ID A0A1Q5TI65_9EURO Unreviewed; 1910 AA.
AC A0A1Q5TI65;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Protein CHROMATIN REMODELING 20 {ECO:0000313|EMBL:OKO99915.1};
GN ORFNames=PENSUB_8132 {ECO:0000313|EMBL:OKO99915.1};
OS Penicillium subrubescens.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1316194 {ECO:0000313|EMBL:OKO99915.1, ECO:0000313|Proteomes:UP000186955};
RN [1] {ECO:0000313|EMBL:OKO99915.1, ECO:0000313|Proteomes:UP000186955}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 132785 {ECO:0000313|EMBL:OKO99915.1,
RC ECO:0000313|Proteomes:UP000186955};
RA De Vries R.P., Peng M., Dilokpimol A., Hilden K., Makela M.R.,
RA Grigoriev I., Riley R., Granchi Z.;
RT "Genome sequence of the ascomycete fungus Penicillium subrubescens.";
RL Submitted (OCT-2016) 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:OKO99915.1}.
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; MNBE01000653; OKO99915.1; -; Genomic_DNA.
DR STRING; 1316194.A0A1Q5TI65; -.
DR OrthoDB; 2787289at2759; -.
DR Proteomes; UP000186955; 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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR CDD; cd18007; DEXHc_ATRX-like; 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; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR InterPro; IPR044574; ARIP4-like.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45797:SF1; HELICASE ARIP4; 1.
DR PANTHER; PTHR45797; RAD54-LIKE; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07647; SAM_2; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
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:UP000186955}.
FT DOMAIN 11..90
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 928..1129
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1304..1463
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 148..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 425..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 581..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 817..893
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1597..1619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1634..1694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1720..1831
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1863..1910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..164
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..201
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..477
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 864..885
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1634..1681
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1720..1769
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1793..1817
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1910 AA; 211586 MW; B0BFEFF6E7410283 CRC64;
MDAQSPDPVD WGVDQVVDYL CNPQEAPWAD SATSSRPNLT ALEAALRDNE INGEALLHDV
DREALRDDMG IKALGHRSSV LRAIDWLRAR SPKYQTSKQN FPSSQQPHPT EHLLSSFNSP
ITTFADSPSR ISSVPPSVLP FVLPSVPPSV PPSVPPPPAP AEMTPAPAAA GMKEKRRIAP
TPVVDLKGEK RGGDEAQKGK SPFDNRAPGL SPQPISESMA NNSTKTVRGE GSQKVSLSDP
SNANIIPPDT AELESKLSKD RSSELTQKDH DFFAELLLKH PVGGDVIPLL GESDAEYDEE
TQNEIEEDEL DSMSPISSTD CEDIFSDFIA DHEKAWMAKH LPKHRPYGQL VWNQARNPRS
GMGYKSGALR TLENLRLRLT KQKSALCDAK YKSRIALRDA CRVMETTLDQ ICFEEWRLQT
MELETCPPFV PPPPRVSRPR RQRVVEADEE SLGSDSDLAA DDEASAEESD SDFVDDDFVD
DIPHRPHKGL LGPVPADTGL VASTSDDSEE VSVAKKRRRM MESQHQSEGK INVNASKPGP
FAEFENGEMY HLSSPDHFSP SGALQLDSSP QALHDSDADM LVETPPLNPT LPASSPPDFD
MEDDFLVKTP PLNPTSLPRP SGKLRLTLPW PEAPLKVIED NALRLPKKLT SRAVSLEKDS
SDAVSPSMDD IDIFDMVSVM SWENVEASRN PVWLLAKHLI GLLPEDQKRF GPYMEELMDS
VYMEEVWAAV QAMLQNSWAM EGRTEEESRP AMRLGAYFVS WHSGKVLNPH GMGKEPLQKA
LEALEEENYL PKFLGFLHRL KKLYASFRAW LSRQPPRKEK PGYTTYSDSA DSDSNSLKRK
RHAKPRSKKP FGPRPLSNMQ KDAQERQAKQ DKDRERLRMA RESKGLSNSD PEGQAVTFKE
PVIYLHPHLG RYVKPHQLTG IQFMWRELIE ANNQQGCLLA HTMGLGKSMQ VISLLVTIAD
AAASDNPKIR EQVPERFHRS QTLVLCPSSV VPNWSDEFAM WAPADHHLGP IRLIAPRGKG
LEMSERLQTI RDWNRRGGIL IMSYEMLRIL IVNKPVRLND EEHRLVEECL LEGPNIIVAD
EAHKLRSGKS AISQVASRFK STSRIAMTGS PLSNQLFEYY QMVEWVAPGY LEDPSTFKRK
FMDPIQAGSY MDSSRMEQRE SLVSLQLLNG ILAPKVLRAD TSVLAADLPS KTEFILTVPL
TELQRNAYNT FVDCAKSKDA DASLKLWSWL AIMQLCCNHP FPFREKLADR LKQQEDTDNL
SILPTSIQDA GLPSDLVSQM DALFSKYPNL EETALSNRAV LLDEILDLSI RANDKVLIFT
QSIPTMNYLD LMLKNKGRKY QRIDGSTTGP DRQNATKRFN SDSSEQILLI STRAGGVGLN
MFGANRVVIF DFLFNPMWEE QAVGRAYRLG QRKPVYVYRF LAGGTFEELI FNNAVFKRQL
AVRVVDKKTV MRESSKKTST YLTHVKDVEK DEKYSALGRD PQVLDQILGG ELNEIILKAR
LSHIQDNEND HLTEEETRQV EYALKMERLK RSDPLAYHAE IKRREDEEKI RQQEVARILK
QRELEKAEEQ RKLFQMSQSG QQQGFMTDQQ RIASLNRGPI PMSTVGRSPL SVNNRGAADA
AGAAQPARFL SGANATPISQ DRPQLPAYQP SSSSLLPVGS NEQPVTPSAY KPSSSTLRQA
DGGEARPTFQ VPSGNEVIVI EDSSVPSTPV KAPVNALPLR SASSDHSPVS PTPNMSGDVA
QENVNQPTSV EMPPQFNQDE SQGSAEHVEN SNMDIGGDGL VDQVDKNTEE TAHNQATETN
PPAAVNQEKS DASNNGIADP KVTALRMADD DNVLKKSAKS STDIGEGSAS KMAAVGTSLI
VPATSPASGQ SEAMDTSDSS RVTVDTPASG AATCPITSSQ SEAVDISDGA
//
