ID F7VKS1_SORMK Unreviewed; 368 AA.
AC F7VKS1;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=WGS project CABT00000000 data, contig 2.1 {ECO:0000313|EMBL:CCC06098.1};
GN ORFNames=SMAC_00315 {ECO:0000313|EMBL:CCC06098.1};
OS Sordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Sordaria.
OX NCBI_TaxID=771870 {ECO:0000313|EMBL:CCC06098.1, ECO:0000313|Proteomes:UP000001881};
RN [1] {ECO:0000313|EMBL:CCC06098.1, ECO:0000313|Proteomes:UP000001881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-333 / DSM 997 / K(L3346) / K-hell
RC {ECO:0000313|Proteomes:UP000001881};
RC TISSUE=Mycelium {ECO:0000313|EMBL:CCC06098.1};
RX PubMed=20386741; DOI=10.1371/journal.pgen.1000891;
RA Nowrousian M., Stajich J., Chu M., Engh I., Espagne E., Halliday K.,
RA Kamerewerd J., Kempken F., Knab B., Kuo H.C., Osiewacz H.D., Poeggeler S.,
RA Read N., Seiler S., Smith K., Zickler D., Kueck U., Freitag M.;
RT "De novo assembly of a 40 Mb eukaryotic genome from short sequence reads:
RT Sordaria macrospora, a model organism for fungal morphogenesis.";
RL PLoS Genet. 6:E1000891-E1000891(2010).
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:CCC06098.1}.
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DR EMBL; CABT02000001; CCC06098.1; -; Genomic_DNA.
DR RefSeq; XP_003351771.1; XM_003351723.1.
DR AlphaFoldDB; F7VKS1; -.
DR STRING; 771870.F7VKS1; -.
DR GeneID; 10809359; -.
DR KEGG; smp:SMAC_00315; -.
DR VEuPathDB; FungiDB:SMAC_00315; -.
DR eggNOG; KOG0651; Eukaryota.
DR HOGENOM; CLU_000688_2_2_1; -.
DR InParanoid; F7VKS1; -.
DR OMA; DHEPCVI; -.
DR OrthoDB; 360215at2759; -.
DR Proteomes; UP000001881; 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:UP000001881}.
FT DOMAIN 145..284
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT COILED 20..54
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 368 AA; 41074 MW; 976628986B84E1A4 CRC64;
MADQERQHAL ASFKAKLIES REWEAKLKNL RLELKGLQKE YDQTEDNIKA LQSVGQIIGE
VLKQLDDERF IVKASSGPRY VVGCRSKVDK AKLKQGTLYN MSLEDPGQVS FAGIGGLNDQ
IRELREVIEL PLKNPELFLR VGIKPPKGVL LYGPPGTGKT LLARAVASSL ETNFLKVVSS
AIVDKYIGES ARLIREMFGY AKEHEPCIIF MDEIDAIGGR RFSEGTSADR EIQRTLMELL
NQLDGFDYLG KTKIIMATNR PDTLDPALLR AGRLDRKIEI PLPNEVGRLE ILKIHASGVV
IEGDIDYESV VKMSDGLNGA DLRNVVTEAG LFAIKDYRDA ISQDDFNKAV RKVAESKKLE
GKLEYQKL
//