ID A0A2K5LL61_CERAT Unreviewed; 1495 AA.
AC A0A2K5LL61;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=ERCC excision repair 6, chromatin remodeling factor {ECO:0000313|Ensembl:ENSCATP00000013686.1};
GN Name=ERCC6 {ECO:0000313|Ensembl:ENSCATP00000013686.1};
OS Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Cercocebus.
OX NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000013686.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000013686.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC {ECO:0000256|ARBA:ARBA00007025}.
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DR RefSeq; XP_011927634.1; XM_012072244.1.
DR STRING; 9531.ENSCATP00000013686; -.
DR Ensembl; ENSCATT00000037827.1; ENSCATP00000013686.1; ENSCATG00000030946.1.
DR Ensembl; ENSCATT00000037831.1; ENSCATP00000013690.1; ENSCATG00000030946.1.
DR GeneID; 105591447; -.
DR GeneTree; ENSGT00940000158057; -.
DR OMA; VKHDAIM; -.
DR OrthoDB; 5488252at2759; -.
DR Proteomes; UP000233060; Unplaced.
DR Bgee; ENSCATG00000030946; Expressed in skeletal muscle tissue and 12 other cell types or tissues.
DR GO; GO:0110016; C:B-WICH complex; IEA:Ensembl.
DR GO; GO:0090734; C:site of DNA damage; IEA:Ensembl.
DR GO; GO:0008023; C:transcription elongation factor complex; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:Ensembl.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:Ensembl.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0003677; F:DNA binding; IEA:Ensembl.
DR GO; GO:0030296; F:protein tyrosine kinase activator activity; IEA:Ensembl.
DR GO; GO:0006284; P:base-excision repair; IEA:Ensembl.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; IEA:Ensembl.
DR GO; GO:0097680; P:double-strand break repair via classical nonhomologous end joining; IEA:Ensembl.
DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IEA:Ensembl.
DR GO; GO:0007254; P:JNK cascade; IEA:Ensembl.
DR GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
DR GO; GO:2001033; P:negative regulation of double-strand break repair via nonhomologous end joining; IEA:Ensembl.
DR GO; GO:0031175; P:neuron projection development; IEA:Ensembl.
DR GO; GO:0045494; P:photoreceptor cell maintenance; IEA:Ensembl.
DR GO; GO:0032786; P:positive regulation of DNA-templated transcription, elongation; IEA:Ensembl.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; IEA:Ensembl.
DR GO; GO:0045945; P:positive regulation of transcription by RNA polymerase III; IEA:Ensembl.
DR GO; GO:0060261; P:positive regulation of transcription initiation by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0006290; P:pyrimidine dimer repair; IEA:Ensembl.
DR GO; GO:0010332; P:response to gamma radiation; IEA:Ensembl.
DR GO; GO:0000303; P:response to superoxide; IEA:Ensembl.
DR GO; GO:0009636; P:response to toxic substance; IEA:Ensembl.
DR GO; GO:0010224; P:response to UV-B; IEA:Ensembl.
DR GO; GO:0010165; P:response to X-ray; IEA:Ensembl.
DR GO; GO:0000012; P:single strand break repair; IEA:Ensembl.
DR GO; GO:0006362; P:transcription elongation by RNA polymerase I; IEA:Ensembl.
DR GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; IEA:Ensembl.
DR CDD; cd21397; cc_ERCC-6_N; 1.
DR CDD; cd22254; CSB_WHD; 1.
DR CDD; cd18000; DEXHc_ERCC6; 1.
DR CDD