ERC6L_BOVIN
ID ERC6L_BOVIN Reviewed; 1242 AA.
AC A6QQR4; Q0V8L7;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 98.
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;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 705-1242.
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
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 -!- SUBUNIT: Interacts with PLK1, which phosphorylates it. Both proteins
CC are mutually dependent on each other for correct subcellular
CC localization. Interacts (via N-terminal TPR repeat) with BEND3 (via BEN
CC domains 1 and 3); the interaction is direct.
CC {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. In prometaphase cells, it mostly concentrates in
CC between kinetochores. In metaphase, it localizes to numerous thin
CC threads that stretch between sister kinetochores of the aligned
CC chromosomes and are composed of catenated centromeric DNA. Evolution
CC from inner centromeres to thin threads takes place in response to
CC tension. Resolution of thin threads requires topoisomerase 2-alpha
CC (TOP2A) after anaphase onset. {ECO:0000250|UniProtKB:Q2NKX8}.
CC -!- PTM: Phosphorylation by PLK1 prevents the association with chromosome
CC arms and restricts its localization to the kinetochore-centromere
CC region. {ECO:0000250|UniProtKB:Q2NKX8}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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DR EMBL; BC149963; AAI49964.1; -; mRNA.
DR EMBL; BT026201; ABG67040.1; -; mRNA.
DR RefSeq; NP_001096000.1; NM_001102530.2.
DR AlphaFoldDB; A6QQR4; -.
DR SMR; A6QQR4; -.
DR STRING; 9913.ENSBTAP00000007362; -.
DR PaxDb; A6QQR4; -.
DR PRIDE; A6QQR4; -.
DR Ensembl; ENSBTAT00000007362; ENSBTAP00000007362; ENSBTAG00000005607.
DR GeneID; 782916; -.
DR KEGG; bta:782916; -.
DR CTD; 54821; -.
DR VEuPathDB; HostDB:ENSBTAG00000005607; -.
DR VGNC; VGNC:28573; ERCC6L.
DR eggNOG; KOG0387; Eukaryota.
DR GeneTree; ENSGT00940000156837; -.
DR HOGENOM; CLU_004666_0_0_1; -.
DR InParanoid; A6QQR4; -.
DR OMA; FTIEDFQ; -.
DR OrthoDB; 372069at2759; -.
DR TreeFam; TF332843; -.
DR Proteomes; UP000009136; Chromosome X.
DR Bgee; ENSBTAG00000005607; Expressed in conceptus and 76 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; ISS:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
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; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
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.
PE 2: Evidence at transcript 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..1242
FT /note="DNA excision repair protein ERCC-6-like"
FT /id="PRO_0000328830"
FT REPEAT 21..54
FT /note="TPR 1"
FT DOMAIN 109..277
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 466..626
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REPEAT 1192..1225
FT /note="TPR 2"
FT REGION 1103..1181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 228..231
FT /note="DEAH box"
FT COMPBIAS 1103..1120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1128..1143
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1144..1161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 122..129
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2NKX8"
FT MOD_RES 755
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2NKX8"
FT MOD_RES 773
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2NKX8"
FT MOD_RES 815
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q2NKX8"
FT MOD_RES 963
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2NKX8"
FT MOD_RES 989
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2NKX8"
FT MOD_RES 998
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BHK9"
FT MOD_RES 1021
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2NKX8"
FT MOD_RES 1055
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q2NKX8"
FT MOD_RES 1061
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2NKX8"
FT MOD_RES 1090
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2NKX8"
FT MOD_RES 1110
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BHK9"
FT MOD_RES 1173
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2NKX8"
FT MOD_RES 1180
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2NKX8"
SQ SEQUENCE 1242 AA; 140510 MW; FF6F937D56CA8C6C CRC64;
MEVSRGFAEA GALSPEQAAS YLRYVKEAKE ATKNGDLEQA LKLFNLAKDI FPNEKVMSRI
QKIQEALEEL AEHGDDEFID VCNSGLLLYQ ELHNQLYEYQ KEGIAFLYSL YRDGRRGGIL
ADDMGLGKTV QIIAFLSGMF DASLVNHVLL IMPTSLISTW LREFVKWTPG MRVKTFHGPS
KDERTRNLCR IQQRNGVIIT TYQMLINNWQ QLSSLNGQEF LWDYVILDEA HKIKSSSTKS
AICARAIPAS NRILLTGTPI QNNLQELWSL FDFACQGSLL GTLRTFKMEY ENPITRAREK
DATPGEKALG FKISENLMAI IKPYFLRRTK EEVQKKKSSN PEVQLSEKSP DVGAICEMPS
LSRKNDLIIW IRLVPLQEEI YRKFVSLDHI KELLMETRSP LAELGVLKKL CDHPRLLSAR
ACGLLNLGAA KFSVQDEIEG EDSSDVDHID QISDDTLMEE SGKMLFLMDL LKKLRDEGHQ
TLVFSQSRRI LNIIERLLKN RHFKILRIDG TITHLVEREK RISLFQQNKD YSVFLLTTQV
GGVGLTLTAA SRVVIFDPSW NPATDAQAVD RVYRIGQKEN VVVYRLITCG TVEEKIYRRQ
VFKDSLIRQT TGDKKNPFRY FSKQELRELF TIEDFQNSAT QLQLQSLHAA QRRSDKNLDE
HIAFLHSLRI AGISDHDLMY TRDLSVKEEL DVIEDSHYIQ QRVQKAQFLV ESESQNTELL
MERQKMGNEG IWLREPVYQT KKKRPKVNKP QPQPSSHLPV YHTQEEISSL MASIIIDDLP
KEDEKDLSRI KLNDTIPQDG RHPCVITLND DFVTTLPKGC GDVEEIFPDS LSGMALQKEA
SQEGFMQESE QESPLASFNY LPSKSARVDL GPNLDQLEDD EVLHHCNPSP ANPKTKEYQR
PESNVSVIKI ADDDLTAAHS ALQDAQANEA KLEEEPLASS GQYACDFNLF LEDSADNGQN
LSSQFLEHVE KENSLCGSAA NSRAESVHSK ACLSVDLSEE DDEPEEVVNV KIRRKARRID
SDNEDEHTFK DTSSTNPFNT SPFPFLSVKQ FDASTPKNDI SLPERFFSPK ISDSINKSVN
SRRSLASRRS LINVVLDHVE DMEERLDNSS EAKVVEDHLE EGAEESGDEA PEHTKEDPSR
ETLSSENKSS QLSTSKPGAL AQETSPGDPE PLSDGQLVDS PQDEAMEAVN DYDTLVLHGK
ELKECGKIQE ALDCLVKALD IKSSDPEVML MTLSLYKQLN KT
