U520_CAEEL
ID U520_CAEEL Reviewed; 2145 AA.
AC Q9U2G0;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Putative U5 small nuclear ribonucleoprotein 200 kDa helicase;
DE EC=3.6.4.13 {ECO:0000250|UniProtKB:O75643};
GN Name=snrp-200 {ECO:0000312|WormBase:Y46G5A.4};
GN ORFNames=Y46G5A.4 {ECO:0000312|WormBase:Y46G5A.4};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Putative RNA helicase involved in the second step of RNA
CC splicing. {ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000250|UniProtKB:O75643};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O75643}.
CC -!- DOMAIN: Contains two helicase domains. The N-terminal helicase domain
CC has catalytic activity by itself, contrary to the C-terminal helicase
CC domain that may have a regulatory role and enhance the activity of the
CC first helicase domain. {ECO:0000250|UniProtKB:O75643}.
CC -!- SIMILARITY: Belongs to the helicase family. SKI2 subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL110485; CAB60351.1; -; Genomic_DNA.
DR RefSeq; NP_496710.1; NM_064309.3.
DR AlphaFoldDB; Q9U2G0; -.
DR SMR; Q9U2G0; -.
DR BioGRID; 40201; 19.
DR IntAct; Q9U2G0; 1.
DR STRING; 6239.Y46G5A.4; -.
DR EPD; Q9U2G0; -.
DR PaxDb; Q9U2G0; -.
DR PeptideAtlas; Q9U2G0; -.
DR EnsemblMetazoa; Y46G5A.4.1; Y46G5A.4.1; WBGene00012896.
DR UCSC; Y46G5A.4; c. elegans.
DR WormBase; Y46G5A.4; CE21971; WBGene00012896; snrp-200.
DR eggNOG; KOG0951; Eukaryota.
DR GeneTree; ENSGT00940000174511; -.
DR HOGENOM; CLU_000335_1_0_1; -.
DR InParanoid; Q9U2G0; -.
DR OMA; ESFWIIV; -.
DR OrthoDB; 154891at2759; -.
DR PhylomeDB; Q9U2G0; -.
DR Reactome; R-CEL-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-CEL-72165; mRNA Splicing - Minor Pathway.
DR PRO; PR:Q9U2G0; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00012896; Expressed in embryo and 4 other tissues.
DR GO; GO:0005681; C:spliceosomal complex; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0000388; P:spliceosome conformational change to release U4 (or U4atac) and U1 (or U11); IBA:GO_Central.
DR Gene3D; 1.10.10.10; -; 2.
DR Gene3D; 2.60.40.150; -; 2.
DR Gene3D; 3.40.50.300; -; 4.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041094; Brr2_helicase_PWI.
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 Pfam; PF00270; DEAD; 2.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF18149; Helicase_PWI; 1.
DR Pfam; PF02889; Sec63; 2.
DR SMART; SM00382; AAA; 2.
DR SMART; SM00487; DEXDc; 2.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00973; Sec63; 2.
DR SUPFAM; SSF46785; SSF46785; 2.
DR SUPFAM; SSF52540; SSF52540; 4.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 2.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding; Helicase; Hydrolase; mRNA processing; mRNA splicing;
KW Nucleotide-binding; Nucleus; Reference proteome; Repeat; Spliceosome.
