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Database: UniProt
Entry: A0A2X0PF50_9BASI
LinkDB: A0A2X0PF50_9BASI
Original site: A0A2X0PF50_9BASI 
ID   A0A2X0PF50_9BASI        Unreviewed;      1128 AA.
AC   A0A2X0PF50;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN   Name=BQ5605_C023g09724 {ECO:0000313|EMBL:SGZ24450.1};
GN   ORFNames=BQ5605_C023G09724 {ECO:0000313|EMBL:SGZ24450.1};
OS   Microbotryum silenes-dioicae.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Microbotryales; Microbotryaceae; Microbotryum.
OX   NCBI_TaxID=796604 {ECO:0000313|EMBL:SGZ24450.1, ECO:0000313|Proteomes:UP000249464};
RN   [1] {ECO:0000313|EMBL:SGZ24450.1, ECO:0000313|Proteomes:UP000249464}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FQNC01000085; SGZ24450.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2X0PF50; -.
DR   STRING; 796604.A0A2X0PF50; -.
DR   Proteomes; UP000249464; 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:UP000249464}.
FT   DOMAIN          487..651
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          673..849
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          66..86
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          118..274
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        147..195
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        210..268
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1128 AA;  126956 MW;  EAE97CD05C000449 CRC64;
     MSSSLKTYVS DNLLSLLGAS DSVTVDYFIT LATSLRHPSP TSIHSLLLTN GLPKSPATQT
     FAQGLTDRLP KSSSSSSTTP LTNLKQTQEL LKKKAEKEKR GMQNQKFTLM LEDEEPALGT
     SLASSSSKSQ KEKGKAKQVS SSKKASSSAL RKRDQAQDGW ESDEEERAAK RSKEEERHKR
     DDEAQARRHA NRRPDGINEF VQPQADQTEQ EEAPVKETEE HAADRRERER LADLKERDEF
     AQRMKDKDKD RTKKLIEDRA DPEAAARRAL AGDPDALQKA MPSLRDRARQ SYLGKREQQQ
     LDLLRIEIAD DERDFRGVKL TKRERQELDR KKELLRLAEE RLAIDEGLDG YQMPDDYFTA
     QGKIDSKKKR DLLSSRYTDV KPKSRGVKDQ EFVTDLEQYE MEQTAKAQLT TGALDRQVVE
     DEYDFVFDES VKIAFALDAE GGIAGSMPTS SKDAALQAQI DEAERKAKSL DEVRKSLPVY
     EWREQFLDAV REYQVVIIEG ETGSGKTTQL PQYLFESGFC KDGLKIGCTQ PRRVAAMSVA
     ARVAEEVGCR LGNEVGYSIR FEDCTSDKTR IKYMTDGMLL REFLTEPDLG GYSVMIIDEA
     HERTLSTDIL LGLVKDIARF RPDFRLLISS ATLNATKFSE YFDDAPIFRI PGRRYPVDIL
     YTPQPEANYL HAAVTTVFQI HTSQPKGDIL VFLTGQDEIE AMQENLEETA RALGNKVAEL
     MICPIYANLP TDMQAKIFEP TPEGARKVVL ATNIAETSIT IDGVVYVIDP GFVKQNSYNP
     RSGMESLVVT PCSRAAAGQR AGRAGRVGPG KCFRLYTKHA YMHELEQDTV PEIQRTNLGT
     VVLMLKSLGI NDLIGFDFLD PPPGDTLIRA LDNLYALGAF NDKGELTKMG RRMAEFPMDP
     AMSKAILASE RYNCTEEVLT IVSMLSESGS LFYRPKQKKL EADTARQNFV KPGGDHFTLL
     NVWEQWQESG FSISWTYEHF IQIKSLTRVR DIRDQLVGLC ERVEIFVDAN PNRTDIVPIQ
     KAICAGYFQN SGRLNRSGDA YRTIKSNQTV NIHPSSSLFQ HQPPPKVVVW FELVLTSREY
     ARQVMEIKSE WLLEVAPHYF KAQDLEALGG QKKGHVKQVG ASALTAKK
//
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