ID A0A226DD66_FOLCA Unreviewed; 1544 AA.
AC A0A226DD66;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Probable ATP-dependent RNA helicase spindle-E {ECO:0000256|ARBA:ARBA00013352};
GN ORFNames=Fcan01_22498 {ECO:0000313|EMBL:OXA42774.1};
OS Folsomia candida (Springtail).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Collembola;
OC Entomobryomorpha; Isotomoidea; Isotomidae; Proisotominae; Folsomia.
OX NCBI_TaxID=158441 {ECO:0000313|EMBL:OXA42774.1, ECO:0000313|Proteomes:UP000198287};
RN [1] {ECO:0000313|EMBL:OXA42774.1, ECO:0000313|Proteomes:UP000198287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VU population {ECO:0000313|EMBL:OXA42774.1,
RC ECO:0000313|Proteomes:UP000198287};
RC TISSUE=Whole body {ECO:0000313|EMBL:OXA42774.1};
RA Faddeeva A., Derks M.F., Anvar Y., Smit S., Van Straalen N., Roelofs D.;
RT "The genome of Folsomia candida.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC {ECO:0000256|ARBA:ARBA00008792}.
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:OXA42774.1}.
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DR EMBL; LNIX01000025; OXA42774.1; -; Genomic_DNA.
DR STRING; 158441.A0A226DD66; -.
DR OMA; FWMHYIF; -.
DR OrthoDB; 21853at2759; -.
DR Proteomes; UP000198287; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; 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; cd17917; DEXHc_RHA-like; 1.
DR CDD; cd18791; SF2_C_RHA; 1.
DR Gene3D; 1.20.120.1080; -; 1.
DR Gene3D; 2.30.30.140; -; 1.
DR Gene3D; 2.40.50.90; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_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 InterPro; IPR035437; SNase_OB-fold_sf.
DR InterPro; IPR002999; Tudor.
DR PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR PANTHER; PTHR18934:SF113; ATP-DEPENDENT RNA HELICASE TDRD9; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF21010; HA2_C; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00567; TUDOR; 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 SUPFAM; SSF63748; Tudor/PWWP/MBT; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50304; TUDOR; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW Differentiation {ECO:0000256|ARBA:ARBA00022782};
KW Helicase {ECO:0000313|EMBL:OXA42774.1};
KW Hydrolase {ECO:0000313|EMBL:OXA42774.1};
KW Meiosis {ECO:0000256|ARBA:ARBA00023254};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000198287};
KW RNA-mediated gene silencing {ECO:0000256|ARBA:ARBA00023158};
KW Spermatogenesis {ECO:0000256|ARBA:ARBA00022871}.
FT DOMAIN 257..428
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 488..690
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1101..1160
FT /note="Tudor"
FT /evidence="ECO:0000259|PROSITE:PS50304"
FT REGION 1..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 196..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..80
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1544 AA; 175969 MW; 5A577F0E8CC71FF1 CRC64;
MDTVRIKEEP IDYDEAASSH TSSKRKRRKR RREEEEEPTS EPTTIKIKKE KDLFEPPEDE
DSSHTVFAET RGDRELTDQA PPSIRVDADE LPGPSSSVPN GSSSAASPSA SATENSIPEW
LPEPDPVPLT NFFEFSSAPI PTLENTVLEN KLKENKLGPE PKIPKVAHYN AHDEVDEKKY
IVENEATNSK LIKDHNRIEA AKDEEDDEAD TNYDTYESSL DPNGPPRREK VYVKYNFKDR
HINTSRLAVF TAKEKILKAI ENHRVVIVDG FTGCGKTTQV PQFILDQHFA NDKVCNIVVT
QPRKIAAISV AKRVCDERNW KLGQVVGYQV GMETKRDRND TLLTYMTTGV LLQKLIATKS
FQSLTHIIID EVHERDLESD LLLLVIKKIL QDDVEGKHRH VKFVLMSATL NSKKFSRYFP
MRTGESEMEE SPVIKIPHSF RHRVDEEFVD NMLASSRDLL DIVESNLNME KATIPEEMYT
VAVDCIISLD EHDRKLATDP RVRSSKQTSN SRVEKRGSVL VFLPGMEEIN RLYRSLTSKN
QIDLEDAVKD DPNFREYDFH QWDVVPLHST ITSDEQQRVF DKPRPFHRKI ILSTNIAESS
VTVPDVMYVI DFCLTKSLCI DPYTNFTTLR MVWASISQCI QRKGRTGRVC DGKVFRLVTK
SFFGKLPQDT KPEMLRSNLE TVVLQLKKLN LGTPKELLSM ALDPPVVSGI ERAVANLKEL
GALTILTTRY PGGVQYDTCD GDLTFLGSIM TDLPIPQQCA RLIMLGHCFG VMKEAIIIAS
ALSVKNPFST PFVRSLDAYL SRLSWSKKSC SDLFALYYVY KHWIKQFSDI GDSTDLDDKK
RNRTTYNERQ WARGAFVQLS VLREIKSTVE LIEERLARHG PHIAPNPFHA ETPSGDLGKD
AGIMLKLAIA GAFYPNYFHR RRPDVKTYER DKSREISGLD LYNTVYFKGF PAGHDGKIYA
KFVADYLSFG LNVPSIKFDG QKVLATFDNR GEKIGPINKG IYRAVKRRQI RDMLEISLTS
RDCEKRILEE WDSRLDRRRF MRCVPQVTLP GVDVSKVYVR VTHVENPGQF WINYSSHTKA
LDEMVDRINE GLVHVPIHSS KVVPNAMCIA PYQGRYYRAK IVLVVPYPID DSLVYFIDYG
NTAWVKNSTL EDFSPSMIEQ RYNSVPCLAV ECRLSNIKPA TIHGAGWHDT AKMEFQMFAE
NAPFVYIDIF SVSKSIISGK LIGHDDRRVE QNLNDRLVNL GFAELTEEAT FSQNNHRARQ
RVSLQDADER IAHNKEQIGE QLDFDFVQPN IDLRKCTKTL IKGPWSPLEL DFQSLCHSSN
TKQVKIDNNS VNSVVLDTEP TAPISRLLVA GYVGIQDRSG SVVARDTTIM PSVPGLLSLM
AMLFAPKIEL RIDVRQTKYT GVLCGLGSAP HEPDLPIYPD HDVEIIFDTV IDDDDIDSIN
RIRYLMNLIM RKDHKKQGGG TVNLSHYQMS VREELLKLLQ RRRKAGEEEI WPQEEYMWSR
IAESSLVPPS RNCFVYEPKD IFAPHYKVRL NDDNAENWSW GFAV
//
