ID S3C528_OPHP1 Unreviewed; 1304 AA.
AC S3C528;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Dead deah box rna helicase {ECO:0000313|EMBL:EPE06956.1};
GN ORFNames=F503_03383 {ECO:0000313|EMBL:EPE06956.1};
OS Ophiostoma piceae (strain UAMH 11346) (Sap stain fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Ophiostoma.
OX NCBI_TaxID=1262450 {ECO:0000313|EMBL:EPE06956.1, ECO:0000313|Proteomes:UP000016923};
RN [1] {ECO:0000313|EMBL:EPE06956.1, ECO:0000313|Proteomes:UP000016923}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 11346 {ECO:0000313|EMBL:EPE06956.1,
RC ECO:0000313|Proteomes:UP000016923};
RX PubMed=23725015; DOI=10.1186/1471-2164-14-373;
RA Haridas S., Wang Y., Lim L., Massoumi Alamouti S., Jackman S., Docking R.,
RA Robertson G., Birol I., Bohlmann J., Breuil C.;
RT "The genome and transcriptome of the pine saprophyte Ophiostoma piceae, and
RT a comparison with the bark beetle-associated pine pathogen Grosmannia
RT clavigera.";
RL BMC Genomics 14:373-373(2013).
CC -!- SIMILARITY: Belongs to the helicase family. SKI2 subfamily.
CC {ECO:0000256|ARBA:ARBA00010140}.
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DR EMBL; KE148152; EPE06956.1; -; Genomic_DNA.
DR STRING; 1262450.S3C528; -.
DR VEuPathDB; FungiDB:F503_03383; -.
DR eggNOG; KOG0947; Eukaryota.
DR HOGENOM; CLU_002902_1_4_1; -.
DR OMA; CGSDITR; -.
DR OrthoDB; 1352at2759; -.
DR Proteomes; UP000016923; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR GO; GO:0006401; P:RNA catabolic process; IEA:InterPro.
DR CDD; cd18795; SF2_C_Ski2; 1.
DR Gene3D; 1.10.3380.30; -; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR048392; MTR4-like_stalk.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR016438; SKI2-like.
DR InterPro; IPR012961; Ski2/MTR4_C.
DR InterPro; IPR040801; Ski2_N.
DR PANTHER; PTHR12131; ATP-DEPENDENT RNA AND DNA HELICASE; 1.
DR PANTHER; PTHR12131:SF8; HELICASE SKI2W; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF08148; DSHCT; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF21408; MTR4-like_stalk; 1.
DR Pfam; PF17911; Ski2_N; 1.
DR PIRSF; PIRSF005198; Antiviral_helicase_SKI2; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01142; DSHCT; 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:EPE06956.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000016923};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 338..494
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 625..816
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 203..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 539..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..221
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..249
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1304 AA; 144266 MW; 0982282872184327 CRC64;
MLMSLQTSPK LGAQQRLHNM DVIHSRVEDK SFRGIDSILF KRRPKNRAHA SAAAKKCQLE
TAFLQPPKQL PAKLVEKTQQ RWDLQVDKSL LFEIDPPDIG TQTLFYRGGR NFRIVNYEEV
PAPKEANGDA QAVAPSNLTA GLALAGRGHG IEDAAAEAEE EWLQRSILAR ENAKSDASGL
QRVIQAGTGG LLEVAPGLQR GIRFMGDRPK PKPKLGKVTS DELDTAEIVQ NDLEMSSQEE
PSAIRSPTET DDNNNEEGAE DTSAKAAEFD GDVDDLLPVE FPSLQAGQFG PTVSKKKRRE
WAHMVDLNSE SSNYRNLVPG EMARQWPFEL DAFQKEAIYH LECGDSVFVA AHTSAGKTVV
AEYAIALAQK HQTKAIYTSP IKALSNQKFR DFKSTFDDVG ILTGDVQINQ EAKCLIMTTE
ILRSKLYNQS DLLREVEFVI FDEVHYVSDS ERGVVWEEVI IMLPEHVSLI LLSATVPNTY
EFASWVGRTK KRDVYVINTP KRPVPLEHYM WSGKTVQKIV SADRKWLEKG YQEAKILVAG
DGKPPSAGTS VTGGGSRGGS GGGRGVPMRG GNNQQRGGVR GGGRGGGGRG GTGPPRASHN
PGHMGRGGRA TGGSSLAQEK TVWSDVVRYL RKSSLLPACI FVFSRMRCEE YAMSLSNLDF
CDAGEKTRIH SIYSKSITRL TKEDQELPQI TRLRDMATRG IAVHHGGLLP IVKEIVELLF
AQSLVKVLFA TETFAVGLNL PTRTVVFSDH RKFDGTKRRI LSPGEYTQMA GRAGRRGLDL
VGTAIIVPMS ENKDVPPAET LKGLILGVPT RLTSQFRLTY NMILSLHRVE TLKVEDMMKR
SFSEHATQNG RSDHEEKMLE LEEELAKLAH ARSHCEACGD TMAACHIAAE TYRQDTAQMY
QKLFKMPAVA TSIFCPGRLV IFINEKGVHA IGVLADDPFR SVPESGTPTL SMVEVQPPRV
APDDTDMMSF VPALRGFWRS SVPAKIRLRE VKVPLAKVEH LAGYIVPIGR RSSDLTPVEE
QMGSLDLSWG SDIWAEVNLD KVRDVDAVWY IDDRKAKAHA VSVSPALGCP EFSEHFAARH
KEWLVRDKLA EMRRAVDDSS LALLPEYENR VAVLKHLGFV NDSSVVMLKG RVACEVRTAD
ELVLTEVILD NLLAGLEPAE IAALLSIFIY QGKDDMEIES APFISNGLSK AIKEVYRIWK
DTIRTQEQFH VISAGDESER SSKLHFGLME VVYEWASGSP FKNIAVMTTE QEGTIVRTIT
RLEDTCREVR NIGRIIGDTT LETKMGGVKE AIMRNITTVP SLYL
//
