ID B6HGJ2_PENRW Unreviewed; 1212 AA.
AC B6HGJ2;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=Pc20g12310 {ECO:0000313|EMBL:CAP86560.1}, PCH_Pc20g12310
GN {ECO:0000313|EMBL:CAP86560.1};
OS Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS 54-1255) (Penicillium chrysogenum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC Penicillium chrysogenum species complex.
OX NCBI_TaxID=500485 {ECO:0000313|EMBL:CAP86560.1, ECO:0000313|Proteomes:UP000000724};
RN [1] {ECO:0000313|EMBL:CAP86560.1, ECO:0000313|Proteomes:UP000000724}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255
RC {ECO:0000313|Proteomes:UP000000724};
RX PubMed=18820685; DOI=10.1038/nbt.1498;
RA van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA Bovenberg R.A.L.;
RT "Genome sequencing and analysis of the filamentous fungus Penicillium
RT chrysogenum.";
RL Nat. Biotechnol. 26:1161-1168(2008).
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 {ECO:0000256|ARBA:ARBA00008792}.
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DR EMBL; AM920435; CAP86560.1; -; Genomic_DNA.
DR RefSeq; XP_002563716.1; XM_002563670.1.
DR AlphaFoldDB; B6HGJ2; -.
DR STRING; 500485.B6HGJ2; -.
DR GeneID; 8307280; -.
DR KEGG; pcs:Pc20g12310; -.
DR VEuPathDB; FungiDB:PCH_Pc20g12310; -.
DR eggNOG; KOG0926; Eukaryota.
DR HOGENOM; CLU_001832_0_4_1; -.
DR OMA; EAIHNNS; -.
DR OrthoDB; 5490433at2759; -.
DR BioCyc; PCHR:PC20G12310-MONOMER; -.
DR Proteomes; UP000000724; Contig Pc00c20.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR CDD; cd17982; DEXHc_DHX37; 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; IPR003593; AAA+_ATPase.
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:SF99; ATP-DEPENDENT RNA HELICASE DHX37-RELATED; 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 SMART; SM00382; AAA; 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:UP000000724}.
FT DOMAIN 366..543
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 566..811
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 84..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 899..941
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..266
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 911..941
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1212 AA; 134243 MW; 7437A68BF6A16379 CRC64;
MPPKFTPRLR KQKHRQNPDG ESADTNVAQL QPVSKDEKEA RRQKLKGELQ EQHLKMSAKK
QKRLDKYIEN KLKKEENIEL LKKLAQSSVD TSSLQSSRDL SKRKRQDDDV SAPTISAPKH
NAPADISGYE SDDSDIHLKV SDPATDPNEQ KLREEAAAGS GLKRPLELGA DGFPVLKKRK
RAPKKKPVPA PVKADVAWEG FDSDEEDEDE DEEDMDEESG SDIEDGSEEE DTSSEGTSGD
EDEDEDEDED DSDDSNDSED DDDMDEDTPT LKTRQSAFKS WAVQQINEAA GFRPTEGAVT
QEEQVFDPSK LPATYNTVQE EPLPRELQVT HGDPNRKAYS VAVDRTEEIQ TARLGLPVVG
EEQKIMEAIH NNSVVVIWGA TGSGKTTQLP QFLFESGFGS PGSPNPGLIG VTQPRRVAAV
SMANRVSQEL GQHAEKVSYQ IRFESTASKK TAIKFMTDGI LLREIADDFA LRKYSIILID
EAHERSVNTD ILIGMVSRIV GLRKSLSKED PSVKPLKVVI MSATLRISDF TENPSLFRDG
APPLVQAEGR QYPVAVHFSR RTQRDYVEDA FRKVSRGHRK LPAGGMLVFL TGQNEIRQLS
KRLKQAFKPT QREDTTQAKV QLSANEAPLE AEDLELGGTE MDNAGHDDYD SDMEITGLDD
AEEDEGFELA EGEEAMDSST RVHVLPLYSQ LPTKEQMKVF ETPPENSRVI ILATNVAETS
LTIPGIKYVF DCGRAKEKQF DLFTGVQSFQ VGWISKASAN QRAGRAGRTG PGHCYRMYSS
AVYESEFAEY TDPEILRTPI EGVVLQMKSM GLHNVINFPF PTPPSRQGLA KAEKLLKNLG
ALTADGQVTP IGRRLSTYPL SPRFSKMLHI GHQHGCMPYV IALVAALAVG DLFVPENQLD
PNNPLPTTSK KQVDDDSDSD SDSNKRKVYT NADRLADDER EQRTKAYARA QRLFSKHDDT
SDALKSLSAI CAYGYASDGD AFSEKMFLRA KAFKEATQLR RQLTDIVRSN NPGLVPAYEA
RLPEPSQKQI KALKQIVTAG FIDHVAIRAD LAPVPPENPR APRRAIDVPY LTLFRSRDGK
GQDLQERAVY VHPSSLLAKL TPKEMPQYVT YSHLQQSSAS LVSDQVPKIR MFPLAAPSGL
QLSAIAHDTP LIEYGKPIGK ADAIEGVPPR RACWVIPALV GDGGSVGWPM PAKKVVQKKD
PKQGWVIEKF VA
//
