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Database: UniProt
Entry: T1FXV7_HELRO
LinkDB: T1FXV7_HELRO
Original site: T1FXV7_HELRO 
ID   T1FXV7_HELRO            Unreviewed;      1159 AA.
AC   T1FXV7;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ESO05942.1, ECO:0000313|EnsemblMetazoa:HelroP64508};
GN   Name=20213655 {ECO:0000313|EnsemblMetazoa:HelroP64508};
GN   ORFNames=HELRODRAFT_64508 {ECO:0000313|EMBL:ESO05942.1};
OS   Helobdella robusta (Californian leech).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Clitellata;
OC   Hirudinea; Rhynchobdellida; Glossiphoniidae; Helobdella.
OX   NCBI_TaxID=6412 {ECO:0000313|EnsemblMetazoa:HelroP64508, ECO:0000313|Proteomes:UP000015101};
RN   [1] {ECO:0000313|Proteomes:UP000015101}
RP   NUCLEOTIDE SEQUENCE.
RA   Hellsten U., Grimwood J., Chapman J.A., Shapiro H., Aerts A., Otillar R.P.,
RA   Terry A.Y., Boore J.L., Simakov O., Marletaz F., Cho S.-J.,
RA   Edsinger-Gonzales E., Havlak P., Kuo D.-H., Larsson T., Lv J., Arendt D.,
RA   Savage R., Osoegawa K., de Jong P., Lindberg D.R., Seaver E.C.,
RA   Weisblat D.A., Putnam N.H., Grigoriev I.V., Rokhsar D.S.;
RL   Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ESO05942.1, ECO:0000313|Proteomes:UP000015101}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=23254933; DOI=10.1038/nature11696;
RA   Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA   Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA   Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA   Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA   Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT   "Insights into bilaterian evolution from three spiralian genomes.";
RL   Nature 493:526-531(2013).
RN   [3] {ECO:0000313|EnsemblMetazoa:HelroP64508}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (JUN-2015) to UniProtKB.
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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC       {ECO:0000256|ARBA:ARBA00008792}.
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DR   EMBL; AMQM01000479; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KB096324; ESO05942.1; -; Genomic_DNA.
DR   RefSeq; XP_009015310.1; XM_009017062.1.
DR   AlphaFoldDB; T1FXV7; -.
DR   STRING; 6412.T1FXV7; -.
DR   EnsemblMetazoa; HelroT64508; HelroP64508; HelroG64508.
DR   GeneID; 20213655; -.
DR   KEGG; hro:HELRODRAFT_64508; -.
DR   CTD; 20213655; -.
DR   eggNOG; KOG0921; Eukaryota.
DR   HOGENOM; CLU_001832_1_2_1; -.
DR   InParanoid; T1FXV7; -.
DR   OMA; RFKCELR; -.
DR   OrthoDB; 1095660at2759; -.
DR   Proteomes; UP000015101; Unassembled WGS sequence.
DR   GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR   GO; GO:0043138; F:3'-5' DNA helicase activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR   GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0050684; P:regulation of mRNA processing; IBA:GO_Central.
DR   CDD; cd19854; DSRM_DHX9_rpt1; 1.
DR   CDD; cd19855; DSRM_DHX9_rpt2; 1.
DR   CDD; cd18791; SF2_C_RHA; 1.
DR   Gene3D; 1.20.120.1080; -; 1.
DR   Gene3D; 3.30.160.20; -; 2.
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; IPR044445; DHX9_DSRM_1.
DR   InterPro; IPR044446; DHX9_DSRM_2.
DR   InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR   InterPro; IPR014720; dsRBD_dom.
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:SF119; ATP-DEPENDENT RNA HELICASE A; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00035; dsrm; 2.
DR   Pfam; PF21010; HA2_C; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF07717; OB_NTP_bind; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00358; DSRM; 2.
DR   SMART; SM00847; HA2; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF54768; dsRNA-binding domain-like; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS50137; DS_RBD; 2.
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   Helicase {ECO:0000256|ARBA:ARBA00022806};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015101};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00266}.
FT   DOMAIN          3..71
FT                   /note="DRBM"
FT                   /evidence="ECO:0000259|PROSITE:PS50137"
FT   DOMAIN          185..257
FT                   /note="DRBM"
FT                   /evidence="ECO:0000259|PROSITE:PS50137"
FT   DOMAIN          394..560
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          636..809
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          75..112
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        79..112
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1159 AA;  130436 MW;  A8594CDD5CBA2C6D CRC64;
     MKDIKDFLYS WCGKKKIVPA YEIRTTGNRQ RQRFLCECRL PGYSYVAVGN STSKKDAQTN
     SARDMLQYLI RTGEIDPSQA PDLNETSEPM GRSQIRDLNR PQEATTRGCT TTTTTTTTTT
     TYNITTITTA ATTITTTAAT TTTTAATAST TRTTATATTT TTAATATAEE ADFTADLHGS
     WTMENSKSRL HQYLQTNKIK TDYKYSFVGP DHSRSFIAEM SFYLPSLRRN ISAREHGSNK
     QVASKSCALS LVRQLFHLKL IEAFTGLKKS KEIELPPFTT KLNSDLEDEL NALLDEMQIS
     INLVGWLLGL AGWFVNSNDV QAACIVSWSP PVPNWNPWVS CNIDEGPLAT ATMEDISGDL
     LNTYTDKLNN DGAFIKSLND RKRLPIFNMR QQLIQTIRRH SVVLVRGETG SGKTTQVPQF
     LLDDMIERGE GSMCNIVVTQ PRRISAISIS ERVAAERCEP LGQTCGYSVR FESCLPRPYG
     SILYCTVGCL LRKLESGLRG VSHVVVDEIH ERDINTDFLL ILLRDMVQTF PDMRVVLMSA
     TIDTTTFQEY FSDSCQLVEV SGRTYDVEEY FLEDVVEMLR FTPTPNLKKR RNNNNNKDDI
     NDDDDENCNM YVSGSYSEHT KRAMSMMSEK EHDFELVEAL IKHISTKNIP GAILIFLSGW
     NIIFTLHKYL SQHPIIGRSR YRILPLHSQI PREEQHKVFE PVPQGVTKII LSTNIAESSV
     TIDDVVYVID FCKSKIKMFT SHNNMTNYAV VWCSRTNLEQ RKGRAGRVRP GFSYHLCSRE
     RFKRLDQYTC PEILRSPLHE LCLSIKLLRL GPIGWFLSKA IQAPPIDAVI EAEALLREMK
     ALDRNDDLTA LGRILARMPI EPRLGKMIIY ACVFRIADAA CIIASSSTFT EPFVVPMDRR
     RLDWIHKNMA GDRFSDHCAL LNAFQMWNDA KNYGEMSEVN FCDAKSLSLS TLRMTNEAKN
     QLCGILINAG FPEDCFTPVK FKFRGGDHNL DLLNTLLGIG FYPNICMHKD KRKVLTMGNK
     PALIHKSSVN CSNRPIQYPI PFFVFSEKIR TRAVSCKQMS MYTPVQMLLF GARSVKFDGN
     HIVLDSWINL AMDPVVAAKV AALRPLLEDL VVRATSDPES LEAGQGRGHE DLDGKLMRLV
     GQLSNINCAT FGFVGPEGE
//
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