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Database: UniProt
Entry: K1XL57_MARBU
LinkDB: K1XL57_MARBU
Original site: K1XL57_MARBU 
ID   K1XL57_MARBU            Unreviewed;       694 AA.
AC   K1XL57;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN   ORFNames=MBM_00441 {ECO:0000313|EMBL:EKD21328.1};
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:EKD21328.1, ECO:0000313|Proteomes:UP000006753};
RN   [1] {ECO:0000313|EMBL:EKD21328.1, ECO:0000313|Proteomes:UP000006753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MB_m1 {ECO:0000313|EMBL:EKD21328.1,
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; JH921428; EKD21328.1; -; Genomic_DNA.
DR   RefSeq; XP_007288330.1; XM_007288268.1.
DR   AlphaFoldDB; K1XL57; -.
DR   STRING; 1072389.K1XL57; -.
DR   GeneID; 18756376; -.
DR   KEGG; mbe:MBM_00441; -.
DR   eggNOG; KOG0922; Eukaryota.
DR   HOGENOM; CLU_001832_5_11_1; -.
DR   InParanoid; K1XL57; -.
DR   OMA; FHEVMET; -.
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: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:SF136; ATP-DEPENDENT RNA HELICASE DHX35-RELATED; 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   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006753}.
FT   DOMAIN          31..196
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          253..428
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          198..220
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   694 AA;  76864 MW;  A6E623B921FD2B92 CRC64;
     MAEFDLSATF IPSLHKPSSL LPIARHRETL LYLIETYPVT IVVGQTGSGK TTQIPQYLEQ
     AGWCSDGKII AVTQPRRVAA TTVAVRVAEE FGCEVGKEVG YSIRFEDVTS SATRIKFLTD
     GLLLREALVD PLLSRYSVIM VDEAHERSLS TDVLLGVLKK ILKRRPKDLR VIVSSATLQA
     EDFLRFFTAH AESRPKSATD DAMTLDDLIS GSSKPKDPVS DGDIGRIINL EGRMYPVDVL
     YLEAPAEDYV EKAVQTVLDI HTKEPDGDIL VFLTGREEID SAVQAVSERA ARLHPRAQAL
     MPLPLYAGLS TEQQMYVFEG APENTRKVIF STNIAEASVT IDGIVYVIDT GFVKLRAYHP
     LTGIDTLTAT PVSKASATQR AGRAGRTKPG KCYRLYTEAD FQALDEATVP EIQRSNLAPV
     ILQLKALGID NIVRFNFITS PPAELVIRAL ELLFSLGALD DYAKLTKPLG VRMAELAVEP
     MMARTLLSAS SFGCLSEILT IAAMTSLGGN IWLPHDGEKK RMETARRKFA VEEGDHITLL
     NVYQAFVGKG RKEARFCHDN YINFKAMTRA VSIRAQLKRY LERFGISVDE SLSSNANKQP
     LSIGGPDTSE QIRRCLTTGF FAHVAKMQPD GTFRNVAGGT ILHAHPSSLM FNRKADWVIF
     HEVMETGNKT FIRDVTKIEK GWLIEYAPDF YKIR
//
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