ID T1IHJ9_STRMM Unreviewed; 1666 AA.
AC T1IHJ9;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
OS Strigamia maritima (European centipede) (Geophilus maritimus).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Myriapoda; Chilopoda;
OC Pleurostigmophora; Geophilomorpha; Linotaeniidae; Strigamia.
OX NCBI_TaxID=126957 {ECO:0000313|EnsemblMetazoa:SMAR000314-PA, ECO:0000313|Proteomes:UP000014500};
RN [1] {ECO:0000313|Proteomes:UP000014500}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Brora {ECO:0000313|Proteomes:UP000014500};
RA Richards S.R., Qu J., Jiang H., Jhangiani S.N., Agravi P., Goodspeed R.,
RA Gross S., Mandapat C., Jackson L., Mathew T., Pu L., Thornton R., Saada N.,
RA Wilczek-Boney K.B., Lee S., Kovar C., Wu Y., Scherer S.E., Worley K.C.,
RA Muzny D.M., Gibbs R.;
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:SMAR000314-PA}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (FEB-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};
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DR EMBL; JH429910; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 126957.T1IHJ9; -.
DR EnsemblMetazoa; SMAR000314-RA; SMAR000314-PA; SMAR000314.
DR eggNOG; KOG0334; Eukaryota.
DR eggNOG; KOG2279; Eukaryota.
DR HOGENOM; CLU_241987_0_0_1; -.
DR OrthoDB; 2958343at2759; -.
DR PhylomeDB; T1IHJ9; -.
DR Proteomes; UP000014500; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0031047; P:regulatory ncRNA-mediated gene silencing; IEA:UniProtKB-KW.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR CDD; cd20435; Tudor_TDRD12_rpt2; 1.
DR Gene3D; 2.30.30.140; -; 1.
DR Gene3D; 2.40.50.90; -; 2.
DR Gene3D; 2.60.40.790; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR007052; CS_dom.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR035437; SNase_OB-fold_sf.
DR InterPro; IPR002999; Tudor.
DR InterPro; IPR000571; Znf_CCCH.
DR PANTHER; PTHR22655:SF2; ATP-DEPENDENT RNA HELICASE TDRD12-RELATED; 1.
DR PANTHER; PTHR22655; UNCHARACTERIZED; 1.
DR Pfam; PF04969; CS; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00567; TUDOR; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00333; TUDOR; 3.
DR SUPFAM; SSF49764; HSP20-like chaperones; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 2.
DR PROSITE; PS51203; CS; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS50304; TUDOR; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW Differentiation {ECO:0000256|ARBA:ARBA00022782};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Meiosis {ECO:0000256|ARBA:ARBA00023254};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000014500};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW RNA-mediated gene silencing {ECO:0000256|ARBA:ARBA00023158};
KW Spermatogenesis {ECO:0000256|ARBA:ARBA00022871};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00723};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00723}.
FT DOMAIN 535..675
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 935..962
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 1322..1381
FT /note="Tudor"
FT /evidence="ECO:0000259|PROSITE:PS50304"
FT DOMAIN 1504..1590
FT /note="CS"
FT /evidence="ECO:0000259|PROSITE:PS51203"
FT ZN_FING 935..962
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 342..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1630..1666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1189..1216
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1632..1658
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1666 AA; 188680 MW; 1412A2DB75CCC4F6 CRC64;
MDRIPVEIRK VVTPVRYLLI NQLVSERDVA SLESELRRYY ENNCIADTDR KPENIALNNM
VITYWEKEDK YVRGIYENKF RRSNGLQHKI FLVDYGRRII LNEINSLKLL PDKFVDKLSF
RSVYLLLPNL EPSSADFLIE DDVKFCFYAS DEWAEAAIDY CKNLVKKYKF EAIAVITDIC
SSNTVKGQLY FVDEVCLNDM LLFKQFAVVA EQSDCCITKE RSPTSCSNTI VSSCGSCDKS
PEQKVSTPCG SRITTEEYTC QPSYNSIKME ISGEKSKPNV QKGLSILEKI ARKAKQKQEQ
EAEAARFSSA ISDSGFEKTQ QCWGAGDQMN VGFNCQSMRN NLSNLSPKPN QNWGAQTSTS
TGDSSKYPNN TEFLRDNLSP KANSDRKTSS SFVNINNEVS RNMLPSRPQS TNQMSSSFVN
INNEVSRNML PSRPQSTNQM SSSFDTIKEM SSSNPQFPHT SPSFNTNKDS RRSMLSFNQQ
TAVQTTPLAF DTDGQLGKTE YCKVFTCGNT KFPHWGIQNF GPRVVRALRN IGIESARPLQ
RLDVALIGPK NSGKSLSYLI PIVVQLLEST ISREKGTPKG NGPEVLILCE SFEAVSSLYN
TCHEILKQDE LREEGSISVI KLNSMVINVR EKGELVNGCH ILISTPAAIV SLLSNESTST
VTNLDRVQYF VFEDCVVEES GRRCDITRVL KCRKEGKTKG DVIEHPKFIL CNQRFVNEIC
QFCTVMSSPM IYMEDLLEAA AFINVNFDVK ICSSYKKDNT LVEILRELSA TKTVVFAASD
NIPHVKVLLE SQSYSVLVAR SGMTKSEVTV VERNWLVETP CILLIDDNTY DEIRITNGKN
LIHYDFLSKP LYSKRFNVLV DAMQEAARFY SGDLTELIKA DCYTCIIITE ANGPQAKFFK
KFANNSCNKA ITQKVEEVLP QLEEIINQSQ MEKETPAVNI CNNFKTFGKC IYNSCKLRHI
LYSNTDNSSY PSQGSVNLKI IRVLCANHFY AHILSYNSEP KNNIQKKYTQ LQMRLQGHLT
SSSNRVTILT PKVGLLAAMK NVDDSFSRVK VEEVNLSTVK VKNLETSICT WIQIDRLLSL
SDEFKQLPAQ AVEIVLANIR PVDESFVWQN EATKYVSSLV LQKELKGKII KSYDNIIWVE
SLKKITILTA ISEAKIDFEL AGQLKKEKLA IGNPEHMTLI EESMRILPSD DATSKLQSLD
NTLEEKEKEI FIEEKNEEVN VDTKLHVVQS EISVLSSKKT GENFKSVSLP PLRKALRSLT
ELRKSLTPQK VFKEKLGLNT LHSVYVPNVI TPSLFYVQKN NEDLDKLTDE INSSQLQELT
GLVKLGEYYL APFECEKIYF RSQTISLMPN NEIKVFCLDV GDTAIVSVKD LRILETKFLE
KLPFQAIPCS MANIIPYEKK WSDKAVEELW GQLITINNLS REVFLLATAE LNPKTNQDAT
YEVVLFNYER TVILNANLVQ KKLARQVCTD FSEYAVHMLP DPGDSAIYTE SDASEICATS
NYQSVAAKVD WYETELEVVL KVLLNNVQDY NLTVDAKRLE FSCLLKDRYY CNNMDLFAPV
DREKVMTTVN SSNVLIRLLK SDKGKWLNLL ASKPKPLWLR YDVDHLDVSD SDEIRPVRLS
CIGKPNATRA YLPDPRQTSD SYDSEDSEFT NAEINNAHQE DSVHPE
//
