ID E1Z1W3_CHLVA Unreviewed; 807 AA.
AC E1Z1W3;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE RecName: Full=ATP-dependent RNA helicase {ECO:0000256|RuleBase:RU365068};
DE EC=3.6.4.13 {ECO:0000256|RuleBase:RU365068};
GN ORFNames=CHLNCDRAFT_56430 {ECO:0000313|EMBL:EFN59565.1};
OS Chlorella variabilis (Green alga).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Chlorellales; Chlorellaceae; Chlorella clade; Chlorella.
OX NCBI_TaxID=554065 {ECO:0000313|Proteomes:UP000008141};
RN [1] {ECO:0000313|EMBL:EFN59565.1, ECO:0000313|Proteomes:UP000008141}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NC64A {ECO:0000313|EMBL:EFN59565.1,
RC ECO:0000313|Proteomes:UP000008141};
RX PubMed=20852019; DOI=10.1105/tpc.110.076406;
RA Blanc G., Duncan G., Agarkova I., Borodovsky M., Gurnon J., Kuo A.,
RA Lindquist E., Lucas S., Pangilinan J., Polle J., Salamov A., Terry A.,
RA Yamada T., Dunigan D.D., Grigoriev I.V., Claverie J.M., Van Etten J.L.;
RT "The Chlorella variabilis NC64A genome reveals adaptation to
RT photosymbiosis, coevolution with viruses, and cryptic sex.";
RL Plant Cell 22:2943-2955(2010).
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.
CC {ECO:0000256|RuleBase:RU365068}.
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DR EMBL; GL433835; EFN59565.1; -; Genomic_DNA.
DR RefSeq; XP_005851667.1; XM_005851605.1.
DR AlphaFoldDB; E1Z1W3; -.
DR STRING; 554065.E1Z1W3; -.
DR GeneID; 17359182; -.
DR KEGG; cvr:CHLNCDRAFT_56430; -.
DR eggNOG; KOG0348; Eukaryota.
DR InParanoid; E1Z1W3; -.
DR OMA; HEVSNKH; -.
DR OrthoDB; 149428at2759; -.
DR Proteomes; UP000008141; 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; IPR025313; DUF4217.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR24031:SF89; ATP-DEPENDENT RNA HELICASE DDX31-RELATED; 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};
KW Hydrolase {ECO:0000256|RuleBase:RU365068};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU365068};
KW Reference proteome {ECO:0000313|Proteomes:UP000008141};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|RuleBase:RU365068}.
FT DOMAIN 500..597
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 540..680
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 290..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 736..807
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..269
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 738..754
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..769
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 791..807
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 807 AA; 84038 MW; E8C266ACF0D72A72 CRC64;
MSDSDNNGLV LNLAAVPEAA GPRQSRTQQR KLKWTQQRAI KRNAHKQKFV GYKGGGSPGW
LGSSRREPEP EQQAAGGGGG GGQLKGYSLD AYEPDPPAAA DLAPNRQKKE EAQQQPGQRQ
QQRDAPCQRQ QQDDPSQQQR QQLEQQQTAA GQQARQKPQP RPRQDVQQQP QQQAWQPSRR
PQPPAAGQLP PGQPRSGARL AAEHLQRRQQ HARGRGGSPR PSGGGGGTAA AANEDEESRR
IGKLRLASRK AGYREPTPDL DEVRAAGSDA DSEDVAAAVA AAVARDRAVQ AELAAVQSRS
RTRHERQHAA GDETGGSGGG GGGAGRVQAG GAGGTRRLAG THDLGRFGGS SSEEEGPGAG
DGVVVDFGVD YGAEEAAQRR RNKRRNKERE AVAAAAAAAA AAGGGGGGAG GGRAKAGGAA
KAAWAGVRPG ELVHAGGGVG EAAAQGQLFG AEPEAGGGGP SGGDGGGGGG FAALGLSRQL
ADHLAAHSFT QPTRVQQQAI PVLLGGRDAL VNAPTGSGKT LRRAAYLAPI VHDLASHQPP
ITRARGTLAL VICPTRELCL QVSDVLTMLV RRFVWLAERT AAFLRFARCA AGVLLCTDVA
ARGLDFPAVT DIVQFDPPGE AAEYVHRVGR TARLGHKGDA VLFLLPSERG YVAHLAAHGA
GADLPMEGHQ GAYALQKQLM EGVAADSHLS RLGGDAFRSW VRAYATHAAA VKNIFHVRRL
HLGHVAHAFA LKERPSLVGK SSTKQASQQK RKAQHAPHAQ QRHKQPKQQH QQHGGGAGAG
GGGGPKQARR QPPQQVASTA GGMYTLT
//
