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Database: UniProt
Entry: A0A1Y1UZU9_9FUNG
LinkDB: A0A1Y1UZU9_9FUNG
Original site: A0A1Y1UZU9_9FUNG 
ID   A0A1Y1UZU9_9FUNG        Unreviewed;       929 AA.
AC   A0A1Y1UZU9;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=AAA ATPase domain-containing protein {ECO:0000313|EMBL:ORX44324.1};
GN   ORFNames=BCR36DRAFT_359793 {ECO:0000313|EMBL:ORX44324.1};
OS   Piromyces finnis.
OC   Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC   Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales;
OC   Neocallimastigaceae; Piromyces.
OX   NCBI_TaxID=1754191 {ECO:0000313|EMBL:ORX44324.1, ECO:0000313|Proteomes:UP000193719};
RN   [1] {ECO:0000313|EMBL:ORX44324.1, ECO:0000313|Proteomes:UP000193719}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=finn {ECO:0000313|Proteomes:UP000193719};
RG   DOE Joint Genome Institute;
RA   Haitjema C.H., Gilmore S.P., Henske J.K., Solomon K.V., De Groot R.,
RA   Kuo A., Mondo S.J., Salamov A.A., Labutti K., Zhao Z., Chiniquy J.,
RA   Barry K., Brewer H.M., Purvine S.O., Wright A.T., Boxma B., Van Alen T.,
RA   Hackstein J.H., Baker S.E., Grigoriev I.V., O'Malley M.A.;
RT   "Genomes of anaerobic fungi encode conserved fungal cellulosomes for
RT   biomass hydrolysis.";
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ORX44324.1, ECO:0000313|Proteomes:UP000193719}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=finn {ECO:0000313|Proteomes:UP000193719};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA   Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA   Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA   Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|RuleBase:RU004432}.
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:ORX44324.1}.
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DR   EMBL; MCFH01000046; ORX44324.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y1UZU9; -.
DR   STRING; 1754191.A0A1Y1UZU9; -.
DR   EnsemblFungi; ORX44324; ORX44324; BCR36DRAFT_359793.
DR   OrthoDB; 35211at2759; -.
DR   Proteomes; UP000193719; 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; 1.
DR   CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR036628; Clp_N_dom_sf.
DR   InterPro; IPR004176; Clp_R_dom.
DR   InterPro; IPR001270; ClpA/B.
DR   InterPro; IPR018368; ClpA/B_CS1.
DR   InterPro; IPR028299; ClpA/B_CS2.
DR   InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR   PANTHER; PTHR11638:SF18; HEAT SHOCK PROTEIN 104; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF17871; AAA_lid_9; 1.
DR   Pfam; PF02861; Clp_N; 2.
DR   Pfam; PF10431; ClpB_D2-small; 1.
DR   PRINTS; PR00300; CLPPROTEASEA.
DR   SMART; SM00382; AAA; 2.
DR   SMART; SM01086; ClpB_D2-small; 1.
DR   SUPFAM; SSF81923; Double Clp-N motif; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51903; CLP_R; 1.
DR   PROSITE; PS00870; CLPAB_1; 1.
DR   PROSITE; PS00871; CLPAB_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004432};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU004432};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193719};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          2..144
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          469..530
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   929 AA;  104593 MW;  BDD22676392CCE41 CRC64;
     MSSRYSNMAE NIILKSKELA QENSHIEIQP WHMFIALIDD EDSMLKKAIT KSGGDSLTVE
     CAIKRKIVQL PVQNPPPIEV NFSKATYTII QNAQKISSKN KDKFCTVYSL IIALIESTEI
     SSILKSSGID VNNVKEQIKK IRGNSTADSK NAEDTFDALN KYAIDMTALA EQGKFDPVIG
     RDDEIRRVIR VLTCRKKNNP CLIGEPGVGK TAIIEGLAQR IVANDIPANL KCRLYSLDMG
     ALVAGSAYRG DFEKRLKAVL NEVTTSEEPI VLFIDEIHLV LGAGKTSGSM DAANLLKPML
     ARGELRCIGA TTLAEYREYV EKDAAFERRF QQVYVGEPSV QDTITILRGL KEKFEAYAGV
     KILDSALVQA AYLSNRYITN RFLPDKAIDL IDEACAYAKV QLESQPEQID ILERKKLQLE
     IEKTALSGEK SQIAKDRLQK VEEEICQLNE KLKPLMEQYK NEKKRIDEIG TMNKKLDEIR
     NKIADAERKH DLALAADLKY YALPEVENRL KELEAKREKE LDEMIEEEDD NFNNGKMIGN
     NNEFFDNNQS GEKPKVPKEQ NERLLKEIIG ANEIADIVSK WTGIPVQRLS QGEAERFLNL
     AEHLHNRIIG QDEAVELVAE AILRSRAGLA REKAPAGSFL FLGPTGVGKT ELAKALACEL
     FDDEKYIVRI DMTEYMEKHS VSRLIGAPPG YVGYEESGQL TEAVRRRPYS IVLFDEVEKA
     HPEVINILLQ VLDDGVLTDG KGRTVDFSNT VIIMTSNLGY RPLQTLAINN RTDIDKNTRD
     LVMEEVRQTL KPELINRLDD IILFHPLSKK ELRTIITNQI KNIEKRIANQ GLLKMTINIT
     EGAQDFILSE AYDPAYGARP IRRYLEKHIV TRLSYLKIKG KLYPGCIVNI DYSSDNNNLI
     YNQVPSNDII LSSDNITTSL SSNFSDTNL
//
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