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Database: UniProt
Entry: A0A0D1WV44_9EURO
LinkDB: A0A0D1WV44_9EURO
Original site: A0A0D1WV44_9EURO 
ID   A0A0D1WV44_9EURO        Unreviewed;      1508 AA.
AC   A0A0D1WV44;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=Chromodomain helicase hrp3 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PV11_06608 {ECO:0000313|EMBL:KIV79016.1};
OS   Exophiala sideris.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=1016849 {ECO:0000313|EMBL:KIV79016.1, ECO:0000313|Proteomes:UP000053599};
RN   [1] {ECO:0000313|EMBL:KIV79016.1, ECO:0000313|Proteomes:UP000053599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 121828 {ECO:0000313|EMBL:KIV79016.1,
RC   ECO:0000313|Proteomes:UP000053599};
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 sideris CBS121828.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; KN846953; KIV79016.1; -; Genomic_DNA.
DR   HOGENOM; CLU_000315_29_2_1; -.
DR   OrthoDB; 5482994at2759; -.
DR   Proteomes; UP000053599; 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:UP000053599};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          240..310
FT                   /note="Chromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50013"
FT   DOMAIN          338..398
FT                   /note="Chromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50013"
FT   DOMAIN          436..607
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          738..896
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..178
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          391..410
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1006..1055
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1274..1385
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1478..1508
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        37..57
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        61..75
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        76..138
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        145..159
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1274..1288
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1301..1373
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1492..1508
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1508 AA;  173208 MW;  1458710E162DF07E CRC64;
     MQNGTKYSDS ESELSDPREP VAAGASPPRV KVVDDDENMQ DLDEPSSDEP DAEGDADFEM
     DTSTRINNVK SEDNNSSSDE SIRPAKRKAH AVEEDDYIRN NPEMYGLRRS GRARHAANMA
     ETSDEQDSDS DIAPRPRKRL RQVSQRSSKQ ATPVIESFSG SDGDSDAYGG KRAKLTKKQR
     RRLLQSAESL TPAHAEIRFS TRRAAKISSY NEDEEDDFEE NDPDTLTPNY WVNEQEDNSP
     AIDVVLNHRL RADVTTPRPS KDDYEFLIKW QQRAHYHATW ETTESLQGVR SFRRLENYIN
     RKLMEDIRMR NDLDVAPEDR EKYVLDREQY ADSLEEHKQV ERIIGDRDGP DGTEYFLKWK
     GLYYDAATWE PSSLASEIAQ NEIDRYINRQ RDDFKSDATE SNPSSRRPFI PMREQPSYIQ
     NGTLKDFQLQ GLNFLAFNWS RAKNVVLADE MGLGKTVQTV AFLSWLRHDR GQQGPFLVTV
     PLSTMPAWAE TFDHWAPDVN YVVYNGKQTA RNIIRDYELI PDGNVRHPRF HVLLTTYEYV
     LHDAPFLSQL KWQFMAVDEA HRLKNRESQL YDRLREFKAP ARLLITGTPV QNNLGELSAL
     FDFLSPGVVN IDENMDLTTE EASAKIAQLT EDIKPYMLRR TKNKVEKDLP PKTEKIIRVE
     LSDIQLEYYK NILTKNYAAL NQGAKGQKQS LLNIMMELKK ASNHPFMFPS AEERLVPDGA
     RRDEVLRALV TSSGKMMLID QLLTKLKRDG HRVLIFSQMV KMLDILGDYM EYRGHAYQRL
     DGTIGAAQRR IAIDHFNAPE SSDFCFLLST RAGGLGINLM TADTVIIFDS DWNPQADLQA
     MARAHRIGQV RPVSVYRLVS KETVEEEILE RARNKLMLEF LTIQRGVTDK ETQARRSALV
     GEPGSSSEIS RILKKRGQKM FEQTDNQKKL EELDLDAVLN SAEDYKVEQP ENTDADGGED
     FLRSFDFVDV KVDDMSWDDI IPKEHLDQLK AEEQRKAEEK YLADVIEQNK PRVRNHQVDD
     RETRKARRSE QRQKEIDSDS EEEENPKADP ARPLSEREYR YLIKGHLRYG SIEDRPEEFL
     AEARLRGRDL DVVKAAMKEV WDKSAELYRA EQDRMAELER TANRPITKKD RKAVLFELHG
     VKRINAETIL DRPAEMRLIA EITSKEPDFK AFRIPEATKA AGYTCPWGAR EDGMLCIGIS
     RHGYGAWEKI RDDPDLGLQD KFFLEEHRVD KKAERERLDD KNAKSPGAVH LVRRADYLIS
     VLKSKYVDDP AAKRAVENHH RNNKKSMADR GSAADSPAPG SHRKTPRESE KPRHRPSQAH
     RDSSERYGTP RSDSRHGHVR HDRDSRDDRD RKHRDDHSHA PHHNRHSSDH RRSDNPANNS
     PADVDPLMVM LFKPVKESLK KIKATTKSAI PDSQQRANEL RILLKVIGNF ITEQVTELDD
     NHDSVEKRFW DYAATYWPNK GIKGRELQTI HGKIVASDNK LAGEGSPDDD TNNVDSRANG
     SYQTSPPR
//
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