A0A1V6PRR9_9EURO Unreviewed; 393 AA.
AC A0A1V6PRR9;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=AAA+ ATPase domain-containing protein {ECO:0000259|SMART:SM00382};
GN ORFNames=PENANT_c052G08868 {ECO:0000313|EMBL:OQD79407.1};
OS Penicillium antarcticum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=416450 {ECO:0000313|EMBL:OQD79407.1, ECO:0000313|Proteomes:UP000191672};
RN [1] {ECO:0000313|Proteomes:UP000191672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 31811 {ECO:0000313|Proteomes:UP000191672};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the activator 1 small subunits family.
CC {ECO:0000256|ARBA:ARBA00005378}.
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:OQD79407.1}.
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DR EMBL; MDYN01000052; OQD79407.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6PRR9; -.
DR STRING; 416450.A0A1V6PRR9; -.
DR OrthoDB; 275853at2759; -.
DR Proteomes; UP000191672; Unassembled WGS sequence.
DR GO; GO:0031391; C:Elg1 RFC-like complex; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0090618; P:DNA clamp unloading; IEA:UniProt.
DR GO; GO:0006271; P:DNA strand elongation involved in DNA replication; IEA:UniProt.
DR CDD; cd00009; AAA; 1.
DR CDD; cd18140; HLD_clamp_RFC; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 1.20.272.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR013748; Rep_factorC_C.
DR InterPro; IPR047854; RFC_lid.
DR PANTHER; PTHR11669; REPLICATION FACTOR C / DNA POLYMERASE III GAMMA-TAU SUBUNIT; 1.
DR PANTHER; PTHR11669:SF9; REPLICATION FACTOR C SUBUNIT 5; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF08542; Rep_fac_C; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF48019; post-AAA+ oligomerization domain-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000191672}.
FT DOMAIN 73..212
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 393 AA; 42959 MW; 1668BA2822AC0B90 CRC64;
MSDYEDEMDV DAPKDVQFSS DNASGKKRTA ADLPIQAQDN LPWVEKYRPN SLDDVSGHQD
ILATINRFVD TNRLPHLLLY GPPGTGKTST ILALARRIYG TKNMRQMVLE LNASDDRGID
VVREQIKTFA STKQIFSMAP QASGGQNLAG YKLIILDEAD AMTATAQMAL RRIMERYTAN
TRFCIIANYT HKLSPALLSR CTRFRFSPLK EADIRVLVDQ VIEKEGVRIQ PDAVDSLVTL
SKGDMRRALN VLQACFASSI PLPMRDAPKA PRPEPEIVTN ATIYDCIAAP HPADIQEIMT
TILSTSDVTS CLNTVQTLKA TKGLALADIL SALADQLQQL EVPAQTRITW LEGLGEIEWR
LAGGGSEAVQ TGGLVGVVRN GCEVMGDKGV VMA
//
