ID E3QG59_COLGM Unreviewed; 1209 AA.
AC E3QG59;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=GLRG_05038 {ECO:0000313|EMBL:EFQ29894.1};
OS Colletotrichum graminicola (strain M1.001 / M2 / FGSC 10212) (Maize
OS anthracnose fungus) (Glomerella graminicola).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum graminicola species complex.
OX NCBI_TaxID=645133 {ECO:0000313|Proteomes:UP000008782};
RN [1] {ECO:0000313|Proteomes:UP000008782}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M1.001 / M2 / FGSC 10212 {ECO:0000313|Proteomes:UP000008782};
RX PubMed=22885923; DOI=10.1038/ng.2372;
RA O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA Ma L.-J., Vaillancourt L.J.;
RT "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT by genome and transcriptome analyses.";
RL Nat. Genet. 44:1060-1065(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};
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC {ECO:0000256|ARBA:ARBA00008792}.
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DR EMBL; GG697346; EFQ29894.1; -; Genomic_DNA.
DR RefSeq; XP_008093914.1; XM_008095723.1.
DR AlphaFoldDB; E3QG59; -.
DR STRING; 645133.E3QG59; -.
DR EnsemblFungi; EFQ29894; EFQ29894; GLRG_05038.
DR GeneID; 24410403; -.
DR VEuPathDB; FungiDB:GLRG_05038; -.
DR eggNOG; KOG0926; Eukaryota.
DR HOGENOM; CLU_001832_0_4_1; -.
DR OrthoDB; 5490433at2759; -.
DR Proteomes; UP000008782; Unassembled WGS sequence.
DR GO; GO:0005730; C:nucleolus; IEA:EnsemblFungi.
DR GO; GO:0032040; C:small-subunit processome; IEA:EnsemblFungi.
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:0003724; F:RNA helicase activity; IEA:EnsemblFungi.
DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IEA:EnsemblFungi.
DR CDD; cd17982; DEXHc_DHX37; 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:SF99; ATP-DEPENDENT RNA HELICASE DHX37-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 3: Inferred from homology;
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:UP000008782}.
FT DOMAIN 395..572
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 594..834
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 119..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 322..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 664..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..157
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..302
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1209 AA; 134039 MW; E3BFA6EE3DF4B1AE CRC64;
MPKFVPRQRK HKVLARERAK ENGVSSLDTN ADEILPEDQK RMQEKRAQLK AELQGDGVKV
SGKKAKRMEK YITNKLRKDE NREILAKLAQ QKVDTSLFTS IKTLGQGKET KRQALIRTLR
EKNAGLEVDP DAEELLYEKR EDAPEQDSDE SEAEAPKAIK PPPKTQAPGP VRAAAPAAPS
STSTSTSASA SAPTPITKSE PQPPASVGSG LKRPLDFDES GRPVLRKRQK RGGVVSKFSI
VETEKAKDAE DEWGGLSDDQ GEDQESGDDE EASEEESEES SEGSEESEDD EDDDDEEEDE
GDSGSDRKSA FKAWAHAQRN QALGYQPVTP SSTALEIPRP ENFQPRPLEQ EPLPQELQPT
TNLARKAYAV QVTRPPEIQV ARMKLPVVAE EQRIMEMIHN NDIVVVCGAT GSGKTTQVPQ
FLYEAGYGSP GSATPGMIGV TQPRRVAAVS MSKRVAQELG DHSDRVGYQI RFEGTTSAKT
AVKFMTDGVL LREMAQDFSL KKYSAIVIDE AHERSVNTDI LVGMLSRVNN IRKGDDKVDP
SIKPLKIIIM SATLRVEDMT NNTTLFPTPP PVVEVEGRQH PVTIHFARHT QADYVDEAFQ
KIMRGHRKLP PGGFLVFLTG QNEIRHLSKR LTEASGGFTG TSAPKVEISA TDAPVEVEDI
DFGEVDDADA ADFDDGLDDD NDNEHEDDKE FEIEGEEGET GPLKMQVLPL YSLLPTREQM
RVFEDPPENH RQVILATNVA ETSLTIPGIR YVFDCGRSKE RQYDRLSGVQ TYEIGWISKA
SASQRAGRAG RTGPGHCYRL YSSAVYERDL PEFTDPEILR MPVDGVVLQL KAMNLSNVVN
FPFPTPPNRM GLHQAEKLLS YLSAVTPEGQ ITKIGATMSI FPLSPRFARI LLVGHQHDCL
PYTIMMVAAL SAAEIFVPEH QAIPSLAARD ESEFRSNADV IAEDRQANIR RLFNAAHKNF
CYLDDRSDAI KLLQVVGEFA HDPTEKWCED HFVRFKVMKE ITQLRQQITE LLRTNIPAFK
NLKYQDRLDA PSDKQVAYLK QMVAAGFIDH IAIRADKSPV PPELARKPRR AIDVPYVPLV
PLGVGHDTEK FVYIHPSSPL SHLSPQECPE YVVYSHLQRA TQGSDPNKAP KTRMQSLTDV
TGGQLASLAK GTPLVSYGKP VKEISSTANT REVWVLPYLR AEGVGGQGWP LPMKKVTQRK
VAGKGWVVE
//
