ID A0A060SAF3_PYCCI Unreviewed; 1083 AA.
AC A0A060SAF3;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=BN946_scf184909.g91 {ECO:0000313|EMBL:CDO71497.1};
OS Pycnoporus cinnabarinus (Cinnabar-red polypore) (Trametes cinnabarina).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Trametes.
OX NCBI_TaxID=5643 {ECO:0000313|EMBL:CDO71497.1, ECO:0000313|Proteomes:UP000029665};
RN [1] {ECO:0000313|EMBL:CDO71497.1, ECO:0000313|Proteomes:UP000029665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRFM137 {ECO:0000313|EMBL:CDO71497.1,
RC ECO:0000313|Proteomes:UP000029665};
RA Levasseur A., Lomascolo A., Ruiz-Duenas F.J., Uzan E., Piumi F., Kues U.,
RA Ram A.F.J., Murat C., Haon M., Benoit I., Arfi Y., Chevret D., Drula E.,
RA Kwon M.J., Gouret P., Lesage-Meessen L., Lombard V., Mariette J.,
RA Noirot C., Park J., Patyshakuliyeva A., Wieneger R.A.B., Wosten H.A.B.,
RA Martin F., Coutinho P.M., de Vries R., Martinez A.T., Klopp C.,
RA Pontarotti P., Henrissat B., Record E.;
RT "The genome of the white-rot fungus Pycnoporus cinnabarinus: a
RT basidiomycete model with a versatile arsenal for lignocellulosic biomass
RT breakdown.";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CDO71497.1}.
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DR EMBL; CCBP010000101; CDO71497.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A060SAF3; -.
DR STRING; 5643.A0A060SAF3; -.
DR HOGENOM; CLU_001832_7_0_1; -.
DR OMA; HITLMNV; -.
DR OrthoDB; 3682876at2759; -.
DR Proteomes; UP000029665; 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; 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:SF83; PRE-MRNA-SPLICING FACTOR ATP-DEPENDENT RNA HELICASE DHX16; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW mRNA splicing {ECO:0000256|ARBA:ARBA00023187};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000029665}.
FT DOMAIN 440..604
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 629..802
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 65..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 109..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1064..1083
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 278..305
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 66..87
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..214
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..248
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1083 AA; 123149 MW; 626AACA0C40F8076 CRC64;
MSDLERYISD NALRFFGLSD RSIVDYVVAC ASSAKSPEAL FVQLNASGLP DTPDAHNFAQ
EVYARVPRKS KQKKAADSAR KQAEQEAKAL RAQKFDFLLD EDGTAGGVVE VSRGANKSDR
KEKKERHLRK REGDTREWES DEEEQVRKRP RQDDEGDRSR REGEDDDMNI ELPEDEEARR
ERERLEDLKE RDAFAERIRQ RDKEKTKKVV EDRSSKASGA AAEAAERRRL ADDAEARSRA
MPSLRERSRQ EYLTKRELQQ IELLRKEIAD DEALFHGMKM TKREKRELER KKELLRLVEE
RLKINDKWEG YQLPEDYFTE QGKIDKKKKE NVLYKRYEEA KPKDGEFTTD VDQWEAAQTK
NSTFKVGALD RQEIVDDYEY VFDESQTIQF VLESTLSGEG TMSAADRLLQ QQIEEAEKRA
KTIEETRKSL PIYQYRDQLL DAIKEHQVLI VVAETGSGKT TQLPQYLHEA GYTANGMKVG
CTQPRRVAAM SVAARVAEEM GTKVGYEVGY SIRFEDCTSD KTVLKYMTDG MLLREFLTEP
DLAGYSALII DEAHERTLST DILFALVKDI ARFRPELRLL ISSATMDAEK FSEYFDNAPV
FYVPGRRYPV DIHYTPQPEA NYLHAAITTV FQIHTTQPKG DILVFLTGQD EIEAAQENLQ
ETARALGNKI KELIICPIYA NLPSEMQAKI FEPTPEGARK VVLATNIAET SITIDGVVFV
IDPGFVKQNS YNPRTGMSSL VVVPCSRASA NQRAGRAGRV GPGKAFRLYT KWAYANELEE
NTVPEIQRTN LGMVVLLLKS LGINDLIGFE FMDPPPGETL MRALELLYAL GALNDRGELT
KLGRRMAEFP VDPMLSKAII ASEQYHCTDE VLTIISMLQE SGSLFYRPKD KKLHADQARQ
NFVRAGGDHF TLLNVWEQWA ETNYSQQFCY EQFLQFKSLS RARDIRDQLA GLCERVEIVV
ESNPNTNDIT PIQKAITAGY FYNTAALQRS GDSYRTMKTN QTVYIHPSSS LFNHTPPVKA
VLYYELVMTS KSYMRQVMEI KPQWLLEVAP HYFKPADLEQ LASGDKKMPK AVGSSGAAGK
SAS
//
