ID A0A165D360_9BASI Unreviewed; 617 AA.
AC A0A165D360;
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};
DE Flags: Fragment;
GN ORFNames=CALCODRAFT_442266 {ECO:0000313|EMBL:KZT51976.1};
OS Calocera cornea HHB12733.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Calocera.
OX NCBI_TaxID=1353952 {ECO:0000313|EMBL:KZT51976.1, ECO:0000313|Proteomes:UP000076842};
RN [1] {ECO:0000313|EMBL:KZT51976.1, ECO:0000313|Proteomes:UP000076842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12733 {ECO:0000313|EMBL:KZT51976.1,
RC ECO:0000313|Proteomes:UP000076842};
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; KV424083; KZT51976.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165D360; -.
DR STRING; 1353952.A0A165D360; -.
DR InParanoid; A0A165D360; -.
DR OrthoDB; 3682876at2759; -.
DR Proteomes; UP000076842; 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; 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:SF136; ATP-DEPENDENT RNA HELICASE DHX35-RELATED; 1.
DR Pfam; PF21010; HA2_C; 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 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KZT51976.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076842}.
FT DOMAIN 1..144
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 172..362
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KZT51976.1"
SQ SEQUENCE 617 AA; 69118 MW; 55B55B69F3540BA8 CRC64;
QLPQYLLEAG WAREGRVIAC TQPRRISATS VAQRVAEEVG SVLGDEVGYT IRFEDLSDPD
RTRIKYLTDG MLFRECMRDP LLSKYSVIMI DEAHERSAYT DLLLGVLKKI RRKRPSLRLV
ISSATLDASY FYDYFTSTPG TTPSTASNPD EATVVAYLQE PVSDYVREAA EVVKRLHVRE
GPGDVLVFLT GREEIDRCLD MLAEWIPTCA LPFAHSQMSL VLTSRRMPKT ALALHPLPLH
AGLPAEDQQR IFDPSLPTSR KVILSTNIAE ASITIDGIRF VIDTGLVKLR SWDALTGISR
LVATPVSQAS ATQRAGRAGR TSRGVCYRLY TEEAFKGLER TTPPELIRTD LSLQVLQLKS
LGIDNLNKFE WVTPPPAENL VRALEWLVAC GALDSEGRMT QEGERMGEMA LDLKMAKCLL
ASGEFKCGEE MLTIAAVTSV QDIFIIPEGQ AGALAELERR KFTAQEGDHL TLLNGTGFNH
PSYNAFVRQG RSSSSFCRAH AMNFRALSRA MSIRAQLKKY FLRWRIPLVS CEGDQQRLRK
CLTSGYWRNA ARIMPDGTWR GVRQETVLHC HPSSVLFTRR PATGWVVFHE VEETRTTNIR
VLTEIDPDWY VLPPPPS
//
