ID A0A166ALS6_9AGAM Unreviewed; 605 AA.
AC A0A166ALS6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=SISSUDRAFT_990542 {ECO:0000313|EMBL:KZT35460.1};
OS Sistotremastrum suecicum HHB10207 ss-3.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Trechisporales; Trechisporales incertae sedis; Sistotremastrum.
OX NCBI_TaxID=1314776 {ECO:0000313|EMBL:KZT35460.1, ECO:0000313|Proteomes:UP000076798};
RN [1] {ECO:0000313|EMBL:KZT35460.1, ECO:0000313|Proteomes:UP000076798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB10207 ss-3 {ECO:0000313|EMBL:KZT35460.1,
RC ECO:0000313|Proteomes:UP000076798};
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};
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC PRP16 sub-subfamily. {ECO:0000256|ARBA:ARBA00038040}.
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DR EMBL; KV428139; KZT35460.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166ALS6; -.
DR STRING; 1314776.A0A166ALS6; -.
DR Proteomes; UP000076798; Unassembled WGS sequence.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProt.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; 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:SF91; PRE-MRNA-SPLICING FACTOR ATP-DEPENDENT RNA HELICASE PRP16; 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; 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 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KZT35460.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076798}.
FT DOMAIN 1..78
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 103..275
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 605 AA; 68072 MW; 4C63EFBBD3FDAE8F CRC64;
MTDGVLLRES LNEGDLDRYS VIILDEAHER SLSTDVLMGL LRKILSRRRD LKLIVTSATM
NADKFSTFYG NAPTFTIPGR TFPVETFHSK SPCEDYVDSA VKQVLQIHLS LPPGDILVFM
TGQEDIEITC QVVQERLSQL DDPAPLAVLP IYSQMPADLQ AKIFEATDDG RRKVIVATNI
AETSLTVDGI LYVVDAGYSK LKVYNPKVGM DALQITPISQ ANANQRKGRA GRTGNGFCYR
LYTEMAFRNE LFPNTIPEIQ RTNLANTVLL LKSLGVKNLL EFDFMDPPPQ ANILNSMYQL
WVLGALDNVG DLTPTGRKMS EFPMEPSMAK MLIVSVEYKC SAEMLTIVSM LSVPSVFYRP
KERMEEADAA REKFAVPESD HLTLLNVFTQ WKSHGFRDDW AMRHFLHPKL LRKAREVRAQ
LEDIMKFQKM DLISAGTDFD VIRKAITAGY FHQAARVKGI GEFVNIRSGL PTHLHPTSAL
YGLGYTPTYV VYHELILTSK EYMTQVTSVD AYWLAELGSV FYSVKEKSFD ERGNYRKADK
EFSKKAELEK EMAQQREMTL KKNLEAENVL SVVEAVKSGV PNTPRHIGIG AGARVTQTPR
RRAGI
//
