ID A0A164VWR5_9CRUS Unreviewed; 1228 AA.
AC A0A164VWR5;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=APZ42_022854 {ECO:0000313|EMBL:KZS12737.1};
OS Daphnia magna.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC Diplostraca; Cladocera; Anomopoda; Daphniidae; Daphnia.
OX NCBI_TaxID=35525 {ECO:0000313|EMBL:KZS12737.1, ECO:0000313|Proteomes:UP000076858};
RN [1] {ECO:0000313|EMBL:KZS12737.1, ECO:0000313|Proteomes:UP000076858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Xinb3 {ECO:0000313|EMBL:KZS12737.1,
RC ECO:0000313|Proteomes:UP000076858};
RC TISSUE=Complete organism {ECO:0000313|EMBL:KZS12737.1};
RA Gilbert D.G., Choi J.-H., Mockaitis K., Colbourne J., Pfrender M.;
RT "EvidentialGene: Evidence-directed Construction of Genes on Genomes.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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:KZS12737.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LRGB01001361; KZS12737.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A164VWR5; -.
DR STRING; 35525.A0A164VWR5; -.
DR Proteomes; UP000076858; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR CDD; cd17983; DEXHc_DHX38; 1.
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; IPR003593; AAA+_ATPase.
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; SM00382; AAA; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Helicase {ECO:0000313|EMBL:KZS12737.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000076858}.
FT DOMAIN 547..710
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 732..907
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 85..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1164..1228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 42..70
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 102..279
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1164..1180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1184..1206
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1228 AA; 140032 MW; 5A4AD6BE05F2E35D CRC64;
MADLDNVDIL EGSAPTTGGI VVRKKKGSAQ IEEGPKESLL GLDKLAEQKR RLKEALLQDL
KEEAEQKKLD EGFQKPHLKV DKKILRASYE TPTYTGGVSD EARNRLQHRQ DRDKQRKFQT
TSKAKIEKHR DESPKFKRPG ERRDDRSIRE DSKRSRRSDN GWETPKFRDE PSTPKIHVKD
TPSRSSWDDD DLAASKGWEK DQAERRERRS QASGGSSERR ERRGDWSERG DRRTSDRSER
GDRRDSDWSE RGNRRSNDRS ERRGSNFSER SERIAYSHYK SARSQRYNTP RDSGIGSSVA
TSDRPATPEV EIDAEEWEAE QKRLDREWYG LDDGYDADSS QPFGGVSEEY AQRKEEQLEQ
KKHKRVSAKQ KQIQKDNELW ERNRMLTSGV VTTIDVDEDY EEEAEARVHL LVHNIVPPFL
DGRYVFTKQP EAVVPVRDPT SDLAMAARKG SALVRVYREQ KERKKAQKKH WELAGTKIGN
IMGVEARPEE DAGAVDETTG ETDYKTSQRF AEHMKSTDNA SSDFAKKKTL QQQRQYLPSF
AVRQQLLTII RENPVVIIVG ETGSGKTTQL TQYLHEAGYS KYGMIGCTQP RRVAAMSVAK
RVSEEMGCNL GDEVGYSIRF EDCTSEKTII KYMTDGILLR ESLREPDLDN YSVVIMDEAH
ERSLNTDVLF GLLRDVVSRR QDLKLIVTSA TMDSTKFADF FGNVPVFIIP GRTFPVDLMF
SKNPCEDYVD SAVKQAIQVH LQPTQGDILI FMPGQEDIEV TCEVIQERLE QVDNAPPLLV
LPIYSQLPSE LQAKIFQKST DGVRKCVVAT NIAETSLTVD GIMFVIDAGF CKLKVYNPRI
GMDALQIYPI SQANANQRAG RAGRTGPGQC FRLYTERQYK DEMLITTLPE IQRTNLANVV
LLLKSLSVQD LLQFHFMDPP PQENMLNSMF QLWTLGALEN TGALTPLGRQ MVEFPLDPAL
SKMLIASVDM KCSADCLVIV SMLSVPAIFF RPKGREEDSD AAREKFQVPE SDHLTLLHVY
NQWKISNYSS TWCQKHFIHH KAMRKVREVR QQLKDIMDQL KLPIISSGQD WDVIRKCICS
AYFHQAARLK GIGEYVHCRT GMPCHLHPTS ALFGMGYTPD YVVYHELIMT SKEYMQCVTA
VEATWLAEMG PMFYSVKQAG AGRSQKRRQA QETMSTMEEE MKLAQEQMVA EKEERLKKEE
SVRKKSSIVT PGRAPEGTPR RTPARFGL
//
