ER6L2_BOVIN
ID ER6L2_BOVIN Reviewed; 1558 AA.
AC A3KMX0;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-MAY-2014, sequence version 3.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=DNA excision repair protein ERCC-6-like 2;
DE EC=3.6.4.-;
GN Name=ERCC6L2;
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 GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19390049; DOI=10.1126/science.1169588;
RG The bovine genome sequencing and analysis consortium;
RT "The genome sequence of taurine cattle: a window to ruminant biology and
RT evolution.";
RL Science 324:522-528(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1041-1558.
RC STRAIN=Hereford; TISSUE=Brain cortex;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May be involved in early DNA damage response. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with NEK6. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome {ECO:0000250}. Mitochondrion
CC {ECO:0000250}. Note=Colocalizes with NEK6 in the centrosome. In
CC response to DNA damage, translocates from the cytosol to mitochondria
CC and nucleus in a reactive oxygen species (ROS)-dependent manner.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI33355.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AAFC03040861; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAFC03121441; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAFC03040862; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC133354; AAI33355.1; ALT_INIT; mRNA.
DR AlphaFoldDB; A3KMX0; -.
DR SMR; A3KMX0; -.
DR STRING; 9913.ENSBTAP00000027486; -.
DR PRIDE; A3KMX0; -.
DR eggNOG; KOG0387; Eukaryota.
DR InParanoid; A3KMX0; -.
DR OrthoDB; 372069at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR029256; Heliccase-ass-bd.
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 Pfam; PF14773; VIGSSK; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cytoplasm; Cytoskeleton; DNA damage; DNA repair; DNA-binding;
KW Helicase; Hydrolase; Mitochondrion; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..1558
FT /note="DNA excision repair protein ERCC-6-like 2"
FT /id="PRO_0000338970"
FT DOMAIN 147..332
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 523..673
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 930..961
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1291..1326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1373..1394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 283..286
FT /note="DEAH box"
FT COMPBIAS 9..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 940..961
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1293..1315
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 160..167
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 989
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIM3"
FT MOD_RES 992
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIM3"
FT MOD_RES 1382
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T890"
FT MOD_RES 1385
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T890"
SQ SEQUENCE 1558 AA; 176299 MW; 4DF06537AB374A80 CRC64;
MQPGCQALPP GQMDQSTPKP HAETNSKDIW HPGERCLAPS PDNEKLCEAS IKSITVDENG
KSFAVILYSN FQERRVPLKR LQEVKSVKDC SRNFIFDDED LEKPYFPDRK FPSSAVPFQL
SENGDSIPYT INRYLRDYQR EGAQFLYGHF IQGRGCILGD DMGLGKTVQV ISFLAAVLGK
KGTREDIENN MPEFLLRNMK KDPPSTAKKM FLIVAPLSVL YNWKDELDTW GYFRVTILHG
NKKDSELIRV KQRKCEIALT TYETLRLCLD ELNSLEWSAV IVDEAHRIKN PKARVTEIMK
ALRCNVRIGL TGTILQNNMK ELWCVMDWAV PGLLGSRIHF KKQFSDPVEH GQRHTATKRE
LATGRKAMQR LARKMSGWFL RRTKTLIKDQ LPKKEDRMVY CSLTDFQKAV YQTVLETEDV
SLILQSSEPC TCNSGQKRRN CCYKTNSQGE TVKTLYFSYL AVLQKVANHV ALLQTASTSR
QQETLIKRIC DQVFSRFPDF VQKSKDAAFE TLSDPKYSGK MKVLQQLLNH CRKNKDKVLL
FSFSTKLLDV LQQYCMASGL DYRRLDGSTK SEERIKIVKE FNSTQDVNIC LVSTMAGGLG
LNFVGANVVV LFDPTWNPAN DLQAIDRAYR IGQCRDVKVL RLISLGTVEE IMYLRQVYKQ
QLHCVVVGSE NAKRYFEAVQ GSKEHQGELF GVYNLFKLRS QGSCLTRDIL EREGKVEAGI
MTATTWLKEE PPVHKLETAR EPDCREHRGP EQLAEAACDL CSDFSEDETA SNSVTKTVKN
KASDSSRASV SPGQFSLLQC GFSKLFETKC ETVEDGDENI ASDNESSDEQ PTCFSTEAKN
AGCQKSQDSL GTLKHQKLAN VLNPNGKCVF EKSEKILKEN IPSESDDEKN FKNTVDHHHI
LQNVTESEDS DIIFPTQYTT QRFLKKNIRF KPPVDGSEDS ESENPVNIKN NGDDTKTNVR
GNGLISKQLN LEIETLKSNT KRKGGSDISD ESDDIEVFCK SRVRKQRATS SLRFKRKKEN
KRELYTFPKT MKKANQQCAT DEDCNSQTID DFSSSDDNLS VGHISFSKQN HRPKTIKDKI
SVSSKLTNHK RNSTFIPRKP MKFSNESVVN QNRICESMDK FLDGVQEVAY IHSNQNVIGS
SKAENHMSRW AARDVFELKQ FSQLPANIAV CTSKTHKEKM KGDISTRTKE CQPLSEGSIS
FPLYISHPVS QKKKKVCRID QTTFIIGETP KGIRRKQFEE MASYFKLSSV KEFAKRVTNA
TSEERQKMLR DFYTSQYPEV REFFVDSPSE CTKSASEKGE RVENKSEKRQ SLMKEQPSDS
ETLSFKNSTK KISPIFSPSI CKKKSIKFQN HSSCKKKVLS NDVETKKLPI SCTQETDGGE
RSQASEGTAA SCSLNSKSGA DELGKLENAG KGQQDLTSLG ISRNGPIFQV ENKTIENPVL
EDTSVVGLLG DTSILDDLFK SHENSPTQLP KKVLSGSIEK AKQRPKDFWD ILNDQNDDSL
SKLTDLAVIE TLCEKVPFAA SSKRKEDLEA SLWKSNEKFL WKKFNSSDTD ESTANTQE
