ID   V4BUA2_LOTGI            Unreviewed;      1025 AA.
AC   V4BUA2;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=Helicase ATP-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=LOTGIDRAFT_162536 {ECO:0000313|EMBL:ESO92619.1};
OS   Lottia gigantea (Giant owl limpet).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Patellogastropoda; Lottioidea; Lottiidae; Lottia.
OX   NCBI_TaxID=225164 {ECO:0000313|EMBL:ESO92619.1, ECO:0000313|Proteomes:UP000030746};
RN   [1] {ECO:0000313|EMBL:ESO92619.1, ECO:0000313|Proteomes:UP000030746}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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).
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DR   EMBL; KB202050; ESO92619.1; -; Genomic_DNA.
DR   RefSeq; XP_009056760.1; XM_009058512.1.
DR   AlphaFoldDB; V4BUA2; -.
DR   STRING; 225164.V4BUA2; -.
DR   EnsemblMetazoa; LotgiT162536; LotgiP162536; LotgiG162536.
DR   GeneID; 20239041; -.
DR   KEGG; lgi:LOTGIDRAFT_162536; -.
DR   CTD; 20239041; -.
DR   HOGENOM; CLU_002902_0_1_1; -.
DR   OMA; IMLKNYN; -.
DR   OrthoDB; 1352at2759; -.
DR   Proteomes; UP000030746; 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:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR   GO; GO:0006401; P:RNA catabolic process; IEA:InterPro.
DR   CDD; cd18024; DEXHc_Mtr4-like; 1.
DR   CDD; cd13154; KOW_Mtr4; 1.
DR   CDD; cd18795; SF2_C_Ski2; 1.
DR   Gene3D; 1.10.3380.30; -; 2.
DR   Gene3D; 2.40.30.300; -; 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; IPR048392; MTR4-like_stalk.
DR   InterPro; IPR025696; MTR4_beta-barrel.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR016438; SKI2-like.
DR   InterPro; IPR012961; Ski2/MTR4_C.
DR   PANTHER; PTHR12131; ATP-DEPENDENT RNA AND DNA HELICASE; 1.
DR   PANTHER; PTHR12131:SF7; EXOSOME RNA HELICASE MTR4; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF08148; DSHCT; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF21408; MTR4-like_stalk; 1.
DR   Pfam; PF13234; MTR4_beta-barrel; 1.
DR   PIRSF; PIRSF005198; Antiviral_helicase_SKI2; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM01142; DSHCT; 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.
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   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030746}.
FT   DOMAIN          130..286
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          388..560
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        17..43
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        52..67
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1025 AA;  117218 MW;  4D227ADD33E199E9 CRC64;
     MADAFGGDLF DVFEDSSNAS KSEKSSKTKK KDSDEKSQED LLHQIIQKRP VQESSQDEET
     ETKKQKTMVD EISTFDTIPR IQIHTVETVE ACLHEVAIPP DAEFTPLKPP PDKPAQEYPF
     ILDPFQKEAI LCLENYQSVL VSAHTSAGKT VVAVYAIAMS LREKQRVIYT SPIKALSNQK
     YRELYEEFQD VGLMTGDVTI NPTASVLVMT TEILRSMLYR GSEIMREVAW VIFDEIHYMR
     DKERGVVWEE TIILLPDNVH YVFLSATIPN ARQFAEWICH LHKQPCHVVY TDYRPIPLQH
     YLFPSGGDGL HLVVDESGDF REENFNTAMS VLKDAGDAAK GDQKGRKGGS KAQDSNCFKI
     VKMIMERNFA PVVVFSFSRK ECEGYGMSMA KLDFNTVEEK KLVEEVFNNA IDALSDEDKK
     LPQVEHVLPL LKKGVGIHHS GLLPILKETI EILFSEGLIK ALFATETFAM GLNMPARTVL
     FTSARKFDGK DFRWLTSGEY IQMSGRAGRR GLDERGIVIL MIDEKMSPDV GKNLLKGLPD
     PLNSAFHLTY NMVLNLLRVE EINPEYMLER SFYQFQNYAA IPDLCEKLKK KELEYKNIVI
     ENEDNVAAYY KIRQQLDSLS RELLYFIRQP SYLLPFLQPG RLVKVKNDND DYGWGVVVNF
     NKKKEDKTSL EREAAVYIVD VLLYITKDGI KSRDITQVKP CPPSEKGEMQ VVPIMSHLIE
     GVSALRVYIS KDLRPVDNRM RVYKSLVEVK KRFPDGLPQL DPIEDMGIKD KSLKEIIKKI
     EAFEHRLYSH PLHKDKNLQY LYDQYDNKNR VNNEIKVIKS ELKKKKSLLQ MDELKKRKRV
     LRRMGYATAS DVIEIKGRVA CEISSGDELL MTELLFNGVF NDLSPQQSCS LVSCFVFQEN
     ANQLSKLSEE LSGPLRIMQD TARRIARISK EAKLEIDEEV YVDGFKPHMM DVVFAWCNGS
     SFAQVCQMTD CFEGSIIRCM RRLEETLRQL CQAAKAIGNT ELENKFAEGI RQIKRDIVFA
     ASLYL
//