ID V2WPV3_MONRO Unreviewed; 897 AA.
AC V2WPV3;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE SubName: Full=Heat shock protein hsp98 {ECO:0000313|EMBL:ESK88873.1};
GN ORFNames=Moror_13235 {ECO:0000313|EMBL:ESK88873.1};
OS Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS (Crinipellis roreri).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK88873.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK88873.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK88873.1,
RC ECO:0000313|Proteomes:UP000017559};
RX PubMed=24571091; DOI=10.1186/1471-2164-15-164;
RA Meinhardt L.W., Costa G.G.L., Thomazella D.P.T., Teixeira P.J.P.L.,
RA Carazzolle M.F., Schuster S.C., Carlson J.E., Guiltinan M.J.,
RA Mieczkowski P., Farmer A., Ramaraj T., Crozier J., Davis R.E., Shao J.,
RA Melnick R.L., Pereira G.A.G., Bailey B.A.;
RT "Genome and secretome analysis of the hemibiotrophic fungal pathogen,
RT Moniliophthora roreri, which causes frosty pod rot disease of cacao:
RT mechanisms of the biotrophic and necrotrophic phases.";
RL BMC Genomics 15:164-164(2014).
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:ESK88873.1}.
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DR EMBL; AWSO01000612; ESK88873.1; -; Genomic_DNA.
DR RefSeq; XP_007851783.1; XM_007853592.1.
DR AlphaFoldDB; V2WPV3; -.
DR STRING; 1381753.V2WPV3; -.
DR KEGG; mrr:Moror_13235; -.
DR HOGENOM; CLU_005070_4_0_1; -.
DR OrthoDB; 35211at2759; -.
DR Proteomes; UP000017559; 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:UP000017559};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000313|EMBL:ESK88873.1}.
FT DOMAIN 1..153
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 423..510
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 897 AA; 99154 MW; 0BC7C0EB44A15B66 CRC64;
MTSNFDFTDK TQQSLAAAIQ LAKDYANAQV HPAHIAFALL NEGAGEGTSG SSLFASVIQK
AGGDPQSIKR GLQKLIVRLP TQSPPPDETS LSSAALKVLR EAQSIQKNMH DSYIAQDHIL
LALIKESSIQ PVLKENGLTE GTLKTAVEQI RGNRRVESKN AEEGFDALNK YAVDLTALAE
EGKIDPVIGR DNEIRRTIRI LCRRTKNNPV LIGEPGVGKT SIAEGLAQRI VKRDVPASLF
CRLFSLDMGA LMAGAKYKGE YEERIKSVLN EVEKAAEDGG PGVILFIDEL HLIMAGRGSE
GGGMDAANLF KPLLARGKLR CIGATTLAEY RKYIETDAAL ERRFAQVIVN EPTVPETISI
LRGIREKYEV HHGVKILDPA LISAAQLAHR YLTSRRLPDA AIDLVDEACA SVRVTRETEP
EAIDKLQRKK LELEVEIHAL EREKDEASKE RLKLARKAIA AVDDELRPLK AAYENEKKIG
DEVNSVRKKI DELKAKAEDA ERKYDLATAS DLKYFAIPDL QARLAELEKK EAEHDEGSGA
NLVTPEQIAE IVARWTSIPV TRLMSSEKEK LLRMEKILSE SVVGQTEAVK AVANAIRLSR
SGLSNPQRPI ASFLMAGPSG TGKTLMAKTL ATLLFDSPDA MIRIDGSEYS EKHAIARLIG
APPGYVGHDQ GGQLTEYIRR KPYSIVLIDE IEKASREFVT LFLQVLDDGR LTDGQGRIVD
FRNTVIIMTS NLGAAYLNDM PEGPVRAETR QLVLGAIQAH FPPEFVNRVD EIIVFRPLSR
KHVLKIVDIR LQEVEARLSE RKITLDIDDA AKGYLSSVGY SPVYGARPLN RAIQQELLNP
LSVMILSDRI RDDEVVRVRF DGPHNRLMIL PNHEGVPGED YMDIDADDDE IEIEEMD
//