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Database: UniProt
Entry: A0A165FPS8_9BASI
LinkDB: A0A165FPS8_9BASI
Original site: A0A165FPS8_9BASI 
ID   A0A165FPS8_9BASI        Unreviewed;      1499 AA.
AC   A0A165FPS8;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=SNF2-family ATP dependent chromatin remodeling factor snf21 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CALCODRAFT_453574 {ECO:0000313|EMBL:KZT57042.1};
OS   Calocera cornea HHB12733.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC   Dacrymycetales; Dacrymycetaceae; Calocera.
OX   NCBI_TaxID=1353952 {ECO:0000313|EMBL:KZT57042.1, ECO:0000313|Proteomes:UP000076842};
RN   [1] {ECO:0000313|EMBL:KZT57042.1, ECO:0000313|Proteomes:UP000076842}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB12733 {ECO:0000313|EMBL:KZT57042.1,
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).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; KV423969; KZT57042.1; -; Genomic_DNA.
DR   STRING; 1353952.A0A165FPS8; -.
DR   InParanoid; A0A165FPS8; -.
DR   OrthoDB; 5482994at2759; -.
DR   Proteomes; UP000076842; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0042393; F:histone binding; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd17996; DEXHc_SMARCA2_SMARCA4; 1.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 1.20.5.170; -; 1.
DR   Gene3D; 1.20.920.10; Bromodomain-like; 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; IPR001487; Bromodomain.
DR   InterPro; IPR036427; Bromodomain-like_sf.
DR   InterPro; IPR014978; Gln-Leu-Gln_QLQ.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR014012; HSA_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR029295; SnAC.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR000330; SNF2_N.
DR   PANTHER; PTHR10799:SF973; ATP-DEPENDENT HELICASE BRM; 1.
DR   PANTHER; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 1.
DR   Pfam; PF00439; Bromodomain; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF07529; HSA; 1.
DR   Pfam; PF08880; QLQ; 1.
DR   Pfam; PF14619; SnAC; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   PRINTS; PR00503; BROMODOMAIN.
DR   SMART; SM00297; BROMO; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00573; HSA; 1.
DR   SMART; SM00951; QLQ; 1.
DR   SMART; SM01314; SnAC; 1.
DR   SUPFAM; SSF47370; Bromodomain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS50014; BROMODOMAIN_2; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51204; HSA; 1.
DR   PROSITE; PS51666; QLQ; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022806};
KW   Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW   ProRule:PRU00035}; Helicase {ECO:0000256|ARBA:ARBA00022806};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022806};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076842}.
FT   DOMAIN          164..199
FT                   /note="QLQ"
FT                   /evidence="ECO:0000259|PROSITE:PS51666"
FT   DOMAIN          415..487
FT                   /note="HSA"
FT                   /evidence="ECO:0000259|PROSITE:PS51204"
FT   DOMAIN          602..767
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          916..1079
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DOMAIN          1349..1419
FT                   /note="Bromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50014"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          117..139
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          244..269
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1219..1319
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1440..1499
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1228..1266
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1278..1294
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1303..1319
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1459..1490
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1499 AA;  169451 MW;  D57A9D631488777D CRC64;
     MATIDPQQLL APPPTADGGS MASASLPAYQ PPQPQLTPQQ ALAMLTPDQL RGMVQRAKVL
     MKLQERDEEQ DQELARIKSV LQYYQQYHRA QAYQQHAYLA HQRAHAAALS APSVNGWAHK
     PAAEGDSKPH PNGTSTPAVP LDPSISAILA GPLPPEPEPN QPVIFTPTQL STLRYQIHAF
     RLLSRGLPLP PHIQLAIQRP DEALQKEEEV VAAASRTTMD RIVDSAVRAH VGAKALEGDV
     EMRDVDEEES TDPNKAGVIP FTHLKRPQHP QQRLAATKNQ RMLISPTTPA NLDPQILLAE
     RDHFVDARVT QRIRELEALP ISIGQGGGPV FKPSDITMDA DAHEDVKPTS GRLRTLIELK
     ALKLREKQRQ LRQDVIATYT RSSFINQSST RAALTKLRQQ TVRDARTTEM LEKKQRDERI
     RKSKQKQLDY LQSIVNHGRD MLAARRSAAQ ASQRFGKMVL RFHADWEKEE QRRLEKLSKD
     RLKALKNDDE EAYMKLIDTA KDTRITHLLK KTNEYLDNLT QGILAQQKAA GAVSTISDEM
     PAVSEATFGA RGFDDGEPAN DKTKAEYYAV AHRIHETVTE QPSILVGGTL KDYQLKGLQW
     MLSLYNNKLN GILADEMGLG KTIQTISLVT FLIEKKRQPG PYLVIVPLST LTNWTLEFQK
     WAPSVNTVVY KGSPPVRKQL QGQIRQGGFQ VLLTTYEYII KDRLVLSKIR WLYMIIDEGH
     RMKNTQSRLS TTLSSFYTSR YRLILTGTPL QNNLPELWAL LNFSLPHIFN SSESFTDWFS
     RPFANTGTQE KLELNEEEAL LVIRGLHKVL RPFLLRRLKK DVESELPDKT EKIIKCRMSA
     LQSRMYEWMK AHKAVLTIAG DGRARATGGK GVNNMIMQLR KICNHPFVFP AVDTDINMSR
     VDTDANIYRA AGKFELIDRM LPKLFRTGHR VLLFFQMTEI MTIFEDYCNY RHYKYLRLDG
     MTKSEDRGEA MRKFNEKDSP YSLFLLSTRA GGLGLNLQTA DTVIIFDSDW NPHADLQAQD
     RAHRIGQKKA VSVFRLITDK SVEEHMLSRA RDKLDMDGKV IQAGRFDQKT SAKEQEDLLR
     LLLEADAADD QDESVEMTND ELNEILARGD EEEEIFQQMD KELEAQDLVE WRAKGRTGPV
     ERLMTDADLP YEYLHPKAPD EAKEEDLLVG RGQRARGPVM YTDGLTDDQF LRALEEDGTD
     LAEMVEKKRL RRERKAAKKV ALASGMTADS SARETPESGL DQDSATPGIS RATSLPWTNG
     VNGTSAFPSP APGDDGTPAP RGRKRKRFDE SSPAVMDGEV EGAEEEPGAK RIKAEDAVKK
     SKKANPYRER LKKVFLQCFQ EIQDSLADDG HYRCAIFKEL PDQTMYPDYY AVILNPIAMS
     VIKRRTYAGY YKNVPQFRED WKLMFDNART YNTEESQVYE DAVELEKELN EILKKLTYGT
     DLPGAEGGTN PVEPEEPTVN GKTDMKDEEA MEVDEPPPPP PPEKKILKIK VKLKQPPAA
//
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