ID R7YJZ5_CONA1 Unreviewed; 981 AA.
AC R7YJZ5;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=W97_01333 {ECO:0000313|EMBL:EON62114.1};
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:EON62114.1, 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};
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; JH767557; EON62114.1; -; Genomic_DNA.
DR RefSeq; XP_007777431.1; XM_007779241.1.
DR AlphaFoldDB; R7YJZ5; -.
DR STRING; 1168221.R7YJZ5; -.
DR GeneID; 19898644; -.
DR eggNOG; KOG0924; Eukaryota.
DR HOGENOM; CLU_001832_6_5_1; -.
DR OMA; VDVMFHR; -.
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; 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:SF91; PRE-MRNA-SPLICING FACTOR ATP-DEPENDENT RNA HELICASE PRP16; 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 3: Inferred from homology;
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 293..456
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 478..653
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 197..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 930..981
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..215
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 930..949
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 981 AA; 110000 MW; 3BABD13A7FEE8A5D CRC64;
MAYQDSPKRR KLDSDNFSVP SRPFTPKPSN SRAQTPRPSR PALLSRPNGT EKPEAEVTEE
DALALDRDWY GGEEYGHTFG DETHNPFGDG DSTWQEQQRE AALVEKKLGK RINARAAQRQ
KDNDAWETNR MLTSGVAQRR DLDTGFDDDD ESTRVHLLVH ELRPPFLDGR QIFTKQLDPV
PAVRDPQSDM AVFARKGSKL VKERRQQRER QKQAHEATNI AGTALGNLMG VKDSDADSAA
PLPGEEEQQL RKRGNRFAGS LKQSEGQSAF SRSKTLEEQR KYLPAFAVRE KLLEVIRNNQ
VTIVVGQTGS GKTTQLTQFL YEDGFAKAGM IGCTQPRRIA AMSVAKRVSE EMSTKLGGLV
GYAIRFEDCT SEETAIKYMT DGVLLRESLV EPDLDKYSCI IMDEAHERGL NTDILMGLFK
KLLPRRRDLR LIVTSATMNA ERFSRFYGGA PEFFIPGRTF PVDIQFSRSP CEDYVDSAVR
QVLAIHVSQS AGDILVFMTG QEDIDVTCEV IEERLKLLND PPKLLILPVY SQLPADLQAK
VFESAPPGVR KVIVATNIAE TSLTVDGIMY VVDAGFSKLN VYNPRMKIDT LQVTPISQAN
ASQRAGRAGR TGPGKCFHLY TERAFRDEFY IQTIPEIQRA NLANIVLLLK SLGVKDLLDF
DFMDPPPQDS IVTSLFDLWA LGAIDNIGGL TALGRAMTAF PMDPSLGKII ITSVDYGCSE
EILTIAAVLS APPVFYRPME RQEEADTAKE KFSVSESDHL TLLNVYNMWK MYGYSDAWCT
THFLHAKALH RARDVRDQLV DIMKKHKMAL TSCGTDWDII RKCICSGYYH QAAKRKGLGE
YINLRTSVTV QLHPTSALYG SPDIPDYVIY HELVQTSKEF MRNVTAVDPH WLAELGGVFY
SVKEKGYSAR DKRVTETEFN RKAELEAKMA EDKEREAQRV AREQEGPKSA VKRPLTSAVH
KVASKGAVRR PTMPKIRGRG F
//
