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Database: UniProt
Entry: A0A2G8KMN9_STIJA
LinkDB: A0A2G8KMN9_STIJA
Original site: A0A2G8KMN9_STIJA 
ID   A0A2G8KMN9_STIJA        Unreviewed;      2094 AA.
AC   A0A2G8KMN9;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=U5 small nuclear ribonucleoprotein 200 kDa helicase {ECO:0000256|ARBA:ARBA00034541};
GN   ORFNames=BSL78_13861 {ECO:0000313|EMBL:PIK49237.1};
OS   Stichopus japonicus (Sea cucumber).
OC   Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Holothuroidea;
OC   Aspidochirotacea; Aspidochirotida; Stichopodidae; Apostichopus.
OX   NCBI_TaxID=307972 {ECO:0000313|EMBL:PIK49237.1, ECO:0000313|Proteomes:UP000230750};
RN   [1] {ECO:0000313|EMBL:PIK49237.1, ECO:0000313|Proteomes:UP000230750}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Shaxun {ECO:0000313|EMBL:PIK49237.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:PIK49237.1};
RX   PubMed=29023486;
RA   Zhang X., Sun L., Yuan J., Sun Y., Gao Y., Zhang L., Li S., Dai H.,
RA   Hamel J.F., Liu C., Yu Y., Liu S., Lin W., Guo K., Jin S., Xu P.,
RA   Storey K.B., Huan P., Zhang T., Zhou Y., Zhang J., Lin C., Li X., Xing L.,
RA   Huo D., Sun M., Wang L., Mercier A., Li F., Yang H., Xiang J.;
RT   "The sea cucumber genome provides insights into morphological evolution and
RT   visceral regeneration.";
RL   PLoS Biol. 15:E2003790-E2003790(2017).
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:PIK49237.1}.
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DR   EMBL; MRZV01000474; PIK49237.1; -; Genomic_DNA.
DR   STRING; 307972.A0A2G8KMN9; -.
DR   Proteomes; UP000230750; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProt.
DR   CDD; cd18021; DEXHc_Brr2_2; 1.
DR   CDD; cd18795; SF2_C_Ski2; 2.
DR   Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 2.
DR   Gene3D; 2.60.40.150; C2 domain; 2.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
DR   Gene3D; 1.10.3380.10; Sec63 N-terminal domain-like domain; 2.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR041094; Brr2_helicase_PWI.
DR   InterPro; IPR048863; BRR2_plug.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR004179; Sec63-dom.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR47961; DNA POLYMERASE THETA, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G05260)-RELATED; 1.
DR   PANTHER; PTHR47961:SF6; DNA POLYMERASE THETA, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G05260)-RELATED; 1.
DR   Pfam; PF21188; BRR2_plug; 1.
DR   Pfam; PF00270; DEAD; 2.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF18149; Helicase_PWI; 1.
DR   Pfam; PF02889; Sec63; 2.
DR   PIRSF; PIRSF039073; BRR2; 2.
DR   SMART; SM00382; AAA; 2.
DR   SMART; SM00487; DEXDc; 2.
DR   SMART; SM00490; HELICc; 2.
DR   SMART; SM00973; Sec63; 2.
DR   SUPFAM; SSF81296; E set domains; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 4.
DR   SUPFAM; SSF158702; Sec63 N-terminal domain-like; 2.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 2.
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:UP000230750}.
