ID A0A176VED7_MARPO Unreviewed; 1063 AA.
AC A0A176VED7;
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_3507s1360 {ECO:0000313|EMBL:OAE19264.1};
OS Marchantia polymorpha subsp. ruderalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE19264.1, ECO:0000313|Proteomes:UP000077202};
RN [1] {ECO:0000313|EMBL:OAE19264.1, 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:OAE19264.1};
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 -!- 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:OAE19264.1}.
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; LVLJ01003906; OAE19264.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A176VED7; -.
DR OrthoDB; 5488182at2759; -.
DR Proteomes; UP000077202; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
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; IPR011709; DEAD-box_helicase_OB_fold.
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:SF83; PRE-MRNA-SPLICING FACTOR ATP-DEPENDENT RNA HELICASE DHX16; 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; 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 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW mRNA splicing {ECO:0000256|ARBA:ARBA00023187};
KW Reference proteome {ECO:0000313|Proteomes:UP000077202}.
FT DOMAIN 416..595
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 620..793
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 98..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1044..1063
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..212
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1063 AA; 121679 MW; 4E2C92A2A61D35F8 CRC64;
MADDKELRAW VSDQLHALLG YSLPPVVSFV LGLAKKSTSV RELISELHAY LPDKSTTDSF
AQDLFSRMPR KQRSLNNYQR AEKDAAAYLR KQQDYQLLDA DDDEETEPVP VESASRKESK
RKHLRKKREV SDVDEDDEII RPAKKGRSSR TWEEEEDEEE VAMERAREED LREREDFEAR
LRERDEAATK KLMEPKLSRR QEEEAKRRAE AEEVKDLVPV MREAARQSYL KLRKQKKLDE
LRDSLEDEAY LFDGVKLTAK EEEDMRFKRK MYELAKERAE DVDAILGYQM PKAYDDTDGK
VRQDERFAVA NQRYKDVGAD DKLNPFAEQE AWEKHQIGKA TMKFGAADKK SQDDYEFIFE
DQIQFIQTSI LDGMKDEEEE KEDEKQIKKL AAKSAFDKLQ EDRKMLPMFP YREELLKAVE
QYQVLVIVGE TGSGKTTQIP QYLHEAGYTK NGKIGCTQPR RVAAMSVSAR VAEEMGVKLG
HEVGYSIRFE DCTSEKTILK YMTDGMLLRE FLSEPDLASY SVMMVDEAHE RTVSTDVLFG
LVKVFLFNNG SVVMISFVKD ITRFRPDIKL LISSATLDAE KFSAYFDGAP IFRIPGRRYP
VDILYTKAPE ADYLEAAVVT VLQIHVTMPP GDVLVFFTGQ EEIEAAEEIL KTRTRGLGTR
IGEMIICPIY ANLPSDLQTK IFEETPEGAR KVVLATNIAE TSLTIDGIKY VIDPGFCKQK
SYNPRTGMES LIVTPVSKAA AQQRTGRAGR TSPGKCFRLY TAHAYQTEMD DNTVPEIQRT
NLGNVVLMLK SLGIHDLINF DFMDPPPAET LLRALEQLYA LGALNDRGEL TKMGRRMAEF
PLDPMLSKMI VASDKFKCAE EVVTICSMLT VGNSIFYRPK DKQVHADNAR MNFHSGNVGD
HLALLKVFDS WKETDFSTQW CYENYIQVRS MKRARDIRDQ LEGLLERVEI EAASNPDDHE
AIKKAITSGF FYHTAKLQKN GSYRTLKNPQ TVTIHPSSGL SQVLPRWVVY HELVFTTKEY
MRQVIEIKPE WLVEIAPHYY KKSDVEDTAS QKMPKGRGRA AMD
//
