ID B3RJU3_TRIAD Unreviewed; 512 AA.
AC B3RJU3;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 24-JAN-2024, entry version 80.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=TRIADDRAFT_52679 {ECO:0000313|EMBL:EDV29844.1};
OS Trichoplax adhaerens (Trichoplax reptans).
OC Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC Trichoplax.
OX NCBI_TaxID=10228 {ECO:0000313|EMBL:EDV29844.1, ECO:0000313|Proteomes:UP000009022};
RN [1] {ECO:0000313|EMBL:EDV29844.1, ECO:0000313|Proteomes:UP000009022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV29844.1,
RC ECO:0000313|Proteomes:UP000009022};
RX PubMed=18719581; DOI=10.1038/nature07191;
RA Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U.,
RA Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L.,
RA Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J.,
RA Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., Dellaporta S.L.,
RA Rokhsar D.S.;
RT "The Trichoplax genome and the nature of placozoans.";
RL Nature 454:955-960(2008).
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DR EMBL; DS985241; EDV29844.1; -; Genomic_DNA.
DR RefSeq; XP_002109046.1; XM_002109010.1.
DR AlphaFoldDB; B3RJU3; -.
DR STRING; 10228.B3RJU3; -.
DR EnsemblMetazoa; TriadT52679; TriadP52679; TriadG52679.
DR GeneID; 6749539; -.
DR KEGG; tad:TRIADDRAFT_52679; -.
DR CTD; 6749539; -.
DR eggNOG; KOG0330; Eukaryota.
DR HOGENOM; CLU_003041_1_3_1; -.
DR InParanoid; B3RJU3; -.
DR OMA; SFVRRAW; -.
DR OrthoDB; 389739at2759; -.
DR PhylomeDB; B3RJU3; -.
DR Proteomes; UP000009022; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; 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 GO; GO:1902775; P:mitochondrial large ribosomal subunit assembly; IBA:GO_Central.
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; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR PANTHER; PTHR47960; DEAD-BOX ATP-DEPENDENT RNA HELICASE 50; 1.
DR PANTHER; PTHR47960:SF1; RNA HELICASE; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 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.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000009022}.
FT DOMAIN 104..132
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 135..327
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 351..503
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 36..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 104..132
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT COMPBIAS 44..60
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..98
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 512 AA; 57761 MW; 50A7F4E4B8CE6539 CRC64;
MNLSGLAYQY FNRYCFTSQL YSKLVPCHRH YSSPALKSVK TRSSRQLEVS RKHKEFTGTK
GNTRMRNQRR FRRPRQNRIL DRPSKTTIKK KKEEPRAITD SGTSSFSRLF LRDDVIDSLA
NINITTPTAI QSLAIPKIAA GKNVLCASET GSGKTIAYLA PLIHRIKEEE EKCGLITRLN
RPRACIVVPS RELAQQTLKV AKSLCHVSKY RVVGVIGGKK QKLLEKALET PTDVVVATPG
MLIKYHRYNQ IFFSDLTHLV LDEADTLFDE SFYERSLEIL EKIKIRGGKP MSLDTLQKDA
QVTVVGATLP KRVEAILNPV IPNLKKVTTK GFHKLLPHIQ QDILKLKQTS KAGTLLKLLK
ERRHGSTIIF CNTVDSCNWL GHYLAKVDLP LLRLHGGMPP EERLIRYDKF QRGEYNILIA
TDIASRGLDT KNVECVINFD FPISVADYIH RAGRTGRVGS KCTGRVISLV SSRKELSLTK
LLEEAAARNT VIDELSKKPK RYSKKKLAAV SS
//
