ID   A0A165CJG9_9BASI        Unreviewed;      1036 AA.
AC   A0A165CJG9;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=P-loop containing nucleoside triphosphate hydrolase protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CALCODRAFT_504196 {ECO:0000313|EMBL:KZT50905.1};
OS   Calocera cornea HHB12733.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC   Dacrymycetales; Dacrymycetaceae; Calocera.
OX   NCBI_TaxID=1353952 {ECO:0000313|EMBL:KZT50905.1, ECO:0000313|Proteomes:UP000076842};
RN   [1] {ECO:0000313|EMBL:KZT50905.1, ECO:0000313|Proteomes:UP000076842}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB12733 {ECO:0000313|EMBL:KZT50905.1,
RC   ECO:0000313|Proteomes:UP000076842};
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).
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DR   EMBL; KV424137; KZT50905.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165CJG9; -.
DR   STRING; 1353952.A0A165CJG9; -.
DR   InParanoid; A0A165CJG9; -.
DR   OrthoDB; 5399336at2759; -.
DR   Proteomes; UP000076842; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR049730; SNF2/RAD54-like_C.
DR   InterPro; IPR000330; SNF2_N.
DR   PANTHER; PTHR45629:SF7; DNA EXCISION REPAIR PROTEIN ERCC-6-RELATED; 1.
DR   PANTHER; PTHR45629; SNF2/RAD54 FAMILY MEMBER; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076842}.
FT   DOMAIN          274..468
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          659..814
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          100..229
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          890..916
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        122..162
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        163..179
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        893..914
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1036 AA;  116273 MW;  BCACEEB1DFBDD883 CRC64;
     MKTSPPPPCF PLSHSPSLSP GRASGGKCSA PYANRDGPLL VCPGGGSQRL DPLSHPVLHS
     LRNYGKTLIS ALGRKAQRRE TVEDVAARAS LLALLALPPA GLPDGEDDAT DGTNTVSEGA
     EDPEDTLTRL SKETALGKRK LESDAEEDGR ETKRPKVVQE ESETEVEESE TETELEEDDE
     ERVRVMSREA GIGSRLPGTE DGESDTEPEP NAPPLPSSQS SQTPSVSLRP NFVPTAEQAL
     TGPLLLDSAT STEVPASINR FLREYQRDGV RFFWRCREEK RGGVLGDDMG LGKTIQVISF
     LAALMHRTGT SSDAGRRRKL VSKLQRRLPS SALPPADSHG PTCLIIAPVS LVDNWARELE
     TWGWFEWAKY TSQMGREERD DVRRDFVKGR LDIVLTSHDC ARNDIEQLAD LRWSVIFVDE
     AHKLKNPLSR FTQSMHQFEH GLRFGLTGTA IQNNYLELWT LLDWANPGRV GRQSQWDFYV
     SRPLLLGQSR DSTLTQKTRM ELVKRALVER LLPSMFLRRT KDIIKDQLPT KTDNVVFCKL
     MPRQAEVYKL FLAHPDVEII VKHNELCECG SKEKRGDCHK KYLSTGEVWR HGVLKYISLF
     IKLSNHVALL YPTEQDTPDQ RLRNRGYVDY ITDHFRDESE LWSAPVVQYE PALCGKWEAL
     STFLTTWKDE GDNKVLIFSK SVKLLDILQT FVQQAAYEFC RLDGKLPADK RMEEVDSFNN
     DPNIFIFLIS TLAGGTGLNL TAANKVVIFD PNWNPAHDLQ AMDRAYRIGQ NRDVTVFRLL
     GAGSLEELVY ARQLYKQAQM RIAYEGSDQR RYWAGVQGLK VKQGELFGIQ NIFSLHEAGL
     VVKSTIEKRL TEDFCWVLEN VQAEMDTEGL DIDDNEKGNQ NAVDFLLEED PATQPTPDTS
     PSFTSATNPK QKSSLKPGAE LDELLDSQKF HTHINDDVLV RSTIDAERLK AEKKAKRAKV
     SAPADGSWIP RRTRIPAKTF EDRISMLEEL GGGDPDEPLG MDMVKKIVEM SVTEQKKFLA
     KLDRQIAAKT EKASSA
//