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Database: UniProt
Entry: A0A165HI79_9APHY
LinkDB: A0A165HI79_9APHY
Original site: A0A165HI79_9APHY 
ID   A0A165HI79_9APHY        Unreviewed;       708 AA.
AC   A0A165HI79;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN   ORFNames=LAESUDRAFT_641454 {ECO:0000313|EMBL:KZT11763.1};
OS   Laetiporus sulphureus 93-53.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Laetiporus.
OX   NCBI_TaxID=1314785 {ECO:0000313|EMBL:KZT11763.1, ECO:0000313|Proteomes:UP000076871};
RN   [1] {ECO:0000313|EMBL:KZT11763.1, ECO:0000313|Proteomes:UP000076871}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-53 {ECO:0000313|EMBL:KZT11763.1,
RC   ECO:0000313|Proteomes:UP000076871};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
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=3.6.4.13;
CC         Evidence={ECO:0000256|ARBA:ARBA00001556};
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DR   EMBL; KV427606; KZT11763.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165HI79; -.
DR   STRING; 1314785.A0A165HI79; -.
DR   InParanoid; A0A165HI79; -.
DR   OrthoDB; 3682876at2759; -.
DR   Proteomes; UP000076871; Unassembled WGS sequence.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProt.
DR   GO; GO:0005524; F:ATP binding; 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; cd17978; DEXHc_DHX33; 1.
DR   CDD; cd18791; SF2_C_RHA; 1.
DR   Gene3D; 1.20.120.1080; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR   InterPro; IPR048333; HA2_WH.
DR   InterPro; IPR007502; Helicase-assoc_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR   PANTHER; PTHR18934:SF118; ATP-DEPENDENT RNA HELICASE DHX33; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF21010; HA2_C; 1.
DR   Pfam; PF04408; HA2_N; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF07717; OB_NTP_bind; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00847; HA2; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 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   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KZT11763.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076871}.
FT   DOMAIN          74..252
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          274..452
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..30
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   708 AA;  77646 MW;  A2516F32D537AB4A CRC64;
     MNVSDDDLEV KKGSRVQNSS LKNAQSTPRK PSFETRKKAR VDTPGKNHAS GTKAALIMEQ
     RKDLPIASGK EALVEVILEH DVTILIGETG SGKTTQVPQY LLESGIAGQG MIAVTQPRKV
     AATSLAARVA AEQNGSVGGV VGYSVRFNEA SSDQTRIKYV TDGMLVRELL GDPLLSRYSV
     IIIDEAHERT LRTDLLITNL KSIQKKRNSP SDAKGKGSAA KMNPLKIVIM SATLDAEKFS
     RFYDNAKIVY VKGRQHPVTI FHTSAGQPDY VDSALRTFFQ IHTDQPSGDV LIFLPGQEDI
     ESLEKSIKIY ADRLPKDSPG ITTCPMYAAL PPNQQGRIFT PTPPNTRKCI LATNIAETSI
     TIPGIKYVID TGKCKEKRYI VRDAGSGFDT LLTKDITKSS AMQRAGRAGR EGSGFCFRLY
     TEEAFNAMPD SAEPEIRRCA LASSLLQLKC LGQDLEELDF MDEPDAGAIV AAALKSLYLL
     GALDSKKRLT QLGRAMAVLP LEPNLARAIV ASRELGCTLE VIDIVSVLSA SSKPFFDSVG
     DREAGLEARQ KFRHRSGDHM TILNVVRAYQ EIAKAESKNG RRKWCQKQFL NERCLLEAQD
     VKNQLREVCA RMGIDWKVSC GDQEQNVLKS LVRGLVQHAA FLQPDGSYKQ LMGPSIVKIH
     PSSSLCDKKV PAIIFDELVY TSNIYARGVS AVPRSYIAEV PVLNQKSV
//
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