ERC6L_DANRE
ID ERC6L_DANRE Reviewed; 1451 AA.
AC A2BGR3; A7E225;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=DNA excision repair protein ERCC-6-like;
DE EC=3.6.4.12 {ECO:0000250|UniProtKB:Q2NKX8};
DE AltName: Full=ATP-dependent helicase ERCC6-like;
GN Name=ercc6l; ORFNames=si:ch211-278b8.3;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-579.
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-961, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18307296; DOI=10.1021/pr700667w;
RA Lemeer S., Pinkse M.W.H., Mohammed S., van Breukelen B., den Hertog J.,
RA Slijper M., Heck A.J.R.;
RT "Online automated in vivo zebrafish phosphoproteomics: from large-scale
RT analysis down to a single embryo.";
RL J. Proteome Res. 7:1555-1564(2008).
CC -!- FUNCTION: DNA helicase that acts as a tension sensor that associates
CC with catenated DNA which is stretched under tension until it is
CC resolved during anaphase. Functions as ATP-dependent DNA translocase.
CC Can promote Holliday junction branch migration (in vitro).
CC {ECO:0000250|UniProtKB:Q2NKX8}.
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=3.6.4.12;
CC Evidence={ECO:0000250|UniProtKB:Q2NKX8};
CC -!- SUBCELLULAR LOCATION: Chromosome, centromere
CC {ECO:0000250|UniProtKB:Q2NKX8}. Chromosome, centromere, kinetochore
CC {ECO:0000250|UniProtKB:Q2NKX8}. Chromosome
CC {ECO:0000250|UniProtKB:Q2NKX8}. Note=Localizes to kinetochores, inner
CC centromeres and thin threads connecting separating chromosomes even
CC during anaphase. {ECO:0000250|UniProtKB:Q2NKX8}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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DR EMBL; CR391924; CAM13192.1; -; Genomic_DNA.
DR EMBL; BX510925; CAM13192.1; JOINED; Genomic_DNA.
DR EMBL; BX510925; CAM14199.1; -; Genomic_DNA.
DR EMBL; CR391924; CAM14199.1; JOINED; Genomic_DNA.
DR EMBL; BC150168; AAI50169.1; -; mRNA.
DR RefSeq; NP_001093563.1; NM_001100093.2.
DR RefSeq; XP_009299551.1; XM_009301276.2.
DR AlphaFoldDB; A2BGR3; -.
DR SMR; A2BGR3; -.
DR STRING; 7955.ENSDARP00000012447; -.
DR iPTMnet; A2BGR3; -.
DR PaxDb; A2BGR3; -.
DR PeptideAtlas; A2BGR3; -.
DR PRIDE; A2BGR3; -.
DR Ensembl; ENSDART00000015401; ENSDARP00000012447; ENSDARG00000002479.
DR GeneID; 100005291; -.
DR KEGG; dre:100005291; -.
DR CTD; 54821; -.
DR ZFIN; ZDB-GENE-060531-56; ercc6l.
DR eggNOG; KOG0387; Eukaryota.
DR GeneTree; ENSGT00940000156837; -.
DR HOGENOM; CLU_004666_0_0_1; -.
DR InParanoid; A2BGR3; -.
DR OMA; HDGESEM; -.
DR OrthoDB; 372069at2759; -.
DR PhylomeDB; A2BGR3; -.
DR TreeFam; TF332843; -.
DR Reactome; R-DRE-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-DRE-2467813; Separation of Sister Chromatids.
DR Reactome; R-DRE-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-DRE-5663220; RHO GTPases Activate Formins.
DR Reactome; R-DRE-9648025; EML4 and NUDC in mitotic spindle formation.
DR PRO; PR:A2BGR3; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 5.
DR Bgee; ENSDARG00000002479; Expressed in blastula and 28 other tissues.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0015616; F:DNA translocase activity; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR006141; Intein_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50005; TPR; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Cell division; Centromere; Chromosome;
KW DNA-binding; Helicase; Hydrolase; Kinetochore; Mitosis; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Repeat; TPR repeat.
