ID A0A2T3ZNZ3_9HYPO Unreviewed; 1430 AA.
AC A0A2T3ZNZ3;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=SNF2-family ATP dependent chromatin remodeling factor snf21 {ECO:0008006|Google:ProtNLM};
GN ORFNames=M441DRAFT_22534 {ECO:0000313|EMBL:PTB46526.1};
OS Trichoderma asperellum CBS 433.97.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=1042311 {ECO:0000313|EMBL:PTB46526.1, ECO:0000313|Proteomes:UP000240493};
RN [1] {ECO:0000313|EMBL:PTB46526.1, ECO:0000313|Proteomes:UP000240493}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 433.97 {ECO:0000313|EMBL:PTB46526.1,
RC ECO:0000313|Proteomes:UP000240493};
RG DOE Joint Genome Institute;
RA Aerts A., Atanasova L., Chenthamara K., Zhang J., Grujic M., Henrissat B.,
RA Kuo A., Salamov A., Lipzen A., Labutti K., Barry K., Miao Y., Rahimi M.J.,
RA Shen Q., Grigoriev I.V., Kubicek C.P., Druzhinina I.S.;
RT "Multiple horizontal gene transfer events from other fungi enriched the
RT ability of initially mycotrophic Trichoderma (Ascomycota) to feed on dead
RT plant biomass.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KZ679256; PTB46526.1; -; Genomic_DNA.
DR STRING; 1042311.A0A2T3ZNZ3; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000240493; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
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: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; IPR049730; SNF2/RAD54-like_C.
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:ARBA00022840};
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000240493}.
FT DOMAIN 151..186
FT /note="QLQ"
FT /evidence="ECO:0000259|PROSITE:PS51666"
FT DOMAIN 388..460
FT /note="HSA"
FT /evidence="ECO:0000259|PROSITE:PS51204"
FT DOMAIN 567..732
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 878..1029
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1287..1357
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 88..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 195..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1149..1252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1382..1430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1157..1179
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1180..1196
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1197..1231
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1393..1409
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1430 AA; 163014 MW; 3F2B595E07596D3F CRC64;
MASVQIPPPV QHPGAPMPAG ATKQQAEEVF RKLKQMKESG VQPNDPEYIK ASQFLLNFQQ
QHNMRRNQQQ YIQAQQQMQQ NAQAIQNGNA NGVNGTINGV QRPQHGAPQT TQGAALPNAM
GTAAAAPNQN ASGTTAPNTP AQPNSNSSSS HFTQKQLGLL RQQIHAFKLL GKNAGISVQL
QQAIFQQRQQ RQAAVMASAQ TPAATKTPQP GSDASKPTPN GVDAAAQDDA LSLPKPHTYK
TVKSPYGSSM IRPSIKYFDH AQRKNRWFIP GVFPTGIDFD HLRYEREVVV FNRMSQRYSE
LKNLPANIAH WDTTKENVEV DDSVKVKAVI EMKSLALYAK QRALREKIAR QMMHYDNLAM
TTNRTNYRRM KKQNVREARI TEKLEKQQRD ARENREKKKH NDFLRAIYNH RAEITETAAA
QKNKSHKLSR LMYSHHFNIE KEEQKRIERT AKQRLQALKA NDEEAYLKLL DQAKDTRITH
LLKQTDGFLH QLASSVKAQQ RQAAETYGTD VGEFIDEESE IDEEDSGKKI DYYAVAHRIR
EEVTQQASIL VGGTLKEYQI KGLQWMISLY NNNLNGILAD EMGLGKTIQT ISLITYLIEQ
KQQSGPYLVI VPLSTLTNWN LEFEKWAPSV SRVVYKGPPN TRKLQQEKIR QGRFQVLLTT
YEYIIKDRPI LSKIKWFHMI IDEGHRMKNT QSKLSATIQQ YYNTRFRLIL TGTPLQNNLS
ELWAMLNFVL PNIFKSVKTF DEWFNTPFAN TGGQDKMELT EEEQILVIRR LHKVLRPFLL
RRLKKDVEKD LPDKTEKVIK CKFSALQSKL YKQMVTHNKL VVSDGKGGKT GARGLSNMIM
QLRKLCNHPF VFDVVENVMN PLNISNDLLW RTAGKFELLD RILPKYKATG HRVLMFFQMT
AIMDIMEDYL RYRSYKYLRL DGTTKSDERS DLLRDFNAPD SDYFLFLLST RAGGLGLNLQ
TADTVIIYDS DWNPHQDLQA QDRAHRIGQK NEVRILRLIS SNSVEEKILE RARFKLDMDG
KVIQAGRFDN KSSETDRDAM LRTLLETADM AESGEQEEME DEELNMLLAR NDDELLTFQK
LDEERQKDGI YGGPKGKPRL MGEDELPDIY LNEGNPIEDD AEEIILGRGA RERTKVKYDD
GLTEEQWLMA VDDDEDSPEA AAARKQARKD KREANRLKRL SQMGSDNSPS VSRASTEELE
TPKKRGRKPG SKNEKRKAEE GEDEPPAKKR RGPQGRPSKS AAHGDSRLGS QQREVLQKSL
RALYDSLMNL EVDDIEPPAE DDESDAGKRL IIGPFVKLPP KREYADYYVI IQNPICMNHI
QTRIKKEEYN CLNDLRKDFD LLIRNCQTYN EDGSILYQDA KTMDEFFTKK YQEELDAHPE
LLELEPGKAG SAAPSGNGST PQPSGTRIKI ISSAAREANG ARSAAQSDED
//
