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Database: UniProt
Entry: A0A0N7LAW4_9BASI
LinkDB: A0A0N7LAW4_9BASI
Original site: A0A0N7LAW4_9BASI 
ID   A0A0N7LAW4_9BASI        Unreviewed;      1085 AA.
AC   A0A0N7LAW4;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE            EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
OS   Ceraceosorus bombacis.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Exobasidiomycetes; Ceraceosorales; Ceraceosoraceae; Ceraceosorus.
OX   NCBI_TaxID=401625 {ECO:0000313|EMBL:CEH17714.1, ECO:0000313|Proteomes:UP000054845};
RN   [1] {ECO:0000313|EMBL:CEH17714.1, ECO:0000313|Proteomes:UP000054845}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Magalhaes I.L.F., Oliveira U., Santos F.R., Vidigal T.H.D.A.,
RA   Brescovit A.D., Santos A.J.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC         Evidence={ECO:0000256|ARBA:ARBA00001665};
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DR   EMBL; CCYA01000265; CEH17714.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N7LAW4; -.
DR   STRING; 401625.A0A0N7LAW4; -.
DR   OrthoDB; 57056at2759; -.
DR   Proteomes; UP000054845; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   CDD; cd18795; SF2_C_Ski2; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR   Gene3D; 1.10.3380.10; Sec63 N-terminal domain-like domain; 2.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR004179; Sec63-dom.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   PANTHER; PTHR47835; HFM1, ATP DEPENDENT DNA HELICASE HOMOLOG; 1.
DR   PANTHER; PTHR47835:SF2; SEC63 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00270; DEAD; 2.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF02889; Sec63; 2.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00973; Sec63; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   SUPFAM; SSF158702; Sec63 N-terminal domain-like; 1.
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:CEH17714.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054845}.
FT   DOMAIN          207..301
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          353..545
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          19..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1000..1085
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..40
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1001..1026
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1027..1043
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1070..1085
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1085 AA;  119411 MW;  1D6057325BD7C6A7 CRC64;
     MDDDNALYQS VEALLRPAEE DYSHQSTQPA TQQHTRNFDL ESGSAGGAPP HRAPLYFMNE
     HGGLQPAQQA PLRALTHVWS HPQPECMDEL PQRSSPTPAF VFGAGPSIDP ANLASTGFVE
     PHFEHSPRQH SIAGSGPKTH VVHARQRHGV QLQPVSILPD IFRPLFQFPA FNAVQSTVFD
     TMLKSDDNCV VTAPTGAGKT AIFEFAIIRM LQNHGVNAKA VYVAPTKALW QEGRAIFDKV
     KVLMIDEVHI LRERQRGARV EVLVSRMKTY GDNVRIVALS ATIPNASDIA QWLGSSGGSS
     KNGIELSDAT VPSAAKLFEF GEEFRPCPLK KYIYAYPNPT GDLWSFNHTL NSKLLPMITE
     HARRRPALIF VATRKMTVQA AEAIAKEFKI LEERGQVTPW SRPSANQLSS YIDPQLHDLA
     RVGIAVHHAG LDQQDRQAVE RDFRSGSIGA LCATSTLAVG VNLPAYLVIV KGTKKYDGSK
     MVDLTDFDLL QAIGRAGRPN YDREGVACIL TEERERKRIS ELVQGGTNVE SVLHHELIEH
     VNAELTLRER TEESAIQEWL ESMFLFVRMQ KNPSHYAVAG VTSAQAAFSE VKAAILSNAL
     DKLQEHGFIS REATSDCSGL ICSTDLGNIL SKYYLGLDTL HRLTRVPRNA KTGDILEAIC
     QAEEWKELRF GSGEKAAWTK VKGHEAIRFP PAKITTAADK VTLIIQVRQK QGFWLLNFFY
     VASSRLSVLQ ATLAGVTIAE AMECDKGERN HSFQDVHYVF ERAPRILKAL LDVALLNADG
     GTVKSAFELL RSVSGRAWDG TWATLRQLEG IGDKSARILA DARLTDLTSV MDCTPDRIEV
     LLNRKPPFGK KVIESAKALP RFAVHIELQE QSLKAVPGRG VCGSVSATVE QQQKECKGRR
     FGHTMFVVCL ALTSDNELVD FRKMPVSKMS KAKTYSFRVT FTKPSQSLIL IVGCSEVSGT
     AVRADVRPQG FSPQDFPGPA LLYGDSPCED PTADELMAET ASGARSSTTS AGDARSLPTL
     NTADCSRHTV QRKEEHTHEK MPNGNYKCNH QCKKESGSQL KAKSAGGHRP SSELQKKGKA
     GERRH
//
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