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Database: UniProt
Entry: V5G3M0_BYSSN
LinkDB: V5G3M0_BYSSN
Original site: V5G3M0_BYSSN 
ID   V5G3M0_BYSSN            Unreviewed;      1493 AA.
AC   V5G3M0;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   SubName: Full=Chromodomain helicase {ECO:0000313|EMBL:GAD96596.1};
GN   ORFNames=PVAR5_5256 {ECO:0000313|EMBL:GAD96596.1};
OS   Byssochlamys spectabilis (strain No. 5 / NBRC 109023) (Paecilomyces
OS   variotii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Thermoascaceae; Paecilomyces.
OX   NCBI_TaxID=1356009 {ECO:0000313|EMBL:GAD96596.1, ECO:0000313|Proteomes:UP000018001};
RN   [1] {ECO:0000313|Proteomes:UP000018001}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=No. 5 / NBRC 109023 {ECO:0000313|Proteomes:UP000018001};
RX   PubMed=24407650; DOI=10.1128/genomeA.01162-13;
RA   Oka T., Ekino K., Fukuda K., Nomura Y.;
RT   "Draft genome sequence of the formaldehyde-resistant fungus Byssochlamys
RT   spectabilis No. 5 (anamorph Paecilomyces variotii No. 5) (NBRC109023).";
RL   Genome Announc. 2:E0116213-E0116213(2014).
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:GAD96596.1}.
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DR   EMBL; BAUL01000170; GAD96596.1; -; Genomic_DNA.
DR   eggNOG; KOG0384; Eukaryota.
DR   HOGENOM; CLU_000315_29_2_1; -.
DR   InParanoid; V5G3M0; -.
DR   OrthoDB; 5482994at2759; -.
DR   Proteomes; UP000018001; 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; 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   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:GAD96596.1};
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:UP000018001};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          247..310
FT                   /note="Chromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50013"
FT   DOMAIN          347..408
FT                   /note="Chromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50013"
FT   DOMAIN          446..617
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          748..906
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..223
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          399..419
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1028..1070
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1292..1396
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        24..40
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        137..153
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        154..171
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        194..213
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        402..419
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1028..1053
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1325..1391
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1493 AA;  170215 MW;  DC92D5F481C0AB6A CRC64;
     MAATPNGHSL PSTMNGAHVD RDPTMVASDS ELSDTSDDRA SSESAEEDDV ADETYDARSP
     DAVDSDGDSP MEDADEHQEH SSPENSASST SGHGRKRKSS AVDETEFMRQ NPDLYGLRRS
     GRARTTRPLA VSDSDSDDVA PRTKRRRRVV SEQSKAPSRS ATQSSFSESD SDEYGGPRAR
     ASRTRRRRLT QTASSREPTH AEVRFSTRNA SRVSNYNEDD DDDDLFEDDV EDMTQNYWVN
     AEEDDRPAVD MVLNHRFKEG VNPSESKVSR HDCEFYIKWQ GKSHYHATWE TIESLANCRS
     TRRVDNYIRK VVEEELRLIN YEDIAPEDKE KWNLDRERDA EAIEDYKKVE RVIGMRKGED
     GGTEYFVKWK RLFYDSCTWE SAELVSEIAQ REIDRYLDRS SHPPISSKTE SNPATRKPFE
     TIKSTPSFLQ NGELKEFQVK GLNFMAFNWV RNRNVVLADE MGLGKTVQTV AFINWLRHVR
     HQQGPFVVVV PLSTMPSWAE TFDNWSPDLN YVVYNGNEAA RNVIKEYELL IDGNPRRPKF
     NVLLTTYEYV LLDSSFLSQL KWQFLAVDEA HRLKNRDSQL YAKLLEFRAP ARLLITGTPI
     QNNLAELSAL MDFLNPGLVE IDADMDLNSE AASEKIAELT KAIQPYMLRR TKSKVETDLP
     PKTEKIIRVE LSDIQLEYYK NILTKNYAAL NEGSKGQKQS LLNIMMELKK ASNHPFMFPN
     AEARILEGST RREDVLRAMI TSSGKMMLLD QLLAKLKRDG HRVLIFSQMV KMLDILGDYM
     EYRGYSYQRL DGTIAAGPRR LAIEHFNAPD SNDFAFILST RAGGLGINLM TADTVVLFDS
     DWNPQADLQA MARAHRIGQT KPVSVYRLVS KDTVEEEVLE RARNKLLLEF ITIQRGVTDK
     EASEIQSKMA RGGISVGEPV ATDDISRILK RRGQRMFEQT DNQKKLEQLD IDSVLANAEL
     HQTEQAEGIQ ADGGEEFLKA FNFVDIKVDD LSWDDIIPKE QLEEIKAEEK RKADERYLAE
     VIEQNRPRKR NVPAEERDSR EERTAKRRAR AQVNYDAADM SDSNSSLDPK RPLVEKEYRH
     LLRAFLRYGA IEDREEEVVH EARLTGRDRD TVKAALREIT DKAAALVRED TQKLEALEHE
     GKIPTKKEKK AVLFDLHGVK RLNAWTIVER PGEMRMLRQL TSAVPDPKNF RIPEATKGAD
     YTCEWGARED GMLCVGIARH GYGAWAQIRD DPDLALSDKF FLEEHRVDKK SERQNGEKTT
     KSPGAVHLVR RADYLLSVLK DKLSNGTSLA AKRAVENHHR NNKKNGMRHQ HSASMSASPA
     PPSGRRGTRE HEKSRHRSQT HGIRDSMERP NTPRSDVRPR SGSDAERVRK RATNGSAEEI
     RRRKSDDNGS SSQDDMFRML FKPIRDKLKR MAAVTKENYP SKAERALQLK NLLRSVGDFI
     AKTLEGESMA SLEDRLWGYV ADKYWPNKEV GTNKIRDMYR KVAAAEKTPA NGA
//
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