ID U4LBI2_PYROM Unreviewed; 1213 AA.
AC U4LBI2;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-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=PCON_03321 {ECO:0000313|EMBL:CCX16622.1};
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:CCX16622.1};
RN [1] {ECO:0000313|EMBL:CCX16622.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS100304 {ECO:0000313|EMBL:CCX16622.1};
RC TISSUE=Vegetative mycelium {ECO:0000313|EMBL:CCX16622.1};
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 PRP16 sub-subfamily. {ECO:0000256|ARBA:ARBA00038040}.
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DR EMBL; HF936487; CCX16622.1; -; Genomic_DNA.
DR AlphaFoldDB; U4LBI2; -.
DR STRING; 1076935.U4LBI2; -.
DR eggNOG; KOG0924; Eukaryota.
DR OMA; VDVMFHR; -.
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:0004386; F:helicase activity; 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 Helicase {ECO:0000313|EMBL:CCX16622.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 523..686
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 708..883
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 77..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 145..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 443..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..186
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..239
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..504
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1213 AA; 136215 MW; 4F95E25883E6CD92 CRC64;
MSDLPPGLSP SFTTHIASEL QSHLGTSAPN EYLARNIIQI ARAQPGPKSF IVSCKAFGRY
SDDFLTDVFN SVKQRHQYDE DHGRVSDLGG GNFSAPETSS KDNNNLPGGL LVSKDQKPKE
STDKRESKLG LDRLAKRIKL DLADEDTAVS TEKKQATASG NERVEFKKPA LPVGRHMRER
RIETPSHGGG LSRAAMEKLQ AHRARRGGGD YAREDDRRDS RGDDRRDDDR RDDRYNPSSM
RRNDPTPMRQ QEQRFAGARQ STARSARYGA ATPRMPNSFD RDPDDGPTVE EGDTTELDRD
WYASDELGHA FGDETHNPFG SDNSWADQQR EAALLAKKQG KRISARAQQK MKDVDAWETN
RMLTSGVAQR KDYDDDFDDE EEVRVHLMVH DLKPPFLDGK RVFTKQIDPV PAVKDPQSDM
AVFSRKGSAL VRERRMRRER EKQAQEATNA AGTALGNIMG LKDDDADSAI PAPHVDEKSS
SNKFADAVKD QKANEGASDF SRSRTLKEQR EFLPAFAVRE ELLRVIRDNQ VIIVIGETGS
GKTTQLTQFL YEDGYGRNGR IGCTQPRRVA AMSVAKRVSE EMEVKLGGIV GYAIRFEDCT
SDETVIKYMT DGVLLRESLV DPNLEKYSCI IMDEAHERAL NTDVLLGLLK KILARRRDLK
LIVTSATMNA ERFSRFYGGA PEYTIPGRTF PVDVLWSKSP CEDYVEAAVK QVLTIHLGQG
TGDILVFMTG QEDIEITCEV IAERLKQLNN PPKLNILPIY SQMPADLQAK IFEKGEGGAR
KVIVATNIAE TSLTVDGIMY VVDAGFSKLK VYNPRMGMDA LQITPISQAN ASQRSGRAGR
TGPGKAYRLY TEQAFRNELY TQTIPEIQRT NLANTVLLLK SLGVKDLMEF DFMDPPPQDT
ITTSLFDLWA LGALDNVGEL TKLGKTMANF PMEPSLSKLI ITAVEAGCSE EMLTIVSMLS
VPNVFSRPKE RQEESDQARE KFFVPESDHL TLLHVYSQWK VNGYADRWCV QHFLQPKSLR
RAREIRQQLA DIMKFQKMEL NSCGMDWDVI RRCICAGYYH QAAKVKGIGE YINLRTSVTV
QLHPTSSLYG LGYLPDYVVY HELILTSKEY MSTVTAVDPQ WLAELGGVFY SVKEKGYSAR
DRRTTENEIN KRMEIEAKMA EDKARAEEAA RVAATNVQEA LVRKPTSYVQ KRMATNSVVK
RPNTPSTMRR RGF
//
