YP93_CAEEL
ID YP93_CAEEL Reviewed; 1714 AA.
AC Q09475;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 06-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Uncharacterized helicase C28H8.3;
DE EC=3.6.4.-;
GN ORFNames=C28H8.3;
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
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; FO080703; CCD65963.1; -; Genomic_DNA.
DR PIR; A88470; A88470.
DR RefSeq; NP_498283.1; NM_065882.4.
DR AlphaFoldDB; Q09475; -.
DR BioGRID; 41056; 4.
DR STRING; 6239.C28H8.3; -.
DR iPTMnet; Q09475; -.
DR EPD; Q09475; -.
DR PaxDb; Q09475; -.
DR PeptideAtlas; Q09475; -.
DR EnsemblMetazoa; C28H8.3.1; C28H8.3.1; WBGene00016194.
DR GeneID; 175834; -.
DR KEGG; cel:CELE_C28H8.3; -.
DR UCSC; C28H8.3.1; c. elegans.
DR CTD; 175834; -.
DR WormBase; C28H8.3; CE29195; WBGene00016194; -.
DR eggNOG; KOG0949; Eukaryota.
DR HOGENOM; CLU_002305_0_0_1; -.
DR InParanoid; Q09475; -.
DR OMA; EVHCISA; -.
DR OrthoDB; 546283at2759; -.
DR PhylomeDB; Q09475; -.
DR PRO; PR:Q09475; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00016194; Expressed in larva and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 2.
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 Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1..1714
FT /note="Uncharacterized helicase C28H8.3"
FT /id="PRO_0000102096"
FT DOMAIN 793..963
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1237..1391
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 47..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 584..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1197..1223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 913..916
FT /note="DEVH box"
FT COMPBIAS 1197..1215
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 607..614
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 806..813
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1714 AA; 194097 MW; 0936764D27C7EFAD CRC64;
MSANAAWDDS DSENENVVVE EKPVILPRAR QPSIAKSLEK VQILENSVAG SEKNASDDDS
DASSVMSDDL ESLGETTEVL NFSLEQLSMM KKNLAQFPCS YKNIISEFAD VEIFLISIDS
LIVECAAHSY HNWDVAGQSM VLNKQIDRFL QQFVDIGGRF KLVVFSDLTT QFAKDTTLSF
ARSTALAHLA NGPHARDLLF FTNPTDPEWD KLLNDLTPSF LMISTDNVTQ NVCASQEIDL
TKQFETIAFD VLTRSMSVVL LHSIKVNFVS VEAYYIQPLL VVAPDWQAFL AAHWDNNGTL
LRNHLSKEIK FNQFETPADL WVKVITDAKA TGKGSDTFDT LAAAVILSSL ICSRRGAHRI
YYPTRTDAKR GLNVIRDRRL ILNAAVVLLD KADHANSKLD LSDLWDGRMV YSIFDELSAN
ETVLPYRLQD DFAKYHQKAG LTVPLATDTN EKLFDPIPEI TDPLVDLPIL YSVTSPMIKR
FVPEIEKMTS QNAVEEGTVQ DYADYLKDTS QWRLKPIEET YAQKEEKIED AWQLKKANRS
KQFLMRWYEL FANSLEGRGS NLLVDFSRVP KGYAVVEEEV TDEKKTGKGG WSGQKQQKPG
AGGKKGATKE SGKSKKDLIL EANKKAKDQK VAESEKVKIK YGCQQGKESV IFLNNLYSSL
DLPETRALCV YEIAVREGRT IFDQHQGTDK QEVRRNAAID LVGHLKDCFV KHWDHLESKQ
KEQIVDLWVS LGFEAPAGSK PSSEAKQKKL NLGINMVYYQ LQYGGELIDI QSDPKKDDRV
SGFAPDGWQR KMLDSVDRGN SALIIAPTSA GKTFVSYYCI EKVLRSSDND VVVYVAPSKA
LINQVCGSVY ARFRNKSMKR GISLFGTLTQ EYSQNAMQCQ VLITVPECLQ ELMLSRTPAV
QKFVSHIKYV VFDEVHSIGA SEESHIWEQL LLLIQCPFLA LSATIGNANK LHEWLNSSEQ
AKSAGKRKVE LINYGERYSE LELSILNIND PHGEDDGAVH KKAGERAVIP LMPYGVYMPE
KLRMFSIPED QQLTARQVLH LYNMMAEVDD ATKKEFEPCK FFGQHGTKAV WISRSELRRL
ENALKERFME WLSSDEQKIN SILKILKEPV NTQLSYRARP FNKEKIANDY IVTLVDDLKE
KGELPAICFN DDRHVCEKLA VTLANELERR ELEYMETDEF KNKYMIKDES KLVKLAKRKR
DDAEKKKKGD KDEDAGPEKD DDEMDVLAMK KAKLARALER FKLRGRNGGD PDIYAKMVER
MQKGAKTRES TQVLLKLFER GIGYHHAGLN TVERGAVEVL FRSGNLAVLF STSTLSLGVN
MPCKTVMFGV DTLQLTPLLY RQMSGRAGRR GFDHSGNVIF MSIPTSKVRR LLTASLSNLQ
GNPPFTVLFL LRLFAYVHQQ DILNEEGQKV STMKQRAFAA KSLLEHSFSI HTRREAQDGI
LQKQLRMFSA FSFQLLRHLQ LLSPFGEGKN FAEMAIHSSS GANGTLLFIY LMQKKCFHQL
IKSYDTAEQA QLGILEVLAN LFTNLRMTPF HERSDNLENV QVTLRGLPSL LKPYVEEYNS
TVTGLYKRFM AASSQDGNLF DPSFAVSGKL DSESVSLTED FLVAPLFDQY SHDESFLPVI
DFNKKDHRGR KIQRNAFAYD FYVHGSRNML MDVNGLHVSV AWFLLHDFAA ILERLAIGVH
NMARPQDPLV LVLEELHKNY DEKFRKAFGM RTRD