ID K1X6L9_MARBU Unreviewed; 900 AA.
AC K1X6L9;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=MBM_01434 {ECO:0000313|EMBL:EKD20752.1};
OS Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS spot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Drepanopezizaceae; Drepanopeziza.
OX NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD20752.1, ECO:0000313|Proteomes:UP000006753};
RN [1] {ECO:0000313|EMBL:EKD20752.1, ECO:0000313|Proteomes:UP000006753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MB_m1 {ECO:0000313|EMBL:EKD20752.1,
RC ECO:0000313|Proteomes:UP000006753};
RX PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA Huang M.-R., Wu R., Zhou Y.;
RT "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT evolution.";
RL BMC Genomics 13:382-382(2012).
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};
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DR EMBL; JH921429; EKD20752.1; -; Genomic_DNA.
DR RefSeq; XP_007289323.1; XM_007289261.1.
DR AlphaFoldDB; K1X6L9; -.
DR STRING; 1072389.K1X6L9; -.
DR GeneID; 18757369; -.
DR KEGG; mbe:MBM_01434; -.
DR eggNOG; KOG0922; Eukaryota.
DR eggNOG; KOG0926; Eukaryota.
DR HOGENOM; CLU_001832_5_11_1; -.
DR InParanoid; K1X6L9; -.
DR OMA; KVKVWRH; -.
DR OrthoDB; 3682876at2759; -.
DR Proteomes; UP000006753; 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:0004386; F:helicase activity; 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; cd17917; DEXHc_RHA-like; 1.
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:SF118; ATP-DEPENDENT RNA HELICASE DHX33; 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 Helicase {ECO:0000313|EMBL:EKD20752.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000006753}.
FT DOMAIN 146..337
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 462..640
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 386..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..58
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..423
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 900 AA; 99380 MW; 172A394AB04C6E55 CRC64;
MPGTVHIKYG NPSSQQSKQT HNTHLKNGTK RMWDGSPKQE SGTKHNSVKN RPTHPTDTPR
DKTGTSLVAP QKNKIQGTPR SEGTVRKTSS TTGLSNRSTA APSKMVNGPG GIYSQKPDRQ
ALRRAALQLE KTRQNLPIWS KRADIRFALR HNDILLINGE TGSGKSTQVP QFLYTEPWCK
KQTVKIEKEG RTEEISVGGM IAITQPRRVA AMTLASRVAR EMGTPLAKGA VSGEVGYAVR
FDSLVPAGAR IKFLTEGMLL QEMLHDPNLR KYSAVVVDEI HERSIDVDLI AGFLRNIVHG
DKRGRGGIPL KIVIMSATLD LGGIEAFFAR PASQPNYKPG KNHGRILAPH LLNSDIDDTA
ESENSLLSNE SFSSWGGFSD LVEGGETGQD ASQTFEDGPA AKRNKSTKSP PGIRSSKGNQ
DSDDSLQSAH EKNGVAVQYI RGRQYEVDIM YEVSPSLDYL HTILQIVLKL HVTEPLPGDI
LVFLTGQDEI ESLRTELENY AEKLVKTQPR MKVMPLYGAL SAQAQQDAFE KVKEKFTRKV
VLATNIAETS VTVSGVRFVV DCGKSKVKQY RPRLGLESLL SKPISRVSAI QRMGRAGREA
PGKCFRIYTE DDYLKLDQDE LPEILRSDVI EAVLKMKSRG VGNISEFPLM DSPDPMAIQN
ALKQLHMMGA VDDEGNISSL GKKMATFPLP AAYSRVLIAA ADPEANILLE AIDVISCLTT
DSEIFIQPKS EEDQERITDA RKDILSPDGD IITLLAVIRR FACEKTDRGE WCRQRVLSPR
AMKMAMQIRQ QLQQICHQQK LLTKLPAEPT TFEPLSAERM VVLLKAFMKA FASKTALLAP
DGSYVMTSGR NAISVHPSSV LYGQKKTEAI MFLDHVFTAK NYAKKVSPVQ ANWIEEAFAI
//
