ID A0A0D1DZB4_USTMA Unreviewed; 1201 AA.
AC A0A0D1DZB4;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=UMAG_03936 {ECO:0000313|EMBL:KIS67880.1};
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631 {ECO:0000313|EMBL:KIS67880.1, ECO:0000313|Proteomes:UP000000561};
RN [1] {ECO:0000313|EMBL:KIS67880.1, ECO:0000313|Proteomes:UP000000561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021 {ECO:0000313|Proteomes:UP000000561};
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kamper J., Kahmann R., Bolker M., Ma L.J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Muller O., Perlin M.H., Wosten H.A.,
RA de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G., Snetselaar K., McCann M.,
RA Perez-Martin J., Feldbrugge M., Basse C.W., Steinberg G., Ibeas J.I.,
RA Holloman W., Guzman P., Farman M., Stajich J.E., Sentandreu R.,
RA Gonzalez-Prieto J.M., Kennell J.C., Molina L., Schirawski J.,
RA Mendoza-Mendoza A., Greilinger D., Munch K., Rossel N., Scherer M.,
RA Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B., Meng S.,
RA Ho E.C., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J., Deelstra H.J.,
RA Ortiz-Castellanos L., Li W., Sanchez-Alonso P., Schreier P.H.,
RA Hauser-Hahn I., Vaupel M., Koopmann E., Friedrich G., Voss H., Schluter T.,
RA Margolis J., Platt D., Swimmer C., Gnirke A., Chen F., Vysotskaia V.,
RA Mannhaupt G., Guldener U., Munsterkotter M., Haase D., Oesterheld M.,
RA Mewes H.W., Mauceli E.W., DeCaprio D., Wade C.M., Butler J., Young S.,
RA Jaffe D.B., Calvo S., Nusbaum C., Galagan J., Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [2] {ECO:0000313|Proteomes:UP000000561}
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021 {ECO:0000313|Proteomes:UP000000561};
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; CM003150; KIS67880.1; -; Genomic_DNA.
DR RefSeq; XP_011390406.1; XM_011392104.1.
DR AlphaFoldDB; A0A0D1DZB4; -.
DR STRING; 237631.A0A0D1DZB4; -.
DR EnsemblFungi; KIS67880; KIS67880; UMAG_03936.
DR GeneID; 23564254; -.
DR KEGG; uma:UMAG_03936; -.
DR VEuPathDB; FungiDB:UMAG_03936; -.
DR eggNOG; KOG0922; Eukaryota.
DR InParanoid; A0A0D1DZB4; -.
DR OMA; DPMVAPE; -.
DR OrthoDB; 3682876at2759; -.
DR Proteomes; UP000000561; Chromosome 11.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
DR GO; GO:0000390; P:spliceosomal complex disassembly; IBA:GO_Central.
DR CDD; cd17971; DEXHc_DHX8; 1.
DR CDD; cd21691; GH2-like_DHX8; 1.
DR CDD; cd05684; S1_DHX8_helicase; 1.
DR CDD; cd18791; SF2_C_RHA; 1.
DR Gene3D; 1.20.120.1080; -; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 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; IPR044762; DHX8/Prp22_DEXHc.
DR InterPro; IPR049588; DHX8_GH2-like.
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; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR049621; S1_DHX8_helicase.
DR InterPro; IPR003029; S1_domain.
DR PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR PANTHER; PTHR18934:SF85; ATP-DEPENDENT RNA HELICASE DHX8; 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; PF00575; S1; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 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.
DR PROSITE; PS50126; S1; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000313|EMBL:KIS67880.1};
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:UP000000561}.
FT DOMAIN 222..293
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 547..710
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 728..908
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 80..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 158..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 456..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..126
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..212
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1201 AA; 133413 MW; DE1A2CBDD9DF8E74 CRC64;
MASKPDDELY QLELLSLTGK VANELLNHTG INDRVLAEFI LSLHDSATSV ADFKSKLSEV
GADFPDSFVT NLDRLILRLH PKHKKPSASK ASTNDKPGSA SPSAKGKEKA TAEDEERERK
ARMFPGLAIK DQEWQPSEDK GRNAVDDFLK EFEDMAAAKS ASHANGHARH NGIRSPPPGK
ANRYDNDENR AASSSSSSRR GRDDRPPSHL SRPTPDDRPQ LYKIYEGQVS NMRDFGVFVS
LEGLRGRFEG MVHIGSIAAG TRVNHPSDLL SRGQRVKVKV MSVVGDRIGL SMKDVDQATG
RDLTPHLRIK TEAEMAEERE RHAARSASGA NSAPLGGTRG SNGAGSGIAV KEDGRGRSMK
RLTSPERWEL RQLIASGVAK ASDYPELLEE DLRTPNTQPG ADDDDEEIDI EVNEKEAPFL
KGQTSSSIEM SPVKIVKAPD GTLNRAAMAG ATLAKERREL RKQEAEEEAD AEAADMTSGW
LDPMAQQGDR MFAQDRRGNI LGAKAQDQPA WKKETFNKAT TFGRITNLSM QEQRQSLPIF
KLRQELVQAI RDNQVLIVVG DTGSGKTTQM TQYLAEEGFA DRGKIGCTQP RRVAAVSVAK
RVAEEVGCRV GQEVGYTIRF EDCTSPETKI KYMTDGMLQR ECLVDPDVSN YSVIMLDEAH
ERTIATDVLF GLLKKALKRR PDLKLIVTSA TLDAEKFSTY FFGCPIFTIP GRTYPVEILY
TKEPEPDYLD AALITVMQIH LSEPTGDILV FLTGQEEIDT SCEILFERMK ALGPSVPELI
ILPVYSALPS EMQTRIFEPT PAGSRKVILA TNIAETSITI DGIYYVVDPG FVKQNAYDPR
LGMDSLVVTP ISQAQARQRA GRAGRTGPGK CYRLYTEAAY RNEMLPNSIP DIQRQNLAST
ILALKAMGIN DLVNFDFMDP PPAQTLLTAL ESLYALSALD DEGLLTRLGR KMADFPMEPM
MSKMLIASVD LGCSEEMLSI VAMLSVQNVF YRPKDKQTQA DAKKAKFFQP EGDHLTLLGV
YNGWAASKFS MPWCMDNFVQ GRSLRRAQDV RKQLVGIMDR YKHDIVSCGK NYNRVRKAIC
SGYFRNAAKK DPQEGYKSLA ESGGSVYIHP SSALFNRAPE YCVYHEVVLT TREYMREVTA
IEPKWLVEVA PRFFRTADAL NISKRKRQEK VAPLFDRFAK HQDEWRLSKV KRVGKSSQTF
G
//
