ID A0A2T6ZYI2_TUBBO Unreviewed; 1439 AA.
AC A0A2T6ZYI2;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 28-JAN-2026, entry version 30.
DE SubName: Full=SNF2 family N-terminal domain-domain-containing protein {ECO:0000313|EMBL:PUU80553.1};
GN ORFNames=B9Z19DRAFT_1079187 {ECO:0000313|EMBL:PUU80553.1};
OS Tuber borchii (White truffle).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Tuberaceae; Tuber.
OX NCBI_TaxID=42251 {ECO:0000313|EMBL:PUU80553.1, ECO:0000313|Proteomes:UP000244722};
RN [1] {ECO:0000313|EMBL:PUU80553.1, ECO:0000313|Proteomes:UP000244722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tbo3840 {ECO:0000313|EMBL:PUU80553.1,
RC ECO:0000313|Proteomes:UP000244722};
RG DOE Joint Genome Institute;
RA Murat C., Kuo A., Barry K.W., Clum A., Dockter R.B., Fauchery L., Iotti M.,
RA Kohler A., Labutti K., Lindquist E.A., Lipzen A., Ohm R.A., Wang M.,
RA Grigoriev I.V., Zambonelli A., Martin F.M.;
RT "Draft genome sequence of Tuber borchii Vittad., a whitish edible
RT truffle.";
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PUU80553.1}.
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DR EMBL; NESQ01000062; PUU80553.1; -; Genomic_DNA.
DR STRING; 42251.A0A2T6ZYI2; -.
DR OrthoDB; 5857104at2759; -.
DR Proteomes; UP000244722; 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:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0042393; F:histone binding; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006338; P:chromatin remodeling; IEA:UniProtKB-ARBA.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:UniProtKB-ARBA.
DR CDD; cd17996; DEXHc_SMARCA2_SMARCA4; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR FunFam; 3.40.50.10810:FF:000008; Chromatin structure-remodeling complex subunit snf21; 1.
DR FunFam; 3.40.50.300:FF:000843; Chromatin structure-remodeling complex subunit snf21; 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; IPR018359; Bromodomain_CS.
DR InterPro; IPR014978; Gln-Leu-Gln_QLQ.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C-like.
DR InterPro; IPR014012; HSA_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR029295; SnAC.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
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; PS00633; BROMODOMAIN_1; 1.
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:ARBA00022840};
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:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000244722};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 166..201
FT /note="QLQ"
FT /evidence="ECO:0000259|PROSITE:PS51666"
FT DOMAIN 392..464
FT /note="HSA"
FT /evidence="ECO:0000259|PROSITE:PS51204"
FT DOMAIN 571..736
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 883..1046
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1275..1345
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 63..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 504..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1176..1253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1364..1439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..101
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..244
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..529
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1215..1230
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1381..1391
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1412..1426
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1428..1439
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1439 AA; 163931 MW; 886ACA5A491B57B5 CRC64;
MMSSIANMPM ATQMGSLPSS LSKEQAQAVL QKWRDLKAQG ASEANHPEFA HLSSILNAMR
QQQQAYKNQM QQQQQPLNMR QMQQQQLHLQ QQQQQQRAQQ LSVSQNGAAQ LNGRSPAHPQ
QSHTNHIASS PQQRPTTDGL TSTNGVPQPS PVPSALAKNA SSPNSTFTQD QLGILRNQIM
AFKMISKNLA VPQLIQSAIF SSSVPKPDAI GSEVAAANSV VDPAAKEEIE AEKPEEDPQK
RRSGYETFTS PWASLQPKIN YHDHGSRAKR LMIPSIMPSG IDVSRLQEER ERVIFNRISA
RKAELENLPS NIGEVDSKKA STVLTDSLKL KALIEYKALC LLPKQRALRR EMVDSMIHAG
NLAVTSNRAM FRRMKKQSLR EARITEKLEK QQRDQREQRE RRKHQEYLQG VIAHGQEIKA
EARARDAKAQ KLGRMMLQHH QYMEKEEQKR MERTAKQRLL ALKANDEVAY LKLLDQAKDT
RITHLLRQTD SFLESLAASV RQQQRDAVET YGKPEGYQEP ESEDEEEDST GEKIDYYAVA
HRIKETVSEQ PTILTGGKLK DYQLKGLQWM ISLYNNNLNG ILADEMGLGK TIQTISLITY
LIERKKQNGP FLVIVPLSTL TNWNLEFEKW APGVGKIVYK GPPAVRKNQQ YDIKFSNWQV
LLTTYEYIIK DRPLLSKVKW NYMIIDEGHR MKNSQSKLSA TLTTYYNCRY RLILTGTPLQ
NNLPELWALL NFVLPTIFKS VKSFDEWFNT PFANTGGQDK MELTEEEALL VIRRLHKVLR
PFLLRRLKKD VESELPDKVE RVIKCKFSAL QQKLYQQMMN NGILYVNEPD KGGKLGVRGL
SNMIMQLRKL CNHPFVFEEV ESAINPTKVN NDALWRTAGK FELLDRLLPK FFHTGHRVLM
FFQMTQIMNI MEDFLHLRGF RYLRLDGSTK ADDRSALLKE FNAPDSPFFI FLLSTRAGGL
GLNLQTADTV IIYDSDWNPH QDLQAQDRAH RIGQKNEVRI LRLITSNSVE ERILERAQYK
LDIDGKVIQA GKFDNKSTNE ERDALLRVML EADEKEVGDS EELDDDELNE IISRNGNELT
LFRQMDIDRE KNSPYGKGKP LDRLYTEAEL PEIYLHDDLI PIEEPTGPVG RGARERKVTN
YDDGLTEEQW LDAIDNDDDT IEDAVRRKRD RIERRQVNKA RRAGELSESS PPPDSPGVED
TPPAVQPKRK RGRKPAAEKR RIEEVEELKV HPRKRQRTAK GYAPPDTVSP GNRAMLQRSC
ETIFDAVHSL EDPETERVRS EIFEKLPSKK LFPDYYHIIK QPISFNEIKK RIRNGDYLDL
DGFHGDFKLM FNNARTYNEE GSKVYEDANA MDAEFDRRYA EEKKTFDSLT NPEHSSVAGD
GTSTGPISSA GTPAAVANPT GNGTPRIRIK SRAAVAAATT AASRASPPDD DEGDSDDSE
//
