ID A0A165HXX4_XYLHT Unreviewed; 929 AA.
AC A0A165HXX4;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Putative heat shock protein Hsp98/Hsp104/ClpA {ECO:0000313|EMBL:KZF24080.1};
GN ORFNames=L228DRAFT_252571 {ECO:0000313|EMBL:KZF24080.1};
OS Xylona heveae (strain CBS 132557 / TC161).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Xylonomycetes;
OC Xylonales; Xylonaceae; Xylona.
OX NCBI_TaxID=1328760 {ECO:0000313|EMBL:KZF24080.1, ECO:0000313|Proteomes:UP000076632};
RN [1] {ECO:0000313|EMBL:KZF24080.1, ECO:0000313|Proteomes:UP000076632}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TC161 {ECO:0000313|EMBL:KZF24080.1,
RC ECO:0000313|Proteomes:UP000076632};
RX PubMed=26693682; DOI=10.1016/j.funbio.2015.10.002;
RA Gazis R., Kuo A., Riley R., LaButti K., Lipzen A., Lin J., Amirebrahimi M.,
RA Hesse C.N., Spatafora J.W., Henrissat B., Hainaut M., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The genome of Xylona heveae provides a window into fungal endophytism.";
RL Fungal Biol. 120:26-42(2016).
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|RuleBase:RU004432}.
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DR EMBL; KV407456; KZF24080.1; -; Genomic_DNA.
DR RefSeq; XP_018189635.1; XM_018333698.1.
DR AlphaFoldDB; A0A165HXX4; -.
DR STRING; 1328760.A0A165HXX4; -.
DR GeneID; 28898835; -.
DR InParanoid; A0A165HXX4; -.
DR OrthoDB; 35211at2759; -.
DR Proteomes; UP000076632; 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; 1.
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:UP000076632};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000313|EMBL:KZF24080.1}.
FT DOMAIN 1..166
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 895..929
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 428..549
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 899..929
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 929 AA; 103157 MW; A3AA0DB0856789D4 CRC64;
MASGLQFTDR ATKALGDAHE LATQYAHSQL LPLHLAVSLF DPPEDLSKDQ QQSVNASQAS
ASAPLFRQVV ERAHGDPQLF DRAVKKALVR LPSQDPPPET VSVSPSFSKV LRSAGELQKT
QKDSFVAVDH LITALAQDSV IQKCLSEANV PNVKLIDQAI QQIRGTKRVD SKTADAEEEN
ENLKKFTIDM TAMAREGKID PVIGREDEIR RVIRILSRRT KNNPVLIGDP GVGKTTVVEG
LASRIVNADV PANLAACRLL SLDVGSLVAG SKYRGEFEER MKGVLKEIED SKDMIVLFVD
EIHLLMGAGA SGEGGMDAAN LLKPMLARGQ LHCIGATTLA EYRKYIEKDQ AFERRFQQVL
VKEPSISETI SILRGLKEKY EVHHGVNIAD GAIVSAATLA ARYLTQRRLP DSAVDLIDEA
AAAVRVTRES QPEALDNLER RLRQLEIEIH ALDREKDEAS RTRLQEAKQE AANVAEELRP
LREKYEAEKQ RSKDVQEAKI KLDQLKVKQA EAERMRDLQT ASDLKYYAIP DVEHRIEQLE
AEKARQDAEM YARRGAGDEP LLTDVVGPDQ INEIVARWTG IPVTRLKTTE KDKLLHMEKY
LGKIVVGQKE AVTSVANAIR LQRSGLANPN QPPSFLFCGP SGTGKTLLTK ALAEFLFDDP
KAMIRFDMSE YQERHSLSRM IGAPPGYVGH DAGGQLTEAL RRRPFSILLF DEVEKAAKEV
LTVLLQLMDD GRITDGQGRV VDAKNSIVVM TSNLGAEYLS RPNGADGKID PATKELVQNT
LRNYFLPEFL NRISSIVIFN RLTKREIRSI VDVRLDEIQR RLQSNGRNVR IELTPEAKDY
LGSAGYSPAY GARPLSRLIE KEVLNRLAVL ILRGGIKDGE VAQVVLEDGK LEVLPNHSDS
ELEEDDEMVD DDDAVAELED AEPDMDLYE
//