ID A0A0D1Z0E8_EXOME Unreviewed; 1540 AA.
AC A0A0D1Z0E8;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Chromodomain helicase hrp3 {ECO:0008006|Google:ProtNLM};
GN ORFNames=PV10_08001 {ECO:0000313|EMBL:KIV88307.1};
OS Exophiala mesophila (Black yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=212818 {ECO:0000313|EMBL:KIV88307.1, ECO:0000313|Proteomes:UP000054302};
RN [1] {ECO:0000313|EMBL:KIV88307.1, ECO:0000313|Proteomes:UP000054302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 40295 {ECO:0000313|EMBL:KIV88307.1,
RC ECO:0000313|Proteomes:UP000054302};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala mesophila CBS40295.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; KN847525; KIV88307.1; -; Genomic_DNA.
DR RefSeq; XP_016219881.1; XM_016372970.1.
DR STRING; 212818.A0A0D1Z0E8; -.
DR GeneID; 27325846; -.
DR VEuPathDB; FungiDB:PV10_08001; -.
DR HOGENOM; CLU_000315_29_2_1; -.
DR OMA; WVQIRDD; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000054302; 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: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};
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:UP000054302};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 281..342
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 379..439
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 477..648
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 779..941
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1047..1098
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1312..1413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1510..1540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..23
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1312..1405
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1518..1540
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1540 AA; 175730 MW; 081271AFBCB2FB9D CRC64;
METSDILAQP PPPSIPEASE PPVTPFEPAS TSKMSTVANG ATHSDSGSDL SDPAEPVAAA
ASPSQTEVDD DHQRFSEQND STPSEPPAGL DEDDEMDTSI QVPRTTSELE PSDHSSSDES
IRPAKRKAPQ AEEDDYIRSN PEMYGLRRSG RARAVPNMAE SSGEQDSDSD IAPRPRKRLR
AGTSRRSSNQ PTPVVESPSA SDGDSDAYGG RRARLSKKQR RRLLQSAESL TPAHAEVRFS
TRKAAKVSTY NEDDDDDMFD DNDPDTLTPS YWANGVEDNS PAIDIVLNHR LKPDVTTENP
SKDDYEFLIK WQQKAYYHAT WETSESLIGV KSVRRLENYI RKTLLTDIHV LTDKTIAPED
REKWILDREQ YADTLDDYKK VERVIGDRDG EEGIEYYVKW KGLFYDQATW ESSALVSEIA
QNEIDRYINR RREDFKSDTT ESNLASRSAF QPVREQPSYI QNGTLRDFQM TGLNFLAYNW
VKGKNVVLAD EMGLGKTVQT VAFLSWLRHN RGQQGPFLVA VPLSTMPAWA DTFDMWAPDL
NYVIYNGNQT ARNIIKDYEL LPDGNTRHPR FHVLLTTYEY VLHDAAFLSQ IKWQFMAVDE
AHRLKNRDSQ LYDRLREFKA PARLLITGTP VQNNLGELSA LFDFLNPGVV NIDENMDLTN
EEASAKISQL TEDIKPFMLR RTKQKVEKDL PPKSEKIIRV ELSDIQLEYY KNILTKNYAA
LNQGAKGQKQ SLLNIMMELK KASNHPFMFP SAEERLVPEG ARREEVLRAL VTSSGKMMLL
DQLLTKLKRD GHRVLIFSQM VKMLDILGDY MEYRGHAYQR LDGTIAAAPR RIAIDHFNAP
DSTDFCFLLS TRAGGLGINL MTADTVIIFD SDWNPQADLQ AMARAHRIGQ VKPVSVYRLV
SKETVEEEIL ERARNKLMLE FLTIQRGVTD KETQARRNAL VGEPGSSSEI SRILKKRGQK
MFEQTGNQKK LEELDLDAML NNAEDYKVEQ PDGTDADGGE DFLRSFDFVD VKVDELSWED
IIPKEQLENI KAEEQRKADE KYLEEVIEQN KPRVRNHQTD DRDARKTRRQ EQRQKEVDSD
SDSEEGGPKS DPSRPLSERE YRYLIKGHLR YGSIDDRTEE FLTEARLRGR DMEVVKAAMN
EVWDESLRLF KQEQQRMEDL ERSANRPLTK KDKKAVLFEL HGVKRINAET ILERPAEMRL
LQEVTSKDPD FKSFRIAEAT KHAGYTCAWG AREDGMLCVG ISRHGYGAWE KIRDDPDLGL
HDKFFLEEHR VDKKAERERL DAKNAKSPGA VHLVRRADYL LSVLKSKYAD DPAAKRAVEN
HHRNNKKLDK VRHNDSPAPR KDRRESDKHR RPASQPHRES SERYGTPRSE LRHPQRDRES
DNRDHRRHRD DHGPHNRHGS DHRRSEAATN GSAAEVDPLM VMIFKPVRES LRKIKATTKS
AIPDGQQRAN ELRVLLKQIG NFITEQVTEL EEPNESVEKR FWDYAATYWP NKGIKGSELQ
TIHGKIVASD KKLAGEGSPN DDSSNVDGRA NGSYRTSPPH
//
