ID A0A0D7BSM7_9AGAR Unreviewed; 1338 AA.
AC A0A0D7BSM7;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=p-loop containing nucleoside triphosphate hydrolase protein {ECO:0000313|EMBL:KIY73553.1};
GN ORFNames=CYLTODRAFT_341974 {ECO:0000313|EMBL:KIY73553.1};
OS Cylindrobasidium torrendii FP15055 ss-10.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Physalacriaceae;
OC Cylindrobasidium.
OX NCBI_TaxID=1314674 {ECO:0000313|EMBL:KIY73553.1, ECO:0000313|Proteomes:UP000054007};
RN [1] {ECO:0000313|EMBL:KIY73553.1, ECO:0000313|Proteomes:UP000054007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FP15055 ss-10 {ECO:0000313|EMBL:KIY73553.1,
RC ECO:0000313|Proteomes:UP000054007};
RX PubMed=25683379; DOI=10.1016/j.fgb.2015.02.002;
RA Floudas D., Held B.W., Riley R., Nagy L.G., Koehler G., Ransdell A.S.,
RA Younus H., Chow J., Chiniquy J., Lipzen A., Tritt A., Sun H., Haridas S.,
RA LaButti K., Ohm R.A., Kues U., Blanchette R.A., Grigoriev I.V., Minto R.E.,
RA Hibbett D.S.;
RT "Evolution of novel wood decay mechanisms in Agaricales revealed by the
RT genome sequences of Fistulina hepatica and Cylindrobasidium torrendii.";
RL Fungal Genet. Biol. 76:78-92(2015).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KN880435; KIY73553.1; -; Genomic_DNA.
DR STRING; 1314674.A0A0D7BSM7; -.
DR OrthoDB; 53793at2759; -.
DR Proteomes; UP000054007; Unassembled WGS sequence.
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; cd17917; DEXHc_RHA-like; 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; 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:SF145; ATP-DEPENDENT RNA HELICASE DHX29; 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; 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:0000313|EMBL:KIY73553.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000054007}.
FT DOMAIN 570..735
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 808..975
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 514..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 760..781
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 765..781
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1338 AA; 148637 MW; 4CD5F441FADD1D62 CRC64;
MPPKRGIIKT GNAGNSSKSS PLPPKKGPAQ EAAEDKPLFP PGSKYPLSLL HEICQQKGWH
KPVIDTHKQN ADWTFSVILS RVNKKGEKET VKWSPVPAEV RSSALEARHW GATYALYRFC
NDKKLYLVLP AGPREYWQKL AAEHKTAPEH QKWMYDLDPF AAKKMVQERQ LQAADKRAAA
SVAAASPATS PQSREFERCP EVKMAPDLRD LVEDAIKQAS NKYTLLDNGT LPSIGHEELR
HVDNELKTLG FKAAQARKAT DFMMVPSPMA SMLLASQGLL AACLEYLILH TPECDLPERF
LPSQNSSDAF IKAVHVGTDN LKTRWLVEKA TKEAGWPIHI VRECLQDSRI DGQWELLLAA
MAKRLLGEDA ADIFDLTQPK AEVHQLEPED IEALGAEYKS NDHVVMPLFG APIQWHILVS
PNEYPRVGFA PMYLTSSTVP AYIRLHMLSC LLQAMATETF DETGGGFCLA GMAVLDEEWS
KIEAMGPPSI SLVFQHFHRE VAEDAGQEDV VVKGKKRAQG KAHAASRDPR SDAQVKEAYT
KTRQLEKPKF AEMMATRSRL PAFKSKDEFL GMLESSRVVV VVGETGCGKT TQLPQFILDS
LIESNRGSNA NIVITQPRRI SAIGVSSRVA AERIEDGSVG YAIRGESTRT KETKLLFCTT
GVVLRRLSSG DKLGDVTHVV VDEVHERSVD GDFLLLELRE LLKINKALKV VLMSATINHE
TFIKYFGGAP LLEIPGFTHP VADKYLEDVI QSIDYRPPPA RVRTKESAAQ QQEFREGFKS
QGLSEESITA LQNLSRTDDI NYDLLGAIIR HIVTTTPERG GILIFLPGVQ EIRQAMDAVR
NSLPSSAPAE ILPLHANLSS DEQREVFKKT SRWKIIASTN VAETSITIDD VIFVVDAGKV
KQTQYDGDTG LSRLVETWVT RAEARQRRGR AGRTQPGTCF KLYTRRQEAQ MAKFAIPEIL
RVPLESISLA VKVTREDEDV RHFLKRAIDP PNVSAMDTAW ENLQNLGAVD ENDKLTALGR
HISMLPIDLR LAKMLVLGTV FRCLGPILTI VAVLSSKPLF VSPLEKRQEA SRARAKFSEG
TSDLLTDLKA YDEVSKLRQD GKTNSAVRLF CEENFISAVT VRDVSGLRND FLSALANIGF
VPQNAKPSTP TLNTNSENLN LLKAVILGGL WPRVARVQLP QKAIKFDKVS GGTVQRENIA
KEYRMFDMRD ERVFLHPASV LFDFAAWKSD YVVYFSKVQT SKLYLRDATE VPLYAILLFG
GPVTVNQVAG GLTIDGKEGV VKLKAWPRIG ILVNMLRRLL DAQLQRGIEE SSVLSSGRND
HVVRAMLMLL EHDGTAHS
//
