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Database: UniProt
Entry: A0A165AJW7_XYLHT
LinkDB: A0A165AJW7_XYLHT
Original site: A0A165AJW7_XYLHT 
ID   A0A165AJW7_XYLHT        Unreviewed;       595 AA.
AC   A0A165AJW7;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   28-JUN-2023, entry version 27.
DE   SubName: Full=p-loop containing nucleoside triphosphate hydrolase protein {ECO:0000313|EMBL:KZF20602.1};
GN   ORFNames=L228DRAFT_240381 {ECO:0000313|EMBL:KZF20602.1};
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:KZF20602.1, ECO:0000313|Proteomes:UP000076632};
RN   [1] {ECO:0000313|EMBL:KZF20602.1, ECO:0000313|Proteomes:UP000076632}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TC161 {ECO:0000313|EMBL:KZF20602.1,
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).
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DR   EMBL; KV407462; KZF20602.1; -; Genomic_DNA.
DR   RefSeq; XP_018186157.1; XM_018331230.1.
DR   AlphaFoldDB; A0A165AJW7; -.
DR   STRING; 1328760.A0A165AJW7; -.
DR   GeneID; 28896367; -.
DR   InParanoid; A0A165AJW7; -.
DR   OrthoDB; 452393at2759; -.
DR   Proteomes; UP000076632; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR48102:SF7; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR48102; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF10431; ClpB_D2-small; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM01086; ClpB_D2-small; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:KZF20602.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076632}.
FT   DOMAIN          177..378
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          450..543
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
FT   REGION          127..153
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        127..141
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   595 AA;  64633 MW;  84938EA6574F993A CRC64;
     MATTISIPRR TLRLTSATFC ILHRRTLATT SKCASQFNRS DFSGQGFTGS YEAGLPTTGP
     LADASIYGVP RITPRMLKQH LDQFVVGQER AKRVLSVAVY NHYQRIQELQ RRDEEEEELL
     QQRLRREMGE RSGERHPVED EFPGQQPTIP IQPPQPVVPT SRLGQAPLID SSPLAIEKSN
     IMMLGPSGVG KTLMAKTLAR VLEVPFSMSD CTPFTQAGYI GEDAEVCVQR LLAAANYDVA
     RAERGIICLD EVDKIATVKV AHGKDVSGEG VQQALLKIVE GTTLQIQAKQ ERGGGRIPGG
     SGMNQNMNIP GGPGGLGGGP GGGAGAGGAG IGPTTGKGEV YNVRTDNILF IFTGAFIGLQ
     KIIMDRIAHG SIGFEQPVRA ANADSSQTTF RGEKEVLKKY LPFFDANESN QSSSQNYNPL
     DLVEPGDLQK YGLIPELVGR VPVATALSPL DEESLVRVLT EPRNCLMKQY QQLFQLSGIE
     LKFTSGALRE VAKAAIGMGT GARGLRTVME RLLADAMFEA PGSSIKFILV NQAAAQKKEA
     LIYLARGQQF KFHSLIASEE EEWERIHGKA STQESDSHYS TFEQYREKGR AAGLL
//
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