ID A8X9E2_CAEBR Unreviewed; 1863 AA.
AC A8X9E2;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 2.
DT 27-MAR-2024, entry version 119.
DE SubName: Full=Protein CBR-LET-418 {ECO:0000313|EMBL:CAP29254.2};
GN Name=let-418 {ECO:0000313|WormBase:CBG09312};
GN Synonyms=Cbr-let-418 {ECO:0000313|EMBL:CAP29254.2};
GN ORFNames=CBG09312 {ECO:0000313|WormBase:CBG09312}, CBG_09312
GN {ECO:0000313|EMBL:CAP29254.2};
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238 {ECO:0000313|EMBL:CAP29254.2, ECO:0000313|Proteomes:UP000008549};
RN [1] {ECO:0000313|EMBL:CAP29254.2, ECO:0000313|Proteomes:UP000008549}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16 {ECO:0000313|EMBL:CAP29254.2,
RC ECO:0000313|Proteomes:UP000008549};
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
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DR EMBL; HE600954; CAP29254.2; -; Genomic_DNA.
DR STRING; 6238.A8X9E2; -.
DR WormBase; CBG09312; CBP16569; WBGene00030916; Cbr-let-418.
DR eggNOG; KOG0383; Eukaryota.
DR HOGENOM; CLU_000315_22_1_1; -.
DR InParanoid; A8X9E2; -.
DR OMA; KAKSRFM; -.
DR OrthoDB; 2910821at2759; -.
DR Proteomes; UP000008549; Unassembled WGS sequence.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0090571; C:RNA polymerase II transcription repressor complex; IEA:EnsemblMetazoa.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IEA:EnsemblMetazoa.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0048557; P:embryonic digestive tract morphogenesis; IEA:EnsemblMetazoa.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0040027; P:negative regulation of vulval development; IEA:EnsemblMetazoa.
DR CDD; cd18667; CD1_tandem_CHD3-4_like; 1.
DR CDD; cd18662; CD2_tandem_CHD3-4_like; 1.
DR CDD; cd15531; PHD1_CHD_II; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 2.40.50.40; -; 2.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR012957; CHD_C2.
DR InterPro; IPR009462; CHD_II_SANT-like.
DR InterPro; IPR012958; CHD_N.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR009463; DUF1087.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45623:SF13; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED; 1.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR Pfam; PF08074; CHDCT2; 1.
DR Pfam; PF06461; CHDII_SANT-like; 1.
DR Pfam; PF08073; CHDNT; 1.
DR Pfam; PF00385; Chromo; 1.
DR Pfam; PF06465; DUF1087; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00628; PHD; 2.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00298; CHROMO; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01146; DUF1086; 1.
DR SMART; SM01147; DUF1087; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF54160; Chromo domain-like; 2.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50013; CHROMO_2; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50016; ZF_PHD_2; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000008549};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 255..299
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 313..361
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 490..551
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 616..800
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 932..1095
