ID A0A176W475_MARPO Unreviewed; 1287 AA.
AC A0A176W475;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=AXG93_1881s1180 {ECO:0000313|EMBL:OAE27827.1};
OS Marchantia polymorpha subsp. ruderalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE27827.1, ECO:0000313|Proteomes:UP000077202};
RN [1] {ECO:0000313|EMBL:OAE27827.1, ECO:0000313|Proteomes:UP000077202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Tak-1 and cv. Tak-2 {ECO:0000313|Proteomes:UP000077202};
RC TISSUE=Whole gametophyte {ECO:0000313|EMBL:OAE27827.1};
RA Honkanen S., Jones V.A., Morieri G., Champion C., Hetherington A.J.,
RA Kelly S., Saint-Marcoux D., Proust H., Prescott H., Dolan L.;
RT "Mechanisms controlling the formation of the plant cell surface in tip-
RT growing cells are functionally conserved among land plants.";
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 -!- 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:OAE27827.1}.
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DR EMBL; LVLJ01001819; OAE27827.1; -; Genomic_DNA.
DR OrthoDB; 53793at2759; -.
DR Proteomes; UP000077202; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR CDD; cd17917; DEXHc_RHA-like; 1.
DR CDD; cd18791; SF2_C_RHA; 1.
DR Gene3D; 1.20.120.1080; -; 1.
DR Gene3D; 3.30.160.20; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014720; dsRBD_dom.
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:SF229; ATP-DEPENDENT RNA HELICASE DHX30; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00035; dsrm; 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; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF54768; dsRNA-binding domain-like; 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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000077202}.
FT DOMAIN 324..491
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 579..753
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 27..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1244..1287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1287 AA; 144423 MW; 38567ED7C5F580D3 CRC64;
MVNAVQVTTN PMFRAIRFQS HRGLLRRPES RVGQKWSRGG AAAQKKEGDA TPEACSSSSS
SSLGGDRRSV LDAFQRYWPA TQSSIADAIP RWREKPRGPR SVVDSRVEFA ISSRELSYYA
AQPYSDDEYD SSDNAEMLFD VDSWRRRLNR LLASDHQELI SRDKKDRQDF AHLGPLLHEL
GLYGQMYSKI VVFSKLPLPN YRPDLDEKRP QRLVSFSPHV KESVDSCLQR HLMQKKEYPG
SEFSSDRSDG FESDRENMQQ GETEHFGTKR NIARVEELMK EERQKRKSLR MRNRQRSWQE
LPEGQKMLSF RRSLPAYSER EKLLAAVAAN QVLVVSGETG CGKTTQLPQY ILESEIAAGR
GAECSIICTQ PRRISAVSVA ERVAAERGEE LGESVGYQVR LEGKRGRDTR LLYCTSGILL
RRLMNDSELK GVTHVLVDEI HERGMNEDFL LIVLKNLLQR RPDLKLVLMS ATLNAELFSS
FFDGAPMLHI PGFTYPVESF FLEDVLKQTG HFLTPMNQID DYGQDKQWKM QKQMRGRSRK
NQVNSIADAA LAEQDYSDLH YRIRDSLACW NPESLNFNLI EKLLAHICKQ DKEGAVLVFM
TGWEDISALM DQLKEHPVLG DTEQVMLLGC HGSMPTAEQK LIFNPAPPGI RKIVLATNMA
ETSITINDVV FVVDCGKAKE TSYDALNNTP CLLPQWISQA SARQRRGRAG RVKPGVAYHL
YPKAVHDALD QYQLPELLRT PLQSLCLQIK SLGLGSIEEF LGKALQPPEQ RAVHNAVQLL
KTIGALDDRE NLTDLGRHLS QLPVEPRLGK MLLMGSIFRC LDPVLTIAAG LTTRDPFLMP
MEKKELADEA RLKFAGEDFS DHLALVRAYD GWQGAMKQGM AGEFCWKNFL SSQTLQSMYS
LRKQFAGLLS DAGFEMNRSN EFSGDWDLVR GVICAGLFPG VASAVQKSRS VTIKTKEDGQ
VNLHQNSVNG RESRLIYPWL VFNEKVKTSS VNIRDSTGIS DSILLLFGGE VRKGYEPGHL
LMQDGFLEFF MDRDLATMIL MLREELDELI QRKLEDPEMD IHAEGYNLIQ AILELLHGDE
CQGKFVYGRK VASHSQKDKP VQEQEEDVKG LLQQLVQRGG KAPPKWKTKA LSRGGFQSTV
IVRNKSFLGK PATSKKQAEK NASKVALEWV LHSDAPKGRL LGKKDGNAVA SAPEAALSLF
MKSDETLRGR ISTTHDCYKK GKAGVPAGSL HSLALDIPPY SATHSSETQV LDPGVRSTLV
RSPPPFGTTE SFQRALEAAD SETGMDR
//
