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Database: UniProt
Entry: A0A0V0RIB0_9BILA
LinkDB: A0A0V0RIB0_9BILA
Original site: A0A0V0RIB0_9BILA 
ID   A0A0V0RIB0_9BILA        Unreviewed;      2116 AA.
AC   A0A0V0RIB0;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=U5 small nuclear ribonucleoprotein 200 kDa helicase {ECO:0000256|ARBA:ARBA00034541};
GN   Name=Snrnp200 {ECO:0000313|EMBL:KRX14222.1};
GN   ORFNames=T07_7898 {ECO:0000313|EMBL:KRX14222.1};
OS   Trichinella nelsoni.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=6336 {ECO:0000313|EMBL:KRX14222.1, ECO:0000313|Proteomes:UP000054630};
RN   [1] {ECO:0000313|EMBL:KRX14222.1, ECO:0000313|Proteomes:UP000054630}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS37 {ECO:0000313|EMBL:KRX14222.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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:KRX14222.1}.
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DR   EMBL; JYDL01000167; KRX14222.1; -; Genomic_DNA.
DR   STRING; 6336.A0A0V0RIB0; -.
DR   Proteomes; UP000054630; Unassembled WGS sequence.
DR   GO; GO:1990904; C:ribonucleoprotein complex; 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:SF4; U5 SMALL NUCLEAR RIBONUCLEOPROTEIN HELICASE; 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; 1.
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.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:KRX14222.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054630};
KW   Ribonucleoprotein {ECO:0000313|EMBL:KRX14222.1}.
FT   DOMAIN          490..673
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          683..920
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DOMAIN          1317..1492
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   REGION          55..79
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          207..238
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          372..391
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        55..72
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        208..234
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2116 AA;  242890 MW;  3DEA37E2B7B9956E CRC64;
     MADAAARELQ YEYKANSNLV LQVDYSLIDR RPKDEATGEV LPLNADRLRG IKMGDKFYRS
     KPPMPDEKKP KKAKKEKSHK EALKLKKHGL FSDSDDFVGV YKPKTQETRQ TYDVILAFIQ
     EAIGDQPRDI LCGAADEVLA TMKSDKIRDK ERKHEVELLL GPLTDERFAL LLNLGKKITD
     YSMHNENKKT TAFEGDIENS YGVNVQFEES DAEDDEEVDD EIRDDSENDD EGEDTLAGST
     LKASGLVEEF SIEEEQKKEL HPRDIDAYWL QRSLGKFYQD PIVAQQQSRE VLEILKTAVD
     DRDCENRLVR LLGFDQFDFI RTLRQHRNMI LYCTLMASAQ SEKERQQIEA VLLETPELTK
     ILHALKEADA EDFTDQERGR RRKVKTEVHS SDKNMEVDDS GWCQQRQFLD FDDLIFAQGS
     HFMSNKRCQL PDGSFRKQHK GYEEVHVPAL KPRPFDPDEK LIKIEELPEF AQAAFGNFKT
     LNRIQSKLVK ATLENDGNLL LCAPTGAGKT NVALLCILRE ISKHVNADGT INVEDFKVIY
     IAPMRSLVQE MVGNFTTRLA PYKLKVGELT GDHQLTQEEI AQSQVIVCTP EKFDIITRKG
     LERSFVQLVR VVIFDEIHLL HDDRGPVLEA LVARVLRNME QSQEHVRLVG LSATLPNYED
     VGTFLRVEKS NVFFFDNSYR PVPLEQEYIG VTEKKAMKRF QIMNEVVYDK VLQHAGRSQI
     LIFVHSRKET GKTARSLRDS CLERDTLSMF MREGSASTEI LRREADQVKN NELKDLLPYG
     FAIHHAGMTR VDRTLVEDLF ADRHIQVLVS TATLAWGVNL PAHTVIIKGT QIYNPEKGRW
     VELGALDIMQ MMGRAGRPQY DTKGKGIMIT NHTELQYYLS LMNQQLSVES QMISKLADCL
     NAEIVLGTVN NVREAVDWLA YTYLYIRMLR APTLYGINHD EVKNDPLLEQ RRADLIHTAA
     TLLDKCNMIK YERRSGIFQV TELGRIASYF YCTHETIHTY NQLLKPVMTE IELLRVFSLS
     SEFKNIMVRE EEKLELLKLA ERVPIPIKEN LEEPSAKVNV LFQAYISQLK LEGFALQSDM
     VYVSQSAGRL FRAIYEIVLF RSWAQLAQKT LSMCKMVERK MWQSMCPLRQ FKKLPDEIVR
     KIEKKNFTFE RLHDLEPNEL GELIRIPKMG KLLHRFIHQA KLTVTPDFQW DEKIHGVSQG
     FWVFVEDVDC ERILHYEYFL LKQKFAEDEH TLKFFVPVFD PMPILYYIHI VSDKWLGAET
     ILPVSFRHLI LPEKYPPPTE LLDLQPLPVS ALNNTDLEEL YADEIKSFNP IQTQVFRVFY
     ENKDNVFVGA PHGSGKTICA ELAILQLFKK NPNGKCVYIA PLEPLCDIVY EKWELKFGKK
     MGKSVVILTG ETAVDLKLLA KGQVIISTPE KWDVLSRRWK QRKHVQNVGL YIADDLHFVG
     GENGPVYEVT CSRMRFMSTQ LDTPLRIVGL SVPLSNAKDV GQWLGCSSQN TFNFHPNVRP
     MPLEVHILGF NITHTASRLD AMAKQVYLSV LKHGGILRPK PMLVFVPTRK QAKVTAVDLL
     AFAAADAQPK RFLLVEATEL QPFIELINDE TLKETLSCGV GYLHEGISEN DRRTVERLFD
     VCAIQVLVAS RSMCYTLRTH AHGVVIMDTQ YYSGRHHTYE DYPIFDILQM IGKANRSDID
     EDAKCVLLCQ NSKKAFYKKF LFEPLPIESH LDHCLHDHFN AEVVTKTIEN KQEAIDYLTW
     TFLYRRMTQN PNYYNLQGIS HRHLSDHLSE LVEDTLNDLE QSKCLAIIND MDVQPLNLGI
     IAAYYSIHYT TIELFSMSLT SKTKIRGFLE IISNAAEFAN IPLRQKEDVV LSQLNEKIPN
     KIPNAKFSDP HVKTNLLIQA HLSRIQLPAE LQSDSDEIIL KAVRLIQAAV DVISTNGWLL
     PALAAMEFSQ MITQAMWNKE SYLKQLPHFS NELIKRCAEK GIETIFDIMD MEDEDRNQLL
     KLNQTEMSDV AKFCNRYPNI ELSFEVENRD SIISGQPVKI CCNLEREDEA VGSVLAPFFP
     KKKEESWWLL VGQPKQNLLT SIKRISLQQK TSTKLDFIAP EPGSKQYTLF FMTDSYLGCD
     QEYKFSIDIK GEPTAA
//
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