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Database: UniProt
Entry: A0A0C9SWL7_PLICR
LinkDB: A0A0C9SWL7_PLICR
Original site: A0A0C9SWL7_PLICR 
ID   A0A0C9SWL7_PLICR        Unreviewed;       865 AA.
AC   A0A0C9SWL7;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=ISWI chromatin-remodeling complex ATPase ISW2 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PLICRDRAFT_95767 {ECO:0000313|EMBL:KII83790.1};
OS   Plicaturopsis crispa FD-325 SS-3.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Amylocorticiales; Amylocorticiaceae; Plicaturopsis.
OX   NCBI_TaxID=944288 {ECO:0000313|EMBL:KII83790.1, ECO:0000313|Proteomes:UP000053263};
RN   [1] {ECO:0000313|EMBL:KII83790.1, ECO:0000313|Proteomes:UP000053263}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FD-325 SS-3 {ECO:0000313|EMBL:KII83790.1,
RC   ECO:0000313|Proteomes:UP000053263};
RG   DOE Joint Genome Institute;
RG   Mycorrhizal Genomics Consortium;
RA   Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA   Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA   Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT   "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KN832574; KII83790.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C9SWL7; -.
DR   HOGENOM; CLU_000315_32_0_1; -.
DR   OrthoDB; 2724556at2759; -.
DR   Proteomes; UP000053263; 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   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd17919; DEXHc_Snf; 1.
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   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR10799:SF879; CHROMATIN-REMODELING COMPLEX ATPASE CHAIN ISWI; 1.
DR   PANTHER; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 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   SMART; SM00249; PHD; 2.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 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.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053263};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          77..240
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          407..571
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   865 AA;  97550 MW;  27DD6F32B02EAC4A CRC64;
     MKMDDKKAMT AEVNVKRAAV EAARKRWLVR HKHLFEPLLP SASVLFHNME AEIKASTDKA
     SYVPLHQLDE QPACIKGGVM KDYQNAILGD EMGLGKTLQT LSLFAHIKEN TKGHQDPHLI
     ICPLSVLSSW MTECGRWLPE FRTLRFHGVK DERDRLKNIK TPFDICITTY DAYIADDGWF
     KTRRWTYCVL DEGHKIKNSE TNLSHKVQGI GALYRLILTG TPVQNNLVEL WGLLHWLYPS
     IFTRTSERIF KDAFNLERGM YSLPFLTAAQ ALLGTIMIRR TKTSVELSVP PRNELTVFLP
     LTEAQRFWTY RLLTRMDTLD LEQIFAAKVE DTPQHAGRQE VLQHLQAQMD QNPKDSGSGE
     GNQWKKLMNL LMQLRKCCDH PYLLKDAEPS PFVNGEHVVA ASSKIIAIDK ILADILPKGE
     RVLIFSVSPS LILCMLELLE DFLALRGIPY AHLDGSTSRP RRALDIKLFQ QEKSPYQVFL
     ISTKAGGLGI NLTKASTVIM CDSDWNPQND LQAIARAHRI GQTKTVNVYR YVEDQMLDRI
     RRKLFLSVKV MGSDNPSNSD NSTTLRSTEL MDILRKGSSA LSREGDSGMD IARFLEAPIS
     EILDESRQRE GLRDAKMKHE LEAGEGDANE KLLADAEEEE RALLSGVAQV QTRLFEGQVV
     KRGAAKGNKE IAREWTELQK RARVDRTVVI DGIHVIASHI GEGVPAAPAK PPAKRSKKKF
     DSEDYCMYCR DGGEVVLCAR CPRVFHPRCH GMTKAEVARS ISIACSQHNC AVCNRSTADA
     GGMLFRCQTC PQAFCEDCLP NDDFDAVGDV LPEFLLLGLG QQNTAYYIRC HDCHAHFKED
     PAVWEAWQEE MKETQAKLQS LEASL
//
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