ID B8LW47_TALSN Unreviewed; 1499 AA.
AC B8LW47;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=Chromodomain helicase (Chd1), putative {ECO:0000313|EMBL:EED24075.1};
GN ORFNames=TSTA_074530 {ECO:0000313|EMBL:EED24075.1};
OS Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS 1006) (Penicillium stipitatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441959 {ECO:0000313|EMBL:EED24075.1, ECO:0000313|Proteomes:UP000001745};
RN [1] {ECO:0000313|Proteomes:UP000001745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006
RC {ECO:0000313|Proteomes:UP000001745};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; EQ962652; EED24075.1; -; Genomic_DNA.
DR RefSeq; XP_002341462.1; XM_002341421.1.
DR STRING; 441959.B8LW47; -.
DR GeneID; 8108475; -.
DR VEuPathDB; FungiDB:TSTA_074530; -.
DR eggNOG; KOG0384; Eukaryota.
DR HOGENOM; CLU_000315_29_2_1; -.
DR InParanoid; B8LW47; -.
DR OMA; WVQIRDD; -.
DR OrthoDB; 5482994at2759; -.
DR PhylomeDB; B8LW47; -.
DR Proteomes; UP000001745; 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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd18660; CD1_tandem; 1.
DR CDD; cd18659; CD2_tandem; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 2.40.50.40; -; 2.
DR Gene3D; 6.10.140.1440; -; 1.
DR Gene3D; 1.10.10.60; Homeodomain-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; IPR041150; Cdh1_DBD.
DR InterPro; IPR025260; CHD1-like_C.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR023779; Chromodomain_CS.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45623:SF14; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 1; 1.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR Pfam; PF18196; Cdh1_DBD_1; 1.
DR Pfam; PF13907; CHD1-like_C; 1.
DR Pfam; PF00385; Chromo; 2.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00298; CHROMO; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01176; DUF4208; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF54160; Chromo domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00598; CHROMO_1; 1.
DR PROSITE; PS50013; CHROMO_2; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:EED24075.1};
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:UP000001745};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 256..330
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 358..418
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 456..627
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 758..913
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1023..1077
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1295..1403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1117..1144
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..159
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1023..1058
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1311..1328
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1329..1343
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1499 AA; 171214 MW; 1D2D5A223E330320 CRC64;
MVYPSVTELS SGTEASKPLT NGYNGYDHTS SSDRASDQED LAMSDPETAT SNSSHVGTNN
HTAADDANHR AYSPTENSSY DDSDLESRRG NHSRNGSSAS SSSASSRDMK RKSPVNETDY
IRSNPELYGL RRSGRSRTER RQALVDSEDD EEPKAPRSKR RRIINSQPPS KQSSRSVTRS
SPSDSDTDEY GATSSRTARH RQLKAATVNV AAEVRFSSRN ATKVANYNED SDDMFEEDEE
DPTPNGAATT QYYSGPGIDS VLDHRLKDGV DPGISDIDVT IRDCLYYIKW QDQSHYHATW
ESSDDLKYHS GFRRLENYFK NKVKTDLYLN NDPDVAPEEK EKWNLDRERD IESLEDYKKV
ERIIGHREGP EGTEYFVKWK RLNYDSCTWE SDSLIKDIAI DELDKFLDRN DKVVTCDKRE
MQPKTRSPHV PITGSPSFLQ NGQLKDFQVK GLNFLAYNWS RNQNVVLADE MGLGKTVQTI
AFMNWLRHIR IQDGPFIVVV PLSTIPSWSE TFDYWTPDVN YVVYTGSSAA RQIIKDYELM
KDGNPRKPKF NVLLTTFEYA NMDFDFLRQF PWQFMAVDEA HRLKNRESNL YANLLDFRSP
ARLLITGTPI QNNLAELSAL MDFLNPGLVE VEVDMDLSSE AASEKLAKLQ NTLKPLMLRR
TKSKVETDLP PKTEKIIRVE LSDVQLEYYK NILTKNYAAL NEGANGQKQS LLNIMMELKK
ASNHPFMFPN AEAKLLEGNT RREDLLRIMI TSSGKMMLLD QLLAKLKRDG HRVLIFSQMV
KMLDILGDYM RFRGYQYQRL DGTISATNRR VAMEHFNAPD SSDFAFLLST RAGGLGINLM
TADTVILFDS DWNPQADLQA MARAHRIGQT KPVSVYRLVS KDTIEEEVLE RARNKLMLEF
ITIQRGLTEK DVLPGKHNRS VGEPTGTDEI SRILKRRGQK MFEQTGNQKK LEQLDIDSVL
ANAEEHKTEQ AEGLEADGGE DFLKSFEFVD VKVDEMSWDD IIPKEQLAEI KAEEKRKADE
KYLRDVIDQN RPRKRSAPND AFDEREERKA KRRARAQVNL ETADGSESES QDPKRSLKEK
ELRHLIRAFL RYGDIEEREE DVVREARLVG RDRETVKAAL QEIIDKASEL VKEDRQKLEE
MERSGKIPTK KEKKAVLFDH QGVKRINAHT IVERPEEMRI LRTATKGLTD QTSFRVPEAS
KKADYTCSWG AREDGMLCIG IVRHGYGAWP EIRDDPDLGL KDKFFLEEHR VDKKNERANA
EEKGTKSPGA VHLVRRADYL ISVLRDKSLN GHSVTARKAV DNHNRNKKLQ NNQRRQSSIS
ASPAPSSSRK ARRESEKPRQ RSQTNGPRDS IERANTPRAE PVKIKNLSAA GKVQKRVRVQ
NGVHGERSRR RSPSSTAPPA SMEDLFFEPK AHLLAKLRDV RKNNPDKDQR ASEMRRLILK
IGNYIHHLLR IDNYPGLEDR LWEHVAKTCF PPGKATLSSI KTMYERVVAN NRDTATTAR
//
