ID A0A165EPA5_9APHY Unreviewed; 644 AA.
AC A0A165EPA5;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=LAESUDRAFT_698779 {ECO:0000313|EMBL:KZT07480.1};
OS Laetiporus sulphureus 93-53.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Laetiporus.
OX NCBI_TaxID=1314785 {ECO:0000313|EMBL:KZT07480.1, ECO:0000313|Proteomes:UP000076871};
RN [1] {ECO:0000313|EMBL:KZT07480.1, ECO:0000313|Proteomes:UP000076871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-53 {ECO:0000313|EMBL:KZT07480.1,
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).
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DR EMBL; KV427619; KZT07480.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165EPA5; -.
DR STRING; 1314785.A0A165EPA5; -.
DR InParanoid; A0A165EPA5; -.
DR OrthoDB; 227126at2759; -.
DR Proteomes; UP000076871; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR CDD; cd17961; DEADc_DDX56; 1.
DR CDD; cd18787; SF2_C_DEAD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
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 PANTHER; PTHR47959:SF13; ATP-DEPENDENT RNA HELICASE RHLE; 1.
DR PANTHER; PTHR47959; ATP-DEPENDENT RNA HELICASE RHLE-RELATED; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000076871}.
FT DOMAIN 44..228
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 254..504
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 328..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 369..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 601..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..353
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..392
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 644 AA; 72117 MW; A361C76DF0DAF40C CRC64;
MPDARLVDSK ASFASFSHIL DARLLRALAD MGFSRPTIVQ TKAIPIAFEN RDILARARTG
SGKTAAYCIP AVQKILNAKA NIPAEDASRQ ATRALILVPT RELAEQVSTQ LRGLLAYCDK
EVIVANISAG TSNQLQRTLL SDRPDIVIAT PSRALALLQS KTLSLESLDT LVIDEADLIL
SYGHDEDVRQ IFNGGYLPKV FQSFLMSATM TEDVEALKGL ALRNPAILRL EEDEDEAANL
TQYSVRCSEV DKFLLTYVIL KLKLIKGKCI LFVNDVDRCY RLKLFLEQFS IKSCVLNSEL
PLNSRYHTVQ EFNKGVYDYI IASDESTGRM EHDSEDVQEE EEEQNEDAGK NDDDEECTFA
RAEWYLDADE PSASRSSTKR KRPVESPETK KSSKSNKRKH RRKTDAEYGV SRGVDFIDVS
CVINFDLPSS ARAYTHRVGR TARAGRTGMA LSFVVPRDQW GKNKVVGGLQ SAKEDEKVFE
RIEREQAARG SQIKEYKFDM KQVEAFRYRM EDALRAVTRS AIKEARIKEL KAEILNSDKL
KAHFEDNPND LEYLRHDKSL HPTRVQPHMK HVPKYLLPRI APVPGSEQVV EAQTGNANGD
VGFVPFVKNS GRGRGRGRGR GRGGRGGSAG RGRKKSDPLK KFGR
//