FT CHAIN 1..2145
FT /note="Putative U5 small nuclear ribonucleoprotein 200 kDa
FT helicase"
FT /id="PRO_0000102088"
FT DOMAIN 484..667
FT /note="Helicase ATP-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 677..894
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 975..1278
FT /note="SEC63 1"
FT /evidence="ECO:0000255"
FT DOMAIN 1331..1506
FT /note="Helicase ATP-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1812..2124
FT /note="SEC63 2"
FT /evidence="ECO:0000255"
FT REGION 54..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 609..612
FT /note="DEAH box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOTIF 1448..1451
FT /note="DEAH box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 497..504
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 1344..1351
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 2145 AA; 243831 MW; 2C1EE0F69583891F CRC64;
MADELARIQQ YEYRQNSNLV LSVDYNLTDR RGREEPTGEV LPITDKEMRK MKMGDRAIKG
KAPVQDQKKK RKKKDDEKAQ QFGRNVLVDN NELMGAYKPR TQETKQTYEV ILSFILDALG
DVPREVLCGA ADEVLLTLKN DKFRDKEKKK EVEALLGPLT DDRIAVLINL SKKISDFSIE
EENKPEGDGD IYENEGVNVQ FDSDEEEDDG GMVNEIKGDS EEESEEEEGV DTDYTATLKG
DGHLTEDEQK ARGILHPRDI DAHWIQRSLA KYFKDPLIAQ QKQTEVIGIL KNAADDRDAE
NQLVLLLGFD QFEFIKCLRQ NRLMILYCTL LRQANEKERL QIEDDMRSRP ELHPILALLQ
ETDEGSVVQV EKSKRDAEKS KKAATAANEA ISAGQWQAGR KMLDLNDLTF SQGSHLMSNK
RCELPDGSYR RQKKSYEEIH VPALKPRPFA EGEKLVSVSE LPKWAQPAFD GYKSLNRIQS
RLCDSALRSK EHLLLCAPTG AGKTNVALLT MLQEIGNHLA EDGSVKLDEF KIVYIAPMKS
LVQEMVGSFS KRLAPFGITV GEMTGDAQMS KEQFMATQVI VCTPEKYDVV TRKGGERAYN
QMVRLLIIDE IHLLHDDRGP VLESIVVRTI RQMEQNHDEC RLVGLSATLP NYQDVATFLR
VKPEHLHFFD NSYRPVPLEQ QYIGVTEKKA LKRFQAMNEV VYDKIMEHAG KSQVLVFVHS
RKETAKTAKA IRDACLEKDT LSAFMREGSA STEILRTEAE QAKNLDLKDL LPYGFAIHHA
GMNRVDRTLV EDLFADRHIQ VLFSTATLAW GVNLPAHTVI IKGTQIYNPE KGRWTELGAL
DIMQMLGRAG RPQYDDRGEG ILITNHSELQ YYLSLMNQQL PVESQMVSRL TDMLNAEVVL
GTVSSVSEAT NWLGYTFLFV RMLKNPTLYG ITHEQARADP LLEQRRADLI HTACVLLDKA
GLIKYDKRSG IIQATELGRI ASHFYCTYES MQTYNKLLVE TCSDIDLFRI FSMSSEFKLL
SVRDEEKLEL QKMAEHAPIP IKENLDEASA KTNVLLQAYI SQLKLEGFAL QADMVFVAQS
AGRLFRALFE IVLWRGWAGL AQKVLTLCKM VTQRQWGSLN PLHQFKKIPS EVVRSIDKKN
YSFDRLYDLD QHQLGDLIKM PKMGKPLFKF IRQFPKLEMT TLIQPITRTT MRIELTITPD
FKWDEKVHGS AEGFWIFIED TDGEKILHHE FFLLKQKFCS DEHVVKMIVP MFDPMPPLYY
VRIVSDRWIG AETVLPISFR HLILPEKYPP PTELLDLQPL PISAVTNKEF QTVFAESGFK
VFNPIQTQVF RTVFESNENV IVCAPNGSGK TAIAELAVLR HFENTPEAKA VYITPMEDMA
TKVYADWKRR LEPAIGHTIV LLTGEQTMDL KLAQRGQLII STPERWDNIS RRWKQRKSVQ
NVKLFIADDL HMIGASNGAV FEVVCSRTRY ISSQLESAVR VVALSSSLTN ARDLGMWLGC
SASATFNFMP STRPVPLDLE IKSFNLSHNA SRFAAMERPV YQAICRHAGK LEPKPALVFV
PVRRQTRPVA VALLTMALAD GAPKRFLRLA EHDDTFQALL ADIEDESLRE SVSCGVGFLH
EGTAPKDVHI VQQLFESNAI QVCVVPRGMC YQIEMSAYLV VVMDTQFYNG KYHVYEDYPI
ADMLHMVGLA NRPILDSDAK CVVMCQTSKR AYYKKFLCDP LPVESHLDHC LHDHFNAEIV
TKTIENKQDA IDYLTWTLLY RRMTQNPNYY NLQGTTHRHL SDALSELVEL TLKDLENSKC
IAVKDEMDTV SLNLGMIASY YYISYQTIEL FSMSLKEKTK TRALIEIISA SSEFGNVPMR
HKEDVILRQL AERLPGQLKN QKFTDPHVKV NLLIHAHLSR VKLTAELNKD TELIVLRACR
LVQACVDVLS SNGWLSPAIH AMELSQMLTQ AMYSNEPYLK QLPHCSAALL ERAKAKEVTS
VFELLELEND DRSDILQMEG AELADVARFC NHYPSIEVAT ELENDVVTSN DNLMLAVSLE
RDNDIDGLAP PVVAPLFPQK RKEEGWWLVI GDSESNALLT IKRLVINEKS SVQLDFAAPR
PGHHKFKLFF ISDSYLGADQ EFDVAFKVEE PGRSNRKRKH EKEED
