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
//