ID G0S9A8_CHATD Unreviewed; 668 AA.
AC G0S9A8;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=AAA+ ATPase domain-containing protein {ECO:0000259|SMART:SM00382};
GN ORFNames=CTHT_0045160 {ECO:0000313|EMBL:EGS20019.1};
OS Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
OS (Thermochaetoides thermophila).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Thermochaetoides.
OX NCBI_TaxID=759272 {ECO:0000313|Proteomes:UP000008066};
RN [1] {ECO:0000313|EMBL:EGS20019.1, ECO:0000313|Proteomes:UP000008066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1495 / CBS 144.50 / IMI 039719
RC {ECO:0000313|Proteomes:UP000008066};
RX PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA Arumugam M., Bork P., Hurt E.;
RT "Insight into structure and assembly of the nuclear pore complex by
RT utilizing the genome of a eukaryotic thermophile.";
RL Cell 146:277-289(2011).
CC -!- SIMILARITY: Belongs to the AFG1 ATPase family.
CC {ECO:0000256|ARBA:ARBA00010322}.
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DR EMBL; GL988043; EGS20019.1; -; Genomic_DNA.
DR RefSeq; XP_006694904.1; XM_006694841.1.
DR AlphaFoldDB; G0S9A8; -.
DR GeneID; 18258554; -.
DR KEGG; cthr:CTHT_0045160; -.
DR eggNOG; KOG2383; Eukaryota.
DR HOGENOM; CLU_008681_7_0_1; -.
DR OMA; WMAKKLV; -.
DR OrthoDB; 1617at2759; -.
DR Proteomes; UP000008066; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR005654; ATPase_AFG1-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR12169:SF2; AFG1P; 1.
DR PANTHER; PTHR12169; ATPASE N2B; 1.
DR Pfam; PF03969; AFG1_ATPase; 2.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
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:UP000008066}.
FT DOMAIN 130..278
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 332..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..356
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 668 AA; 74114 MW; D2FCB8D2C3062D4D CRC64;
MKRAATTSSL TITDPFIKYT TLVAQGTYLP DAAQYRLAHH LQKVYLRLKD YKPSPEYRRR
LRQLSRALDA HEAHVRNTAN LASASHPIRR NPLFARFFQQ DDGNGQALGR ESLALARVLT
SHQAALAIDS PKGLFVSGEV GTGKSMLLDL LADGLPTRHK KRWHFNTFML HTLSKLEHYR
RTYASHGSGS GAEYSLLWLA RELVETSPIL FLDEFQLPDR AASKIMSHLF IAFFQLGGVL
VASSNRMPEE LEKATGGAFV PPATGGLVER VFALGRRLAG WGELYGASSD FAAFLEVLRA
RCEFWHVEGT RDFRRREEEV VNVVSGGGQF DSLDGGSLLT GTAELPSQNE PPSDTATHPA
MYTLTSSPSD TWSSLVLAAA GVPPPSHSPT SWTPDSHTVY GRLLPVPHTH NGVAYFRFPD
LVSTLGPADY ITLACNYHTF IIDDVPVLPL SMKNEARRFI TLLDALYEAR CKLLIRAAAG
PDEIFFPETR RPRPSQSPDG TSEEGDATYA ETLSEVYQDL VSPFRPNTSS TYVPSAPEPS
LTSPSTTPQI DFLSSTKTFT GEDERFAYKR ATSRLWELCS IRWHGNPTEQ WWMPLPTEAR
HWEGGEVSRP LQDAKDVMVR AAGKGEGFVG ERVLEGPMGL SKYVVERLKK EEVEQVGEEG
SCDKEEGR
//
