ID W6ZPI6_COCMI Unreviewed; 706 AA.
AC W6ZPI6;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=ATP-dependent RNA helicase {ECO:0000256|RuleBase:RU365068};
DE EC=3.6.4.13 {ECO:0000256|RuleBase:RU365068};
GN ORFNames=COCMIDRAFT_95322 {ECO:0000313|EMBL:EUC45521.1};
OS Bipolaris oryzae ATCC 44560.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX NCBI_TaxID=930090 {ECO:0000313|EMBL:EUC45521.1};
RN [1] {ECO:0000313|EMBL:EUC45521.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 44560 {ECO:0000313|EMBL:EUC45521.1};
RX PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT "Comparative genome structure, secondary metabolite, and effector coding
RT capacity across Cochliobolus pathogens.";
RL PLoS Genet. 9:E1003233-E1003233(2013).
CC -!- FUNCTION: RNA helicase. {ECO:0000256|RuleBase:RU365068}.
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|RuleBase:RU365068};
CC -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD box
CC family of RNA helicases and controls ATP binding and hydrolysis.
CC {ECO:0000256|RuleBase:RU365068}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX51/DBP6
CC subfamily. {ECO:0000256|ARBA:ARBA00038200}.
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DR EMBL; KI963983; EUC45521.1; -; Genomic_DNA.
DR RefSeq; XP_007688012.1; XM_007689822.1.
DR AlphaFoldDB; W6ZPI6; -.
DR STRING; 930090.W6ZPI6; -.
DR GeneID; 19128633; -.
DR KEGG; bor:COCMIDRAFT_95322; -.
DR eggNOG; KOG0350; Eukaryota.
DR HOGENOM; CLU_003041_15_2_1; -.
DR OrthoDB; 5476171at2759; -.
DR Proteomes; UP000054032; 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; cd17956; DEADc_DDX51; 1.
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; PTHR24031:SF68; ATP-DEPENDENT RNA HELICASE DDX51; 1.
DR PANTHER; PTHR24031; RNA HELICASE; 1.
DR Pfam; PF00270; DEAD; 2.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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, ECO:0000256|RuleBase:RU365068};
KW Helicase {ECO:0000256|RuleBase:RU365068};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU365068};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU365068};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|RuleBase:RU365068}.
FT DOMAIN 192..443
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 526..680
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..539
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 706 AA; 77510 MW; 4E32272110311757 CRC64;
MAGPLFKRFA PPAPAPKKQP SPTPVHSETS NSAHTTNEPV AGSVITPVED DAVPRSVKKP
KRRKRETDEA NNEHNEIAKK HKSILSKFEK SSKLAEAKSQ QHEDETADKE EEEEELHDLE
PMPQPAPVPE PVYEPTFSTL PTWLAQPTTV EASKTFPFSG LGVDATYVKK LEKQGFKDAL
AVQMALLPML HPGFDQHLGD ICVSAKTGSG KTLAYLLPII EALKDRAVPI LSAIIVVPSR
QLVNQALQVA EELCAGTRIK VGTALGNVAF ATEQKQLVKM RSQYDQKRAQ ELNEKALQQY
QTGLMERGGL YEDLKSMPIG HVPKYDSGVD ILICTPGRLV EHIEHTTGFL LNNLRWLVID
EADQLLNQNF QGWASVLMDA IHGETRPEFM DARERMAKQL RDANSAWSVA LPQRQVTKVV
LSATMEKDLS KLGTLKLRRP KLVVVQDAST ELQSMETEDN VFELPSKLEE FAVHVGDGAN
KPLHLLHVLL NFVFTEKHED ADPSSDSDSS DSSSSSSSDD DSDAGQVSQS SAPRQTGRVL
IFTKSTESAS RLSHLLSALM PGFKNHLKTM TRALTADASR KLLKSFSSGA VKILIASDAA
SRGLDIPDIT HVINYDLPTS ITSYVHRVGR TARAGKAGQA WTLFSKTEAA WFLKQIAKGD
GIKRGNKKVK RMEWKESAVT ADGKKQAYRA ALKQLESAVS GQTESG
//
