ID A0A0W8C303_PHYNI Unreviewed; 660 AA.
AC A0A0W8C303;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=ATP-dependent RNA helicase {ECO:0000256|RuleBase:RU365068};
DE EC=3.6.4.13 {ECO:0000256|RuleBase:RU365068};
GN ORFNames=AM587_10008840 {ECO:0000313|EMBL:KUF78406.1};
OS Phytophthora nicotianae (Buckeye rot agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4790 {ECO:0000313|EMBL:KUF78406.1, ECO:0000313|Proteomes:UP000052943};
RN [1] {ECO:0000313|EMBL:KUF78406.1, ECO:0000313|Proteomes:UP000052943}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 0 {ECO:0000313|Proteomes:UP000052943};
RA Liu H., Ma X., Yu H., Fang D., Li Y., Wang X., Wang W., Dong Y., Xiao B.;
RT "Genomes and virulence difference between two physiological races of
RT Phytophthora nicotianae.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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. DDX55/SPB4
CC subfamily. {ECO:0000256|ARBA:ARBA00038002}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KUF78406.1}.
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DR EMBL; LNFO01005336; KUF78406.1; -; Genomic_DNA.
DR STRING; 4790.A0A0W8C303; -.
DR EnsemblProtists; KUF78406; KUF78406; AM587_10008840.
DR OMA; HHIGAII; -.
DR Proteomes; UP000052943; 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; cd17960; DEADc_DDX55; 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; IPR025313; DUF4217.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR24031:SF2; ATP-DEPENDENT RNA HELICASE DDX55; 1.
DR PANTHER; PTHR24031; RNA HELICASE; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF13959; DUF4217; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01178; DUF4217; 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, ECO:0000313|EMBL:KUF78406.1};
KW Hydrolase {ECO:0000256|RuleBase:RU365068};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU365068};
KW Reference proteome {ECO:0000313|Proteomes:UP000052943};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|RuleBase:RU365068}.
FT DOMAIN 34..225
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 252..410
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 498..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 565..660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..535
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..583
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..634
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..660
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 660 AA; 75566 MW; 3867917AA2E25927 CRC64;
MRFHDFKPAL CPEILAETDA LGFEHMTPVQ AATLPLFLSN KDVCVDACTG SGKTLSFVLP
IVQLLKAKLA DGSITAPRHA DLTKLVAMII SPTRELARQI FECAEKFFTR ALPSVQLLLF
VGGTSVDEDL SLIRGAVGKC SVVIGTPGRT EDLLNRCVGS SVETREFEML ILDEADTLLD
MGFEVSLNKI LEHLPKQRRT GLFSATQTQE VKALARAGLR NPATISVQVA NNTQVTPATL
QNYYCLVGHD QRLSALHHFV QSKKGEKLIV FFSTCGSVDF FSRVLEELFK GKNDFPVVAL
HGKMPQKKRT TNYDHFSTLK SGLLVCTDVV ARGIDLPDVD WIVQYDPPQD PNFFVHRVGR
TARAGRSGCA LSFLSSNEDA YVNFLKIRKV PCEEMTLPLD TMEDVLPKVK SFILEDRDLL
EKGTKAFMAF VRSYKEHQCQ FIFRFKELDX GAAARGFCLL QLPKINELRN VRINFEKTDI
KTTDIKYKDK AREKERQKKL AVIAKENEAR DKKNAEMREK KRKRPLDEEN QKHPRRREKK
KGLHQQIVEE WDELAEEEKL YKKMKKGKIT EEEYEKALLG KADSSDDEDD EDEDGDMKKK
SKWQRSEEKM KERFKKKEQV VKKTAEQKRE AAKREERIRK RKKSQHVQRA MQRAQRRARR
//
