ID A0A0D6ZZF7_9AGAR Unreviewed; 1186 AA.
AC A0A0D6ZZF7;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN ORFNames=FISHEDRAFT_54489 {ECO:0000313|EMBL:KIY42928.1};
OS Fistulina hepatica ATCC 64428.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Fistulinaceae; Fistulina.
OX NCBI_TaxID=1128425 {ECO:0000313|EMBL:KIY42928.1, ECO:0000313|Proteomes:UP000054144};
RN [1] {ECO:0000313|EMBL:KIY42928.1, ECO:0000313|Proteomes:UP000054144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 64428 {ECO:0000313|EMBL:KIY42928.1,
RC ECO:0000313|Proteomes:UP000054144};
RX PubMed=25683379; DOI=10.1016/j.fgb.2015.02.002;
RA Floudas D., Held B.W., Riley R., Nagy L.G., Koehler G., Ransdell A.S.,
RA Younus H., Chow J., Chiniquy J., Lipzen A., Tritt A., Sun H., Haridas S.,
RA LaButti K., Ohm R.A., Kues U., Blanchette R.A., Grigoriev I.V., Minto R.E.,
RA Hibbett D.S.;
RT "Evolution of novel wood decay mechanisms in Agaricales revealed by the
RT genome sequences of Fistulina hepatica and Cylindrobasidium torrendii.";
RL Fungal Genet. Biol. 76:78-92(2015).
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; KN882150; KIY42928.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D6ZZF7; -.
DR OrthoDB; 57056at2759; -.
DR Proteomes; UP000054144; 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; 2.
DR Gene3D; 1.10.3380.10; Sec63 N-terminal domain-like domain; 1.
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 InterPro; IPR036390; WH_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; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF02889; Sec63; 1.
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 SUPFAM; SSF46785; Winged helix' DNA-binding domain; 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};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KIY42928.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000054144}.
FT DOMAIN 73..250
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 294..483
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 950..998
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1122..1166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 950..967
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 968..989
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1133..1153
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1186 AA; 133354 MW; 71FD734B68E73F79 CRC64;
MSNSSANQHV LNGRGQGHTP SASRTRLRPV SDLPDVYRSM FKFGVFNAVQ STCFELILET
DENVVISGTV YPLNSFYVRG LIIPAAPTGS GKTVLFELAV IRMLCASRES GQQVKSVYIA
PTKALCSERF RDWSAKFEPM GIKCCELTGD TVTFGKGAWS DAKHASVMYG EKWDSLTRNW
QQHGSILSQI RLSLIDEVHI LNESRGSTLE VVVSRMKARG TKVRFVMVSA TVPNIRDIAS
WVGRSRSRDL PATVFEFGEE FRPCKLTRHV VGIPRQKHQN DFQFARVLDY RLFETLQMYS
QNKPILIFVP TRKGVFSTAE QLMKDYRDAE TKKKQLPWTK PGRMSLNFRD KRAAELAEYG
VGMHHAGLAI DDRRMIEDLF LKKHLRVVVA TSTLAVGVNL PAHTVVVKGV HIFQNNSSVE
YSDLDLIQML GRAGRPQFAD KDGVAIILCE SELEGKYRSL IKGTTVIESS LHVNICEHIN
SEIGLGTITT VGTAKEWLRS SFLFQRVRQN PEHYAINKGE SQTWEECIDD LVLKSIAELK
NNKLITYENG NGGDFGELKS TEYGDIMSKL YIKQSTMALI LALPKKVVMR DVVFNKLRRH
NDIRYEVKKV EKTSDKVFLL IQAVLGGISL NSPDYRSGDS QPSLEAFAIW KHVIRVARAV
IEVAIVRKRG AQLKYGLDAL RCLTAKAWED RPVVLRQLSQ IGEKSKRYMG RRLQVLAEHG
INSLQSLRKQ NPLRIELLLN RKPPFGHEII ASLNEMPQYA LKLKEIEVTA SDGKKPVQVE
LNIECGLLVP RTKSNNKSPR SFDMTAILTL TSDMDFIDFR RISTRQLAEK KSYDLEFELS
KPSQSVVVYI TSERDLEGLE EMEGFWLSEE DFEDDELPSS APPVKALLDC STNGSYEVST
IPRNKVLSAA PNKASFEGHH PVRQIFCRCN HTCKDKTKCR HLCCRDGLDE PPHKRPSAAK
KDGPDRAAKQ STPSTTKKNT SSSTKKSIPV KNKIRPPDRR LAELERLHEK AGVSSNLKLP
EGKRIKLAHS GVKRKLDFDV HWSDLNNDGG QADDSGHNLK ELQDDDDEFP EPLDILNAIS
KKTKQPLSSE TTNYSDSEFD ALIRDAPDEL LESGDLISCD KKVTASTRTG KRKRPLRQND
SPRHVKPKLE PIDVIEMSDS SLSSPAVEEP EVTANKISLC FCLFSV
//
