ID A0A090CGT2_PODAN Unreviewed; 592 AA.
AC A0A090CGT2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=AAA+ ATPase domain-containing protein {ECO:0000259|SMART:SM00382};
OS Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)
OS (Pleurage anserina).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Podosporaceae; Podospora;
OC Podospora anserina.
OX NCBI_TaxID=515849 {ECO:0000313|EMBL:CDP24642.1, ECO:0000313|Proteomes:UP000001197};
RN [1] {ECO:0000313|EMBL:CDP24642.1, ECO:0000313|Proteomes:UP000001197}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC {ECO:0000313|Proteomes:UP000001197};
RX PubMed=18460219; DOI=10.1186/gb-2008-9-5-r77;
RA Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O., Porcel B.M.,
RA Couloux A., Aury J.-M., Segurens B., Poulain J., Anthouard V.,
RA Grossetete S., Khalili H., Coppin E., Dequard-Chablat M., Picard M.,
RA Contamine V., Arnaise S., Bourdais A., Berteaux-Lecellier V., Gautheret D.,
RA de Vries R.P., Battaglia E., Coutinho P.M., Danchin E.G.J., Henrissat B.,
RA El Khoury R., Sainsard-Chanet A., Boivin A., Pinan-Lucarre B., Sellem C.H.,
RA Debuchy R., Wincker P., Weissenbach J., Silar P.;
RT "The genome sequence of the model ascomycete fungus Podospora anserina.";
RL Genome Biol. 9:R77.1-R77.22(2008).
RN [2] {ECO:0000313|Proteomes:UP000001197}
RP GENOME REANNOTATION.
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC {ECO:0000313|Proteomes:UP000001197};
RX PubMed=24558260; DOI=10.1534/genetics.113.159988;
RA Grognet P., Bidard F., Kuchly C., Tong L.C.H., Coppin E., Benkhali J.A.,
RA Couloux A., Wincker P., Debuchy R., Silar P.;
RT "Maintaining two mating types: Structure of the mating type locus and its
RT role in heterokaryosis in Podospora anserina.";
RL Genetics 197:421-432(2014).
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DR EMBL; FO904936; CDP24642.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A090CGT2; -.
DR STRING; 515849.A0A090CGT2; -.
DR eggNOG; KOG1051; Eukaryota.
DR InParanoid; A0A090CGT2; -.
DR Proteomes; UP000001197; Chromosome 1.
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; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR019489; Clp_ATPase_C.
DR InterPro; IPR001270; ClpA/B.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF18; HEAT SHOCK PROTEIN 78, MITOCHONDRIAL; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF10431; ClpB_D2-small; 1.
DR PRINTS; PR00300; CLPPROTEASEA.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000001197}.
FT DOMAIN 271..408
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 592 AA; 65532 MW; 0CC66CB58C6B3475 CRC64;
MKKNTKSTAS KKQQWDSALI LPRVEKRASD KDEDYASFSY WYSSTSGVFN LRDIVVAIQR
GDTCDRIRSL LSPHQTEFQS LKLKHEICGT VDDIPAFFFV VESGSAEMIR MWASYGGEVN
TEYREVSLLV YAMVRCLSPK ADGPVMVATL LSLGASIDSV PPPFYLPIDR DLPEAGPSDA
ELAVFKQAKT GWVLGPVRRL LTDALNSCFT LRYALHRASI TEPLSGANQA IAKKHSATGL
LGVHYFLVGQ TQACQSLVEI FMAQLALGAD RPIILLFAGP SGHGKTELAQ NMGKLLSLDL
QTVDCTNLRT SMDLFGPFFP FAGYDQSSVV NNFLDEHKSQ RSIVFLDEFE KTQPNVQEAL
LLPFQSGLYL DRRNQQIVDC SKTIWILATN AFDDTILSFC KTHYRELFTN TVGLDKRASH
QARALGKELS AMIKKEAIGK FGAPLTGRIT SVIPFLTFSP TEQAAVACKE MDRLGRKLAR
PVKLCDDLKL YRPVGNIKLQ IPFSYSVCKA LASQGYDEQL GARSIINTVD SEVALPLVTQ
YLAAREEISE DDEESCFTIT VDADLGMIEV VEKQDTLLDE VGLILNSLRG KI
//
