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Database: UniProt
Entry: S7QMF3_GLOTA
LinkDB: S7QMF3_GLOTA
Original site: S7QMF3_GLOTA 
ID   S7QMF3_GLOTA            Unreviewed;       905 AA.
AC   S7QMF3;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=Clp R domain-containing protein {ECO:0000259|PROSITE:PS51903};
GN   ORFNames=GLOTRDRAFT_52989 {ECO:0000313|EMBL:EPQ60633.1};
OS   Gloeophyllum trabeum (strain ATCC 11539 / FP-39264 / Madison 617) (Brown
OS   rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Gloeophyllales; Gloeophyllaceae; Gloeophyllum.
OX   NCBI_TaxID=670483 {ECO:0000313|EMBL:EPQ60633.1, ECO:0000313|Proteomes:UP000030669};
RN   [1] {ECO:0000313|EMBL:EPQ60633.1, ECO:0000313|Proteomes:UP000030669}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11539 {ECO:0000313|EMBL:EPQ60633.1,
RC   ECO:0000313|Proteomes:UP000030669};
RX   PubMed=22745431; DOI=10.1126/science.1221748;
RA   Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA   Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA   Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA   Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA   Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA   Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA   Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA   Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA   Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA   Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA   Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA   Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA   Hibbett D.S.;
RT   "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT   31 fungal genomes.";
RL   Science 336:1715-1719(2012).
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|RuleBase:RU004432}.
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DR   EMBL; KB469296; EPQ60633.1; -; Genomic_DNA.
DR   RefSeq; XP_007860378.1; XM_007862187.1.
DR   AlphaFoldDB; S7QMF3; -.
DR   STRING; 670483.S7QMF3; -.
DR   GeneID; 19306910; -.
DR   KEGG; gtr:GLOTRDRAFT_52989; -.
DR   eggNOG; KOG1051; Eukaryota.
DR   HOGENOM; CLU_005070_4_2_1; -.
DR   OMA; MESEPAK; -.
DR   OrthoDB; 35211at2759; -.
DR   Proteomes; UP000030669; 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:SF194; 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|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:UP000030669};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          2..161
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          430..544
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   905 AA;  99981 MW;  4C1826DCD8C33BAA CRC64;
     MASNFEFTDK AQETLAAAIQ LAKDYANAQV HPSHIGFVLL NENAGDQTAP GGITHTSGTS
     LFSSVIQKAG GDPALVKRGL QKLIVRLPAQ SPPPEETTLS SAALKVLREA QSLQKTMHDS
     YIAQDHLILA LIKDPSIGPI LKEAGCNENT VKTAVEQARG NRRVESKTAE QGFDALNKYA
     VDLTALAEEG KIDPVIGRDN EIRRVIRILC RRTKNNPVLI GEPGVGKTSI AEGLAQRIVN
     RDVPASLIGR LFSLDMGALM AGAKYKGEYE ERIKSVLNEV EKSAEEGQTI ILFIDELHLI
     MAGRGSEGGG MDAANLFKPL LARGKLRCIG ATTLAEYRKY IETDAALERR FAQVIVNEPS
     VPETISILRG IREKYEVHHG VRIHDGALIA AAQLAHRYLT SRRLPDAAID LVDEACASVR
     VTRETAPEAI DKLQRRKLEL EVEIHALERE KDEASKERLQ IAKKAIADVD DQLRPLQAAY
     EEEKRIGDQI HEVRRRMDEL RAKADEAERR YDLATASDLR YYALPDLQNK LAQLEAKKAE
     EDARRGGGTD TVTPEQIAEI VARWTSIPVT RLMSTEKEKL LRMEKVLSES VVGQPEAVKA
     VANAIRLSRS GLRNAQRPIA SFLMAGPSGT GKTLLSKTLA TILFDSPDAM IRIDGSEYSE
     KHSIARLIGA PPGYVGYDAG GQLTEYVRRK PYCIVLIDEI EKASREFVTL FLQVLDDGRL
     TDGQGRVVDF RNTVIIMTSN LGAAYLNDMG EGPVKPATRE LVMGAIQGHF PPEFINRIDE
     IVIFRTLSRK NVLNIVDIRI KEVQDRLVDR KITLDLDDQA KEYLVSVGYS PTYGARPLNR
     AIQSELLNPL SVMILSERVR DGEIVKVRFD PAHNRLAIVP NHEGSGDVDG MDVDLEDDIE
     IEEMD
//
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