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Database: UniProt
Entry: B6QRV4_TALMQ
LinkDB: B6QRV4_TALMQ
Original site: B6QRV4_TALMQ 
ID   B6QRV4_TALMQ            Unreviewed;      1497 AA.
AC   B6QRV4;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   SubName: Full=Chromodomain helicase (Chd1), putative {ECO:0000313|EMBL:EEA20574.1};
GN   ORFNames=PMAA_044070 {ECO:0000313|EMBL:EEA20574.1};
OS   Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS   (Penicillium marneffei).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Talaromyces.
OX   NCBI_TaxID=441960 {ECO:0000313|EMBL:EEA20574.1, ECO:0000313|Proteomes:UP000001294};
RN   [1] {ECO:0000313|Proteomes:UP000001294}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18224 / CBS 334.59 / QM 7333
RC   {ECO:0000313|Proteomes:UP000001294};
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; DS995904; EEA20574.1; -; Genomic_DNA.
DR   RefSeq; XP_002151574.1; XM_002151538.1.
DR   STRING; 441960.B6QRV4; -.
DR   VEuPathDB; FungiDB:PMAA_044070; -.
DR   HOGENOM; CLU_000315_29_2_1; -.
DR   OrthoDB; 5482994at2759; -.
DR   PhylomeDB; B6QRV4; -.
DR   Proteomes; UP000001294; 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; 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; 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; PF13907; CHD1-like_C; 1.
DR   Pfam; PF00385; Chromo; 1.
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   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:EEA20574.1};
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:UP000001294};
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..206
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1024..1078
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1289..1400
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..39
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        47..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        169..201
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1024..1058
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1329..1389
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1497 AA;  170900 MW;  492C59A860F6B73F CRC64;
     MVYPSVTELS SGTDASKPLT NGYNGYDHSS SSEQASDQED QVMSDAESET SDSSHVDTNN
     SAAAGDDNNR EYSLAGNSSY DDSDLESRAG IGSRNGSSAS SSPGSSQEVK RRSAVDETDY
     IRSNPELYGL RRSGRSRTER RQTLVDSDED EEPKAPRSKR RRIVNSRPPS KEASRSVTRS
     SPSDSDTDEY GGTSTRTARR RQLQAAKVRI PAEVRFSSRN ATKVANYNED SDDMFEEDEE
     DLTPNDASTA QYYNGPGIDF VLDHRLKDGV DPNISDTDVT IRDCLYYIKW QNQSHYHATW
     ESSDSLKYHT GFRRLENYFK NKVKTDLYLN NDPDVAPEEK EKWNLDRERD IESLEDYKKV
     DRIIGHRDTL DGTEYFVKWK RLNYDACTWE SDSLVKEIAI DELDQFLDRN DKVVSCDKRE
     MQPRTRSPHV PITGSPSFLQ NGQLKDFQVK GLNFLAYNWS RNQNVVLADE MGLGKTVQTI
     AFINWLRHVR GQDGPFIVVV PLSTIPSWSE TFEYWTPDVN YIVYTGSSQA RQILKDYELM
     KDGNPRKPKF NVMLTTFEYA NMDFDFLRQF PWQFMAVDEA HRLKNRESNL YGNLLDFKAP
     ARLLITGTPI QNNLAELSAL MDFLNPGLVE VEVDMDLSSE QASEKLAKLQ NTLKPLMLRR
     TKSKVETDLP PKTEKIIRVE LSDIQLEYYK NILTKNYAAL NEGANGQKQS LLNIMMELKK
     ASNHPFMFPN AEAKLLEGNT RREDLLRIMI TSSGKMMLLD QLLAKLKRDG HRVLIFSQMV
     KMLDLLGDYM RFRGYQYQRL DGTISAANRR VAMEHFNAPE SSDFAFLLST RAGGLGINLM
     TADTVILFDS DWNPQADLQA MARAHRIGQT RPVSVYRLVS KDTIEEEVLE RARNKLMLEF
     ITIQRGLTEK DVLPGKANRA VGEPTGTDEI SRILKRRGQK MFEQTGNQKK LEQLDIDSVL
     ANAEEHKTEQ TEGLEADGGE DFLKSFEFVD VKVDEMSWDD IIPKEQLAEI KAEEKRKADE
     KYLHDVIEQN QPRKRNAPND AFDEREERKA KRRARAQVNI ETADGSESES QDPKRSLKEK
     ELRHLIRAFL RYGDVDEREE DVVREARLVG RDRDTVKAAL RAITDKAAQL VREDREKLEE
     MERSGKIPTK KEKKAVLFDH QGVKRINAHT IVERPEEMRI LRTATQGLTD QTSFRVPEAS
     KKADYTCSWG AREDGMLCIG IVRHGYGAWP EIRDDPDLGL GDKFFLEEHR VDKKNERANA
     DAKGTKSPGA VHLVRRADYL ISVLRDKSSN GHSVTARKAV ENHHRNKKLQ NIQRRQPSIS
     ASPAPSSGRK IRRESEKPRQ RSHTNGPRES TERASTPRAE PARIKNGSAT EKVHKRIQNG
     VHEDHTRPRS VSTTAPPLTM EDSIFEPKAH LLHKLRDVKK NNPDKEQRAN EMRRLILKIG
     NFIKQLLRND NYPGLEDRLW GHVAKNCFPP GKATLESIKN MYEKVVANNR DTATTAR
//
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