FT   DOMAIN          485..664
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          1284..1459
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   REGION          29..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          183..234
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        51..76
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        202..229
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2094 AA;  237977 MW;  929906817F1F5E83 CRC64;
     MAGATARSLQ YEYKANSNLV LQADRSLIER RGRDEATGEV MSLSGRTTGS RMGDKAKRNK
     PPMQEERKIK RQKRDDAKYD MNKFKGQTLL SEGIDDMVGI YYRPKTPETR TTYEALLSFI
     QAALGDQPRD ILCGAADEVL ATLKNDNSRS KEKEKELELL LGKLAEERFA LLVNLGKKIT
     DYGGDKDKNP IDETIGVNVQ FEESDAEDDP EDYGEVKDEE SESEEEGEEP ARDNALTTSL
     AGGEALLGSQ KDLHPRDIDA YWLQRQLGTF YDDPNVSQAK AGEVLDILKD AADDGQVENQ
     LVMLLGTNRF DFIKLLRKER QMILHCTLLA KAQNSAERAR LEEKMKAEPE LTAILEALTE
     TEKEDLIQEE RARKAAARQT RVDADLEAME TDEADNNLAP QKLLDMDDLT FAQGSHLMAN
     QKCQLPDGSF RKQRKGYEEV HVPALKPKPF DEDETLVYID KLPKYAQPAF EGFKSLNRIQ
     SRLYKAALET DENLLLCAPT GAGKTNVALL TILREIGKNI NTDGTINTEA FKIIYIAPMK
     SLVQEMVGNF RKRLSSYGIT VSELTGDTQL TKEQITATQI IVCTPEKWDI ITRKGGEKTY
     TQLVRLIIID EIHLLHDDRG PVLECLIASF RPVPLEQQYI GITEKKAIKR FQLMNEIVYE
     KVMDHAGKNQ VLVFVHSRKE TGKTARAIRD MCLEQDSLGQ FLKEGSASTE ILRTEADQAE
     NLELKDLLSY GFAIHHAGMS KIDRTLVEDL FADRHIQVLV STATLAWGVN LPAHTVIIKG
     TQPRKGTMGR AWPLDSFRCW GVLVDPVCTK GEGILITGHS ELQYYLSLQN QQLPVESQLV
     SKMVDNLNAE VVLGNIQNMK DAINWLGYTY LYIRMMRNPT LYGIPVDAKD KDPYLEQFRI
     DLIHTAAMVL DKNNLIKYDK KSGNFQMTEL GRIASHYYCT NDSMSTYNSL LKPTLSEIDL
     FRVFSLSSEF RNMVVREEEK MELNMLLDRV PIPIKESIEE PSAKVNTLLQ AFISHLKLEG
     FALVSDMVYI TQSAGRLIRA IFEIVLHRGW AQLTDKTLAL AKMIDKRMWQ SMSPLRQFKR
     IPEEVTRKIE KKNFPWERFY DLGPNELGEL IRMPKMGKTI HKYIHFFPKL ELSAHIQPIT
     RSTLRVELTI TPDFQWDEKV HGQSEAFWIL VEDVDSEIIL HHEYFLLKSK FAQDEHVVKF
     FVPVFEPLPP QYFIRVVSDK WIGSETQLPV SFRHLLLPEK NAPPTELLDL QPLPVSALRN
     PTFESLYSSK FSVFNPIQTQ VFYAVYNGDD NIFIIGAPTG SGKTVIGEMA ILRMLTQDSD
     GRCVYVTPLD DVAEQIYNEW HAKFQMQLGK KVVLLTGETA TDLKLLAKGN IIVCTPDKWD
     VLSRRWKQRK NVQSVNLFIV DELHLIGGDD GPILEVLCSR MRYISSQIER NIRIVSLSSS
     LANAKDVAQW LGAAANNTFN FHPNVRPVSL ELHIQGFNIT HTASRLVAMV KPTYNAILKY
     SPSKPVIVFV PSRKQTKLTA IDLLTYVSVE ESDESRFLHV DKKDLAAHLS KVTDETLREM
     LENGIAYLHE GLSEIEQRVV EQLYSVGAIQ VVVASRNMCW GLTLSAHLAV IMDTQYYNGK
     IHAYVDYPVT DVLQMVGRAN RPDIENEVSK CVILCQGSKK DFYKKFLYEP LPVESHLDHC
     LHDHFNAEVV TKTIENKQDA VDYLTWTFLY RRMAQNPNYY GLQGITHRHL SDNLSELVES
     TLQDLEHSKC VSIEDEMEIN PLNLGMIAAY YYINYTTIES FSMSLNNKTK IKGLIEIIAS
     AAEYENIPIR HHEDSILKQL ASRVPNKLSQ ARYNDPHVKT NLLLQAHLGR MQLSAELQGD
     TEEILSKALR LIQACVDVLS SNGWLSPALA AMELAQMVTQ AMWNKDSYLK QLPHFDSDLI
     KRCMEKEVES IFDIMEMEDQ ERTDLLQLKD VQMADVARFC NRYPNIELTY EVQEKDSIES
     GGPVVVMVTL EREDEITGPV IAPLFPQKRE EGWWVVIGDT KTNSLISIKR LTLQHKAKVK
     LDFVAPSPGS HNYTIYYMSD AYMGCDQEYK FSIDVKEVAS DDESGDSQES SDED
//
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