ID R7Z4G6_CONA1 Unreviewed; 827 AA.
AC R7Z4G6;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=W97_08167 {ECO:0000313|EMBL:EON68909.1};
OS Coniosporium apollinis (strain CBS 100218) (Rock-inhabiting black yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Coniosporium.
OX NCBI_TaxID=1168221 {ECO:0000313|EMBL:EON68909.1, ECO:0000313|Proteomes:UP000016924};
RN [1] {ECO:0000313|Proteomes:UP000016924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 100218 {ECO:0000313|Proteomes:UP000016924};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Gorbushina A., Noack S., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The genome sequence of Coniosporium apollinis CBS 100218.";
RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
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; JH767603; EON68909.1; -; Genomic_DNA.
DR RefSeq; XP_007784226.1; XM_007786036.1.
DR AlphaFoldDB; R7Z4G6; -.
DR STRING; 1168221.R7Z4G6; -.
DR GeneID; 19905478; -.
DR eggNOG; KOG0922; Eukaryota.
DR HOGENOM; CLU_001832_5_11_1; -.
DR OMA; KVKVWRH; -.
DR OrthoDB; 3682876at2759; -.
DR Proteomes; UP000016924; 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; 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; 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:SF118; ATP-DEPENDENT RNA HELICASE DHX33; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000016924}.
FT DOMAIN 138..311
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 399..574
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 309..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..46
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..97
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 827 AA; 90580 MW; C026E881D1F72279 CRC64;
MPERVHTRFD DEPGPSKPAP ASTAPRQLQQ GKKRKLDDRR GRGPEGRKPP PQAPLKHAKP
QNGTQTNGHQ INGTHINGAH TNGTQIHSTQ TKAPSVARGT SEPKGKAPPG HLAKKRQELL
PIRQALPIWP HAQEIRQALR SPHKDVLLLV GETGSGKSTQ VPQFLLSEPW CTGQIAITQP
RRVAAISLAR RVADEMGSTL GSSSPGSRVG YSVRFDQSVS PSTRIKFLTE GMLLQEMLRD
PWLRQYSVVV VDEVHERSVN VDLVLGFLRN IVTGDKKGRG GKPLKVVVMS ATADIESLQK
FFEDGYRSAS QHPISNGENA VTNGAEDSES SWSGISSSSE DEVPRSITSN KGEPNGVQLE
DGSPTASISQ CHIKGRQYPV KTMYLPDPTQ DFVEAALNSI FQIHYKEPMP GDILVFLTGQ
DTVEGLEKLV NEYALGMGPE VPKIITLPLF AALPQHLQQR VFAPAPPKTR KVILSTNIAE
TSVTVTGVRF VVDCGKAKIK QFRNRLGLDS LLVKPISQSA AIQRQGRAGR EAPGQCYRLY
TEKDYSTLEK NTTPEILRCD LSAAILVMKA RGISDVLNFP FLSQPPREAL EKALLQLLQL
GALSEAGEIS DVGRTIAKLP LTPTLGRCLV EAAKPERNCL TEMIDIIAAL SVENVFLNLV
TEEKREEAEV ARRQLYRREG DHMTFLATVR GYAEEKSDRK AWAERHYVSH RAMQNVMDIR
KQLRGLCGQL SLPAADTEKS SEELTASVLQ SLLRGFAANT ARLMPDGSYR TLLGNQTIAI
HPSSVLFGKK VEAIVFSESV FTSRSYARGV SAVRLDWVAG VLAGVDG
//