ID U4LF48_PYROM Unreviewed; 765 AA.
AC U4LF48;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=PCON_09147 {ECO:0000313|EMBL:CCX30744.1};
OS Pyronema omphalodes (strain CBS 100304) (Pyronema confluens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Pyronemataceae; Pyronema.
OX NCBI_TaxID=1076935 {ECO:0000313|EMBL:CCX30744.1};
RN [1] {ECO:0000313|EMBL:CCX30744.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS100304 {ECO:0000313|EMBL:CCX30744.1};
RC TISSUE=Vegetative mycelium {ECO:0000313|EMBL:CCX30744.1};
RX PubMed=24068976; DOI=10.1371/journal.pgen.1003820;
RA Traeger S., Altegoer F., Freitag M., Gabaldon T., Kempken F., Kumar A.,
RA Marcet-Houben M., Poggeler S., Stajich J.E., Nowrousian M.;
RT "The genome and development-dependent transcriptomes of Pyronema confluens:
RT a window into fungal evolution.";
RL PLoS Genet. 9:E1003820-E1003820(2013).
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 DDX15/PRP43 sub-subfamily. {ECO:0000256|ARBA:ARBA00024333}.
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DR EMBL; HF935475; CCX30744.1; -; Genomic_DNA.
DR AlphaFoldDB; U4LF48; -.
DR STRING; 1076935.U4LF48; -.
DR eggNOG; KOG0925; Eukaryota.
DR OMA; MKVYPLY; -.
DR OrthoDB; 3682876at2759; -.
DR Proteomes; UP000018144; 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 GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR CDD; cd17973; DEXHc_DHX15; 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; IPR044756; DHX15_DEXHc.
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:SF109; ATP-DEPENDENT RNA HELICASE DHX15 HOMOLOG; 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 Helicase {ECO:0000313|EMBL:CCX30744.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 104..270
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 295..477
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 765 AA; 85936 MW; 5F0B4F519D104B0C CRC64;
MASEKKRTGS DGERPTKRSK AESDPAENPY LAHMYNGAEK TAANGNGETI LHTFKRHDTT
AAQAEMAEDG PSNPFNSKPL SKQYFGILKS RRNLPVHQQR QEFLDMFHST QIMVFVGETG
SGKTTQIPQF VLFDDLPHLN GCKMVACTQP RRVAAMSVAK RVADEMDVQL GDEVGYNIRF
ENNTGPKTIL TYMTDGMLLR EAMNDHNLDR YSCIILDEAH ERTLATDILM GLLKEVAQRR
PDLKIIIMSA TLDAQKFQHY FNDAPLLAVP GRTHPVEIYY TAEAERDYCE AALRTVLQIH
ATEAEGDILL FLTGEEEIED ACRKIKLEAD ELLRETDCGP LSVYALYGSL PPAQQQKIFE
PAPPPRRPGG PPGRKVVVST NIAETSLTID GIVYVVDPGF SKQKVYNPRI RVESLLVSPI
SKASAQQRAG RAGRTRPGKC YRLYTESAFK KELIEQTYPE ILRSNLASTV LELKKLGIDD
LVHFDFMDPP APETMMRALE ELNYLACLDD DGNLTTLGKL ASEFPLDPAL AVMLISSPEF
YCSNEMLSLT ALLSVPQVFT RPPSARKAAD EAKAAFAHPD GDHLTMLNVY HAFKSPEAQR
SPNQWCYDNF LSLRALQSAD NVRNQLQRIM DRNGIELVST PFEDKNYYTN IRKALCAGFF
MQVAKKGQSG KMYVTVKDQQ DVFIHPSTVL QQDNEWLIYN EFVLTTKNYI RTVTHVKPEW
LLEIAPLYYD VTSFPKGPVR TALERTLEKS KRKELIGGKS SGSRR
//
