ID C9SMG1_VERA1 Unreviewed; 1047 AA.
AC C9SMG1;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=VDBG_06085 {ECO:0000313|EMBL:EEY19976.1};
OS Verticillium alfalfae (strain VaMs.102 / ATCC MYA-4576 / FGSC 10136)
OS (Verticillium wilt of alfalfa) (Verticillium albo-atrum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=526221 {ECO:0000313|Proteomes:UP000008698};
RN [1] {ECO:0000313|Proteomes:UP000008698}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VaMs.102 / ATCC MYA-4576 / FGSC 10136
RC {ECO:0000313|Proteomes:UP000008698};
RX PubMed=21829347; DOI=10.1371/journal.ppat.1002137;
RA Klosterman S.J., Subbarao K.V., Kang S., Veronese P., Gold S.E.,
RA Thomma B.P.H.J., Chen Z., Henrissat B., Lee Y.-H., Park J.,
RA Garcia-Pedrajas M.D., Barbara D.J., Anchieta A., de Jonge R., Santhanam P.,
RA Maruthachalam K., Atallah Z., Amyotte S.G., Paz Z., Inderbitzin P.,
RA Hayes R.J., Heiman D.I., Young S., Zeng Q., Engels R., Galagan J.,
RA Cuomo C.A., Dobinson K.F., Ma L.-J.;
RT "Comparative genomics yields insights into niche adaptation of plant
RT vascular wilt pathogens.";
RL PLoS Pathog. 7:E1002137-E1002137(2011).
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 PRP16 sub-subfamily. {ECO:0000256|ARBA:ARBA00038040}.
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DR EMBL; DS985220; EEY19976.1; -; Genomic_DNA.
DR RefSeq; XP_003003643.1; XM_003003597.1.
DR AlphaFoldDB; C9SMG1; -.
DR STRING; 526221.C9SMG1; -.
DR GeneID; 9534745; -.
DR KEGG; val:VDBG_06085; -.
DR eggNOG; KOG0924; Eukaryota.
DR HOGENOM; CLU_001832_6_1_1; -.
DR OMA; LYDLWAI; -.
DR OrthoDB; 3682876at2759; -.
DR Proteomes; UP000008698; 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; 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:SF91; PRE-MRNA-SPLICING FACTOR ATP-DEPENDENT RNA HELICASE PRP16; 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 Helicase {ECO:0000313|EMBL:EEY19976.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000008698}.
FT DOMAIN 230..393
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 418..590
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 154..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 866..889
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..170
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1047 AA; 117365 MW; C138485A16D83D3A CRC64;
MSEDRSYAPP VFKRRRLDGS GRSTPRAEHA STPGADVPQP TDEDTKALDR DWYAGDEFGG
HVFGDDMHNP FGNDYSAWEK EHQEAVKAGE DVEPRRDMAA DFDDDEATRV HLLVHELRPP
FLDGRTIFTK QLEPVPAVRD YQSDMAVFSR KGSKVVKEAR QQRERQRQAQ EATSMKGTAL
GNLMGVKEED GDSAMAIAGE EDAVRKPDGE TSNKSRGSTC PRLPSGKDLM RVIRENQVIV
VVGETGSGKT TQLTQFLHEE GYGDAGMIGC TQPRRVAAMS VAKRVAEEMD VKLGSTVGYA
IRFEDCTSKE TVIKYMTDGV LLRESLNEPD LDKYSCIIMD EAHERALNTD ILMGLFKKIL
QRRRDLKLIV TSATMNSKKF SEFYGGAPDF TIPGRTFPVD TMFHRSPVED YVDQAVQQVL
SIHVSMDQGD ILVFMTGQED IEVTCELVQK RLDALNDPPK LSILPIYSQM PADLQAKIFD
RAAPGVRKCI VATNIAETSL TVDGIKYVVD AGYSKMKVYN PKMGMDTLQI TPISQANASQ
RSGRAGRTGP GKAFRLFTEK AFKEELYLQT IPEIQRTNLS NTVLMLKSLG VKDLLDFDFM
DPPPQDTITT SMFDLWALGA LNNLGELTKL GAKMSAFPMD PSLSKLLITA EEYGCSEEMI
TIVSMLSVPN VFYRPKERQD EADTQREKFW VHESDHLTYL QVYSAWKSNG MSDGWCIKHF
LHPKSLRRAK EIRDQLLDIM KMQKMQMLSC GMDWDVIRKC ICSGYYHQAA KYKGSGEYIN
LRTNLGVQLH PTSALYAGHP PDYIVYHELI LTSKVYVSTV TAVDPHWLAD LGGVFYSVKE
KGYSMRDKRI TETEFNRKME IETQMADDRR RQQEQIAAEQ ARDSRKKTLS GPVKKVVTQG
AVKKPNFNEA SPLFLIGRVG PPPPVSVYIV LSLSECPECF CARAGRSAHL KVLLSVDDVP
LRLVQLDDLG RARALVDVLE ELLQHVFGSL RLAFHLVSSA RCRALPRRVM RAGVWAQSHL
VVIRVATPSR EPVLCSSFLR KVAETDA
//
