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Database: UniProt
Entry: C9SVH1_VERA1
LinkDB: C9SVH1_VERA1
Original site: C9SVH1_VERA1 
ID   C9SVH1_VERA1            Unreviewed;       423 AA.
AC   C9SVH1;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN   ORFNames=VDBG_08896 {ECO:0000313|EMBL:EEY22786.1};
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).
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DR   EMBL; DS985226; EEY22786.1; -; Genomic_DNA.
DR   RefSeq; XP_003001100.1; XM_003001054.1.
DR   AlphaFoldDB; C9SVH1; -.
DR   STRING; 526221.C9SVH1; -.
DR   GeneID; 9534492; -.
DR   KEGG; val:VDBG_08896; -.
DR   eggNOG; KOG0346; Eukaryota.
DR   HOGENOM; CLU_003041_17_1_1; -.
DR   OMA; VATDECH; -.
DR   OrthoDB; 227126at2759; -.
DR   Proteomes; UP000008698; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   CDD; cd18787; SF2_C_DEAD; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR47959:SF13; ATP-DEPENDENT RNA HELICASE RHLE; 1.
DR   PANTHER; PTHR47959; ATP-DEPENDENT RNA HELICASE RHLE-RELATED; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 2.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
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:EEY22786.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008698}.
FT   DOMAIN          1..131
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          142..361
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          232..273
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          326..361
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          373..423
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        232..246
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        334..361
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        385..403
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        404..423
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   423 AA;  47209 MW;  E2F413CE0FFBB9E9 CRC64;
     MLVPTRELAD QVHRSIESLA AFCAKDIQAV KLTDKVSTTV QRALLSANPD IVISTPARAW
     ENVSSSALSL ANLTHLVLDE ADLVLSYGYK EDLQNVARSL PKGVQTILMS ATLTPEVDTV
     KGLFCRNPAL LDLEQPEAEG DGITQFVVKC AEDEKFLLIY VIFKLKLIQG KALVFCHDVD
     RSYKLKLYFE QFGIRSCILN AELPVNSRLH VVDEFNKGVY DILIASDDNE VVGDEGQEDE
     GEEETTEEPK KETKKSKKKQ QQQQRASRKD KEYGVSRGID FKNVAAVINF DLPTSAKSYT
     HRIGRTARAG QRGMALSFVI PAQHYRATRP RRLSRPSTTR DSRAHREAAG QEGKRHVPDY
     LLPADGKKGL TADEVGFVPL RKKNDRRNSS RRAGGKKNSN RVFKVGRKKS DPLKSFKAKA
     AKK
//
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