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Database: UniProt
Entry: A0A0V0XFW9_TRIPS
LinkDB: A0A0V0XFW9_TRIPS
Original site: A0A0V0XFW9_TRIPS 
ID   A0A0V0XFW9_TRIPS        Unreviewed;      1917 AA.
AC   A0A0V0XFW9;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=U5 small nuclear ribonucleoprotein 200 kDa helicase {ECO:0000256|ARBA:ARBA00034541};
GN   Name=Snrnp200 {ECO:0000313|EMBL:KRX86945.1};
GN   ORFNames=T4E_1752 {ECO:0000313|EMBL:KRX86945.1};
OS   Trichinella pseudospiralis (Parasitic roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=6337 {ECO:0000313|EMBL:KRX86945.1, ECO:0000313|Proteomes:UP000054815};
RN   [1] {ECO:0000313|EMBL:KRX86945.1, ECO:0000313|Proteomes:UP000054815}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS141 {ECO:0000313|EMBL:KRX86945.1};
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:KRX86945.1}.
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DR   EMBL; JYDU01000321; KRX86945.1; -; Genomic_DNA.
DR   Proteomes; UP000054815; 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; cd18019; DEXHc_Brr2_1; 1.
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; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
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; 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; 2.
DR   SMART; SM00382; AAA; 2.
DR   SMART; SM00487; DEXDc; 2.
DR   SMART; SM00490; HELICc; 2.
DR   SMART; SM00973; Sec63; 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:KRX86945.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054815};
KW   Ribonucleoprotein {ECO:0000313|EMBL:KRX86945.1}.
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          54..85
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   COMPBIAS        54..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   1917 AA;  220138 MW;  9AAA63EE63B1C803 CRC64;
     MADAAARELQ YEYKANSNLV LQVDYSLIDR RPKDEATGEV LPLNADRLRG IKMGDKFYRS
     KPPMPDEKKP KKSKKEKSHK ESLKLKKHGL FSDSDDFVGV YKPKTQETRQ TYDVILAFIQ
     EAIGDQPRDI LCGAADEVLA TMKSDKIRDK ERKHEVELLL GPLTDERFAL LLNLGKKITD
     YSLPNENKKT TGFEGDIENS YGVNVQFEES DAEDDEEVDD EIRDDSENDD EGEDTLAGST
     LKASGLVEEF SIEEEQKKEL HPRDIDAYWL QRSLGKFYQD PIVAQQQSRE VLEILKMAVD
     DRDCENRLVR LLGFDQFDFI RTLRQHRNMI LYCTLMASAQ SEKERQQIEA ILLETPELTK
     ILHALKEADA EDFIEQERGR RRKVKTEIHS TDKNMEVDDS GWCQQRQFLD FDDLIFAQGS
     HFMSNKRCQL PDGSFRKQRK GYEEVHVPAL KPRPFDSDER LIKIEELPEF AQAAFGSFKT
     LNRIQSKLVK VALENDSNLL LCAPTGAGKT NVALLCILRE ISKHVNADGT INVEDFKVVY
     VAPMRSLVQE MVGNFTTRLA PYKLKVGELT GDHQLTQEEI AQSQVIVCTP EKFDIITRKG
     LERSFVQLVR VVIFDEIHLL HDDRGPVLEA LVARVIRNME QTQEHVRLVG LSATLPNYED
     VGTFLRVEKA NVFFFDNSYR PVPLEQEYIG VTEKKAMKRF QIMNEVVYDK VLQHAGRSQI
     LIFVHSRKET GKTARSLRDL CLERDTLSMF MREGSASTEI LRREADQVKN SELKDLLPYG
     FAIHHAGMTR VDRTLVEDLF ADRHIQVLVS TATLAWGVNL PAHTVIIKGT QIYNPEKGRW
     VELGALDIMQ MMGRAGRPQY DTKGKGIMIT NHTELQYYLS LMNQQLSVES QMISKLADCL
     NAEIVLGTVN NVREAVDWLA YTYLYIRMLR APTLYGISHD EVKNDPLLEQ RRADLIHTAA
     TLLDKCNMIK YERRSGIFQV TELGRIASYF YCTHETIHTY NQLLKPVMTE IELLRVFSLS
     SEFKNIMVRE EEKLELLKLA ERVPIPIKEN LEEPSAKVNV LFQAYISQLK LEGFALQSDM
     VYVSQSAGRL FRAIYEIVLF RSWAQLAQKT LSMCKMVERK MWQSMCPLRQ FKKLPDEIVR
     KIEKKNFSFE RLHDLEPNEL GELIRIPKMG KLLHRFIHQA ISQAGTDYPY PTDNTINTAC
     FWVFVEDVDC ERILHYEYFL LKQKFAEDEH TLKFFVPVFD PMPILYYIHI VSDKWLGAET
     ILPVSFRHLI LPEKYPPPTE LLDLQPLPVS ALNNTDLEEL YTDEIKSFNP IQTQVFRVFY
     ENKDNVFVGA PHGSGKTICA ELAILQLFKK NPNGKCVYIA PLEPLCDIVY EKWELKFGKK
     MGKCVVILTG ETAVDLKLLA KGQVIISTPE KWDVLSRRWK QRKHVQNVGL YIADDLHFVG
     GENGPVYEVT CSRMRFMSTQ LDTPLRIIGL SVPLSNAKDV GQWLGCSSQN TFNFHPNVRP
     MPLEVHILGF NITHTASRLD AMAKQVYLSV LKHGGILRPK PMLVFVPTRK QTKVTAVDLL
     AFAAADAQPK RFLLVEATEL QPFIELINDE TLKETLSCGV GYLHEGISEN DRRTVERLFD
     VCAIQVLVAS RSMCYILRTH AHGVVIMDTQ YYSGRNHTYE DYPIYDILQM IGKANRSNID
     EDAKCVLLCQ NSKKAFYKKF LFEPLPIESH LDHCLHDHFN AEVVTKTIEN KQEAIDYLTW
     TFLYRRMTQN PNYYNLQGVS HRHLSDHLSE LVEDTLNDLE QSKCLAIIND MDVQPLNLGI
     IAAYYSIHYT TIELFSMSLT SKTKIRGFLE IISNAAEFAN IPLRQKEDVV LSQLNEKIPN
     KIPNAKFSDP HVKTNLLIQA HLSRIHLPAE LQSDSDEIIL KVLHRQIPQV CLLLMSL
//
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