ID S8ASQ9_PENO1 Unreviewed; 1118 AA.
AC S8ASQ9;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=PDE_04077 {ECO:0000313|EMBL:EPS29128.1};
OS Penicillium oxalicum (strain 114-2 / CGMCC 5302) (Penicillium decumbens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=933388 {ECO:0000313|EMBL:EPS29128.1, ECO:0000313|Proteomes:UP000019376};
RN [1] {ECO:0000313|EMBL:EPS29128.1, ECO:0000313|Proteomes:UP000019376}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=114-2 / CGMCC 5302 {ECO:0000313|Proteomes:UP000019376};
RX PubMed=23383313; DOI=10.1371/journal.pone.0055185;
RA Liu G., Zhang L., Wei X., Zou G., Qin Y., Ma L., Li J., Zheng H., Wang S.,
RA Wang C., Xun L., Zhao G.-P., Zhou Z., Qu Y.;
RT "Genomic and secretomic analyses reveal unique features of the
RT lignocellulolytic enzyme system of Penicillium decumbens.";
RL PLoS ONE 8:E55185-E55185(2013).
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DR EMBL; KB644411; EPS29128.1; -; Genomic_DNA.
DR AlphaFoldDB; S8ASQ9; -.
DR STRING; 933388.S8ASQ9; -.
DR eggNOG; KOG0923; Eukaryota.
DR HOGENOM; CLU_001832_7_0_1; -.
DR OrthoDB; 3682876at2759; -.
DR PhylomeDB; S8ASQ9; -.
DR Proteomes; UP000019376; 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:SF83; PRE-MRNA-SPLICING FACTOR ATP-DEPENDENT RNA HELICASE DHX16; 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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW mRNA splicing {ECO:0000256|ARBA:ARBA00023187};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000019376}.
FT DOMAIN 480..644
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 669..842
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 65..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..95
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..188
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..204
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..280
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1118 AA; 126732 MW; EB2D8FD77FA292E1 CRC64;
MDNKTFVSDS LIRLTGASDP IAVDFVLAEA SSAKSASALQ DKLVSFLDGS PDDVGAFCGQ
LFSRVGKKAQ SSSSASKPSA SKDSSKKKYR LVDMGEDLPD PASSLGPVNV EAERDRRRQR
DRDRDRDAPS DRDRSRREKE DNRKRDRSRD AESRDRPRTK KLRQRDTNDF DDRWGDEEFG
DEDRYQDEAE FAESPAKRTR LEDGSASPHP ASPDEDMDPQ TKQELERQRD LRERDEFAKR
LANKDSSKSK KIVEDRTRDS EAAKRRALAD DAAARSAVMP DLRERSRQEY LKKREAERLA
LLRSQVAEET AELRENPNLT RREKEEFARN REVLRIAEER LRIDDHRDGY MMPEDYITEK
GKIDRKKKEE ALYKRYVDRD ESGQERFVTE HEEWELEQAA KAKAQIKKAE FVDEGDYEYV
FDDTQQINFV MESKIEGTEK PMTQEQLRFK QQVDAAEKKA ATMEETRKSL PIYQFRDQII
QAVHDHQVLI IVGETGSGKT TQIPQYLHEA GFTKDGLKIG CTQPRRVAAM SVAARVADEM
GTKLGNEVGY AIRFEDNTSD KTILKYMTDG MLLRELLTEP DLGQYAALMI DEAHERTVPT
DIACGLLKDI AKARPDLKLL ISSATMDAQK FQKYFDDAPI FNIPGRRYPV DVHYTSQPEA
NYLAAAITTV FQIHVTQGPG DILVFLTGQE EIEAAEQSLQ ETARKLGSKI PEMIICPIYA
NLPSELQTKI FEPTPPKARK VVLATNIAET SLTIDGIVYV IDPGFVKENV FNPRTGMESL
VVTPCSRASA NQRAGRAGRV GPGKCFRLYT KWAYYNELEE NTTPEIQRTN LNGVILMLKS
LGIDQLLDFD FMDPPPAETI IRALEQLYAL GALNDRGELT KVGRQMAEFP TDPMLAKAIL
AAGQYGCVEE VLSIVSMLGE ASALFFRPKD KKIHADSARN RFTIKEGGDH LTLLNIWNQW
VDSDFSFVWA KENFLQQRSL TRARDVRDQL AKLCDRVEVT ISTCGSTNLV PIQKAITAGF
FPNAARLQRG GDSYRTIKNG QSVYLHPSST LFEVNPRWVI YFELVLTSKE YMRSNMPLQA
EWLVEVAPHY YKKKDLESLG LDRKVPKGTG VAGEKSRT
//
