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Database: UniProt
Entry: A0A165NKG2_9APHY
LinkDB: A0A165NKG2_9APHY
Original site: A0A165NKG2_9APHY 
ID   A0A165NKG2_9APHY        Unreviewed;       564 AA.
AC   A0A165NKG2;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=p-loop containing nucleoside triphosphate hydrolase protein {ECO:0000313|EMBL:KZT67077.1};
GN   ORFNames=DAEQUDRAFT_767447 {ECO:0000313|EMBL:KZT67077.1};
OS   Daedalea quercina L-15889.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Daedalea.
OX   NCBI_TaxID=1314783 {ECO:0000313|EMBL:KZT67077.1, ECO:0000313|Proteomes:UP000076727};
RN   [1] {ECO:0000313|EMBL:KZT67077.1, ECO:0000313|Proteomes:UP000076727}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L-15889 {ECO:0000313|EMBL:KZT67077.1,
RC   ECO:0000313|Proteomes:UP000076727};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004167}. Mitochondrion
CC       inner membrane {ECO:0000256|ARBA:ARBA00004434}; Single-pass membrane
CC       protein {ECO:0000256|ARBA:ARBA00004434}.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family. BCS1 subfamily.
CC       {ECO:0000256|ARBA:ARBA00007448}.
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DR   EMBL; KV429080; KZT67077.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165NKG2; -.
DR   STRING; 1314783.A0A165NKG2; -.
DR   OrthoDB; 404208at2759; -.
DR   Proteomes; UP000076727; Unassembled WGS sequence.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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; IPR003960; ATPase_AAA_CS.
DR   InterPro; IPR014851; BCS1_N.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR23070:SF87; ATPASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G14760)-RELATED; 1.
DR   PANTHER; PTHR23070; BCS1 AAA-TYPE ATPASE; 1.
DR   Pfam; PF00004; AAA; 2.
DR   Pfam; PF08740; BCS1_N; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM01024; BCS1_N; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00674; AAA; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU003651};
KW   Hydrolase {ECO:0000313|EMBL:KZT67077.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00022792};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00022792};
KW   Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076727}.
FT   DOMAIN          52..226
FT                   /note="BCS1 N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01024"
FT   DOMAIN          257..419
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          334..365
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          438..502
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        334..364
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   564 AA;  63483 MW;  D350ADBB64DED56C CRC64;
     MSLSAITAAI ANATNGTASI VASNTTPSSG DFHSLVSTLL SASALRDWLK LFVVGGALET
     CRRYLFSWWD AIVEAFWITA TFDANDDAYR WVLYWLSRHP AWKEARTFEV STRTFGLDYA
     SDEDEEDSTS RPVSYLPSME NTYSIWYKRR YMTVAREEKS ENRWSTKESL ELKILARDRS
     ILQSLLDEAR ETYKAAEKKF ISIYAADTSG DWRYMTCRPK RPLSSIILDP GIKELLLNDA
     RDFLDSRKWY TDRGIPFRRG YLLYGAPGSG KTSMIQSIAG ELSLNVYIVT LSRIGMDDSS
     LNELISNMPR RCIALMEDID AAFTTGIKRD LPLDVPVKRS GNEDHDSDDE SNEKARHDDN
     KNVDTGSRVT LSGLLNALDG IGAQEGRILF ATTNNYKALD PALCRPGRMD LHVEFKLASR
     HQTESLYKCF YMPVGADDTD SAEADEGYGS RRGSIDGDET DDEDENVESS EKKPLLRTSS
     SPTRRSPTSP PPSDLPSSHL PHHDLSRSEV LALAARFADT IPEREVSMAS LQGYLMMYKT
     RAREAVENAS EWIEKERAAR RERS
//
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