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 146..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 562..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1176..1213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1242..1299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1423..1524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1730..1750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1777..1863
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 218..255
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..38
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..163
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..199
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1182..1197
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1198..1213
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1277..1295
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1434..1485
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1494..1524
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1777..1794
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1822..1836
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1838..1863
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1863 AA; 213282 MW; 3FEE7F104A8DCC6D CRC64;
MSAEEDTTIV EDESMEEGSV TQEATEETEE EEDQDQGDEA GPSDRRRSSR KKGGKGAKKA
SKKAAAAAAK AEIPDPYTAS SEEVCAAIGL TDVQFDYDLE EFQGITNLKN FSAVVKAQIL
EANPGTNVSK LYPMYQVKYK EYQDHMTAQG KPVQKQQRGS KTPAVATPVA PPRSAPTKTR
SARKKRRDSE APDSDQEFEN FIKQQEQLED DKVKEKEDAK VKRAVQKQEK KKEALEAARA
AKKAKLEQGE EVENNDFCET CKVGGELVLC DTCPRAYHTG CMDEDPPEGD WSCPHCIEHG
PEVIKEEPTK QNDDFCKICK ETENLLLCDS CVCAFHAYCI DPPLTQVPQE ETWACPRCEC
VKPEQKSEKI LCWRWKEISY PDPVPEGTVP TEDDALLKPP RKMAPRRERE FFIKWKYLSY
WQCSWVSEMM LEVHFRMVSS NFQYMMYFRR NDSEIPPEFE ESTASRHHSD NDPYKLREKY
YQFGVKPEWM QIHRIINHQS YAKSQQDYLV KWKELSYDAA TWERDDADIA NYEEAIIKYW
QHRERMLNDD VPKNVQKMIA KHREAKGLPP KEEESRRPKK REKVDIRKKY DVQPDYVSET
GGNLHPYQLE GINWLRHCWS NGTDAILADE MGLGKTVQSL TFLYTLMKEG HCKGPFLIAA
PLSTIINWER EAEQWCPDFY VVTYVGDRDS RVVLREHEFS FVDGAVRTGP KAGRMKTTDN
LKFHVLLTSY ETINMDKTIL SSIEWGALVV DEAHRLKNNQ SLFFKNLNEY TIHYRVLLTG
TPLQNNLEEL FHLLNFLSKE RFNQLEAFTA EFSEISKEDQ IEKLHNLLGP HMLRRLKADV
LTGMPSKSEL IVRVELSQMQ KKWYKNILTR NFDALNVKNG GTQMSLMNVL MELKKCCNHP
YLFVKASLEA PKEKNGMYEG TALIKNSGKF VLLQKMLRKL KDTGHRVLIF SQMTMMMDIL
EDFCDVEGYK YERIDGSITG QMRQDAIDRY NAPGAQQFVF LLSTRAGGLG INLATADTVI
IYDSDWNPHN DIQAFSRAHR LGQKHKVMIY RFVTKNSVEE RITTVAKKKM LLNHLVVRAG
LGGKEGKSMS KTELDDVLRW GTEELFKEDE AVAEGAEGAE GAEKKGTTQE IVWDDAAVDF
LLDRDKKEET GPGPEDGEGK ADWQNEYLSS FKVASYQTKE AEGQEEEEED EIEVMKEGDE
KEPDPDYWEK LLKHHYEQDK EIEAQKLGKG KRVRKQINYA SENMGTDWSK QNQPQEDDDD
NESYHGSDNG DPLNSDDDDY DEKRKKRRDE NNEKMPPLMA KVNGQVEILG FNPRQRKAFY
GAVMRWGMPP QDSHQSQWLV RDLRNKSEKV FRAYASLFMR HLCEPGADGH DTFNDGVPRE
GLNRQHVLGR IGLLSLVRRK VNEFEDFNGA WSMPEVQDEI LSKAANGSAE ESSRNSPKPK
DVKEEVKEEK EATPVTTQDE PMEKTDDAME STSEETPDAE KTSENTETAA EASAEEPVQK
DEPMETNAPV EEVKEEEKKP KAARPPFKFN ICDGGFTELH ALWTNEEKVA RNGREYEIWY
RRHDYWLLAG VMLHGYGRFQ ANFNDIINDP KFAILNEPFK EAGADAVISA DLKSKFMQRR
FKLLEQSLVI EEQLRRAAHA NRHLTPDNVG PLAQRFADLE NIAESQANIA KESAAGNRNA
NAVLHKCLVQ LDEILSDMKS DVSRLPATFT QLSSVTERLN MTERQILSRL TTKDEDAKAG
RTPIPPPGPF VTPVLRQQMD GIQPKFAALY SKFMSENGER MEEDEPVQAE PEDVPVKEEQ
EDGENADAGE TPPVLSKTTP KKEAKPHHKL NQKQIKPLNK KPRLSQSLNQ WRLNTHSQPL
LTP
//
