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Database: UniProt
Entry: A0A1S8W5Y3_9FUNG
LinkDB: A0A1S8W5Y3_9FUNG
Original site: A0A1S8W5Y3_9FUNG 
ID   A0A1S8W5Y3_9FUNG        Unreviewed;      1116 AA.
AC   A0A1S8W5Y3;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN   ORFNames=BSLG_01177 {ECO:0000313|EMBL:OON09887.1};
OS   Batrachochytrium salamandrivorans.
OC   Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC   Chytridiomycota incertae sedis; Chytridiomycetes; Rhizophydiales;
OC   Rhizophydiales incertae sedis; Batrachochytrium.
OX   NCBI_TaxID=1357716 {ECO:0000313|EMBL:OON09887.1, ECO:0000313|Proteomes:UP000189906};
RN   [1] {ECO:0000313|EMBL:OON09887.1, ECO:0000313|Proteomes:UP000189906}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BS {ECO:0000313|EMBL:OON09887.1,
RC   ECO:0000313|Proteomes:UP000189906};
RA   Lavstsen T., Jespersen J.S.;
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OON09887.1}.
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DR   EMBL; LYON01000104; OON09887.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1S8W5Y3; -.
DR   STRING; 1357716.A0A1S8W5Y3; -.
DR   VEuPathDB; FungiDB:BSLG_01177; -.
DR   OrthoDB; 3682876at2759; -.
DR   Proteomes; UP000189906; 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:0006397; P:mRNA processing; 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   InterPro; IPR002483; PWI_dom.
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   Pfam; PF01480; PWI; 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:UP000189906}.
FT   DOMAIN          485..650
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          672..848
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          73..93
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          127..268
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        127..146
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        147..165
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        166..197
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        198..225
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        227..268
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1116 AA;  125222 MW;  00CD8C310ABF690D CRC64;
     MTQGDDRALR TWVSDNVMKL LGMSEGTVVD YVLAAATRSK TPRVLLKRLQ AEAQFPVNVE
     TAEFVGQLFA RVPRKAAPPP PTSSTAIGSR SASSAVAGMS ASSNADRRKL EKEAVSLLKK
     NSRFTLLLDD DDDNNNDADI PKKTLQSSKK GKSSGSGGSN TLDEGNISKK NKKDRNLRAK
     DVEDQAKNWE KDASSEPAKN ESASPTDPTN RVDGSTANDQ GDGDQNSESS ETERDRDLRE
     RDEFAQRLKD KDKEGTKKVV EDKSSRIADE EARKRRLLAT DRELRTKAMP DLRDRSRYDY
     LGKRESQRLE LLKKSIEDEE FLFHGESMTK KERRDLELNK KILKITQERL SINDKMDGYM
     MPDDYITEKG KLDKKRQESV LYKRYDDADG DPDAFVTEQD QWEKNQIVKS LAKTSTKDKQ
     ASYADAYDYV IDEEQQIEFV LESAAAIQEN IDSNANKMSD AERKAMSIKE VRESLPIYAY
     REQFLQAMEN YQSLVIVGET GSGKTTQIPQ YLAEAGYTKG GKLKIGCTQP RRVAAMSVAA
     RVAEEMGTKL GYEVGYSIRF EDCTSDKTFV KYMTDGMLLR EFLTEPDLAS YSCLIIDEAH
     ERTLHTDILF GLVKDIARFR PDLKLIISSA TMDAQKFSEY FDNAPIFNVP GRKYPVEVYH
     TAAPEANYLA AAITTIMTIH ITQDKGDILL FLTGQEEIES AQEGLTLTCK ALGSSIAELI
     ICPIFANLPS DMQSKIFEPT PEGARKVVLA TNIAETSITI DGIVYVIDPG FCKQKSFNPQ
     TGMESLVVVP ASRASANQRK GRAGRVGPGK CFRLYTAWAY QNELEENVVP DIQRSNMAST
     SLGINDLMSF DFMDAPPAET LIKSLAQLYA LGALNDRGEL TKLGRRMAEF PVDPMLSKTI
     IAAETYGCTE EIVSIIAMLS IGNAVFHRPK DKAVHADQAR KNFFRPGGDH MTLLAVWNAW
     VETNYSIQWC FENFLQHRSM KRARDIRDQL VGLMERTEVP LISNPDPGNT VPIRQAITAG
     YFYNTATLQR SGDTYRTIKH NQTVSIHPSS SLNSMEKPKW IVYFELVYTT REFVRQVIEI
     QPEWLMEVAP HYYKSNELQD DSLKKLPKSV GKAPIG
//
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