ID A0A1E3NSL1_9ASCO Unreviewed; 906 AA.
AC A0A1E3NSL1;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=PICMEDRAFT_70695 {ECO:0000313|EMBL:ODQ49125.1};
OS Pichia membranifaciens NRRL Y-2026.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Pichia.
OX NCBI_TaxID=763406 {ECO:0000313|EMBL:ODQ49125.1, ECO:0000313|Proteomes:UP000094455};
RN [1] {ECO:0000313|EMBL:ODQ49125.1, ECO:0000313|Proteomes:UP000094455}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-2026 {ECO:0000313|EMBL:ODQ49125.1,
RC ECO:0000313|Proteomes:UP000094455};
RX PubMed=27535936; DOI=10.1073/pnas.1603941113;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goeker M.,
RA Salamov A.A., Wisecaver J.H., Long T.M., Calvey C.H., Aerts A.L.,
RA Barry K.W., Choi C., Clum A., Coughlan A.Y., Deshpande S., Douglass A.P.,
RA Hanson S.J., Klenk H.-P., LaButti K.M., Lapidus A., Lindquist E.A.,
RA Lipzen A.M., Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J.L.,
RA Peng Y., Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C.,
RA Stielow J.B., Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V.,
RA Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:9882-9887(2016).
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DR EMBL; KV454001; ODQ49125.1; -; Genomic_DNA.
DR RefSeq; XP_019020238.1; XM_019163707.1.
DR AlphaFoldDB; A0A1E3NSL1; -.
DR STRING; 763406.A0A1E3NSL1; -.
DR GeneID; 30180394; -.
DR OrthoDB; 3682876at2759; -.
DR Proteomes; UP000094455; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProt.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008186; F:ATP-dependent activity, acting on RNA; IEA:UniProt.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0022613; P:ribonucleoprotein complex biogenesis; IEA:UniProt.
DR GO; GO:0006396; P:RNA processing; IEA:UniProt.
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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000094455}.
FT DOMAIN 280..444
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 469..643
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 169..201
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 239..266
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 7..54
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 906 AA; 102892 MW; 1C34991B815CA48B CRC64;
MSGNKGRFGK RVRDSETWKD DLDLPSDLES VHTSKKRIDK KVSKTTDGNE EKNIDKTDAV
LDEEQMLFGN KISLESNGNN GAALSPQQPI EALPHTLELP KREVDILRLE VTHFQERVAR
NGLTSLSAED KSEFQSRKEL LQKLQQNNHS DNYLLPDDYI TEEGKIDLAK KAKALKMNMR
AERKQRENEW YENQINRAQQ VNQLSKLKKE TTDETEIKYE YVFDKSHMID YVADVPEDEM
KELENKIELE ELIEQEEKRV YSIEETKKSL PVFQFRDELL NAVKKYQVLI VVGETGSGKT
TQLPQYLYEA GYGKHGKIIG CTQPRRVAAV SVAARVADEV GTRVGDKVGY SIRFDERSSE
NTVIKYMTDG MLVREFLTDH DLAKYSVMII DEAHERTLQT DILLGLFKDL LKKRPDLKLI
ISSATINAKK FSDYFDSAPI FNVPGRRYPV EIFYTQQPEA NYLSAAIITV FQIHISQNSA
GDILVFLTGQ DEIETMAESL AETCKKLEGQ IKEMVICPIY ANLPPEQQKK IFEPTPKGAR
KVVISTNIAE TSLTIDGIVY VIDCGFVKEN IYNATTGMES LEVLPCSKAS ADQRAGRAGR
VGPGKCFRLY TKWVYLNDLP RNPTPEILRT DLTGVVLLMM TLGITDLVHF DFMDKPSTKT
LVKALELLYA LGALNERGEL TNIGIKMAMF PTKPMLSKSL LASSELKCCD EVLSIVSMLE
DTGSLFVNSK EKKEMAKNAH ASFHSKIGGD HLTLLQIWNR FVESGFSPQW CHDNFLQYKA
LQKARNVKKQ LQRICRRLGL LSDDRQEPER DPNTTALHVM RAITAGYFPQ SARLSPRGDT
YTTLSRKQPV LIHPSSTLHG AVPPVKLIVY HELVMTTKEF MRHVMPVQGK WLAEYGRNYF
DKKDLL
//