FT CHAIN 1..1451
FT /note="DNA excision repair protein ERCC-6-like"
FT /id="PRO_0000328833"
FT REPEAT 27..60
FT /note="TPR 1"
FT DOMAIN 118..286
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 479..639
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REPEAT 1402..1435
FT /note="TPR 2"
FT REGION 647..669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 778..804
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 935..1006
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1035..1054
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1063..1083
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1096..1140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1182..1343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 237..240
FT /note="DEAH box"
FT COMPBIAS 648..665
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 781..804
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 947..980
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1107..1121
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1202..1230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1241..1301
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1313..1343
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 131..138
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 961
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18307296"
FT CONFLICT 45
FT /note="R -> H (in Ref. 2; AAI50169)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="T -> A (in Ref. 2; AAI50169)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1451 AA; 163227 MW; 4BE27ACF410D1EDB CRC64;
MESNNVEEVT DKFGGCLSLD TEKMGKYDRY RQKGKEAALN GELPRALELF QLAYQLQPSE
KLKKRIQAIQ DLIQREDEED EEEEEEFVNV NNSGLKLYKG LYDKLYDHQK EGVAFLYSLY
RDGRKGGILA DDMGLGKTIQ VISFLSGMYD AELANHTLLV MPTSLIKNWV REFAKWTPGM
RVKEFHGSSK TERNRNLERI QRKGGVIITT YQMLINNYEQ LGSNGHREFK WDYVILDEAH
KIKTSSTKTA KSAHAIPAKN RVLLTGTPVQ NNLREMWALF DFACQGSLLG TSKTFKTEYE
NPITRAREKD ATPGEKALGL RISQNLTDII KPYFLRRTKA DVQQKKLKLE EGFEEEEDQE
NKCPNAREGV EMPSLTRKND LIVWTYLSSV QEDIYNKFIS LDQIKELLTT TRSPLAELTV
LKKLCDHPRL LSQRAVIQLG LERGSDSELV HSDESESAVS QIDNISDHTL IEESGKLQFV
VSLMECLREE GHRTLIFSQS RKMLDIMERV LRNRNFRLLR LDGTVTQLAE REKRISLFQT
DKRYTIFLLT TQVGGVGITL TGANRVVIFD PSWNPATDAQ AVDRAYRIGQ TENVIIYRLI
TCGTVEEKIY RRQVFKDSLI RQTTGDKKNP FRYFSKQELR ELFKLEDTRS SSTQQQLQAM
HAQSRRSDTS LDHHIARLHS MEMFGISDHD LMFTKEPAAD EDDPEDAESH HYIQTRVQKA
QELMQAESEL HGQLLDSMAQ NTEPAWLRQM GQPNSSIRDR PAPPRIKNEP VTVDLTHNSF
DEPEFEEDEQ NLPSAEDAEM ETASEDVEVI GDEDLGDKVI SSEVEVVGEE VEVVAEEVED
AGEVEVVSEE VEGVGVEVED VGVEVEDAGV EVEDAGVEVE DAGVEVEDAG EVEVVSGEGQ
VQPKSPQSGG EWNLQIVKTE VSPIAEKFAD VITLDDTSDE ADSSDFNTES KQQNSSQRFQ
SPSLQFPKLD DLSGASNTLG NEEVEPEKCH SQVLSSPLSQ HEATTDEPFK AEMEMPHGNF
NLLLEDSADM YFPEDEEVHE VEESAAEESP EFQLQMDVSG ERLEEPSINH DKQNNGEFVN
YNDSEVSKRE SLLKIRSTPN ESVDDSFVHS VRTKKRQVIS DTEEEEEEEE ESEKPCLTSS
PFIDAISRLG SSTPKAVLVD GARLRRSLNA SVASRRSFVV SLLENESDEE SNEDKTKSSG
ASETCADELV EEVQTSSGDN SKSYETSEAN GTLADELVEE EGEYREGKNT SDKVSESNET
HSEEFAEEEK PSGDKSESYE ISEASETHTD NSEEEIIGDH TGSYKISESS EADESVVEEE
EPSGETLNTE ESEMGEEEES AELIAGQEQE EWHSAVLEST GDVELDSNET MDQCAPKTVP
VETHVLPVSS TNTAAEASDN KYNLLVLSGK QSLAEGRKQE ALDFFLKAID INTGDPEIQL
LIIQLYRQLS Q
