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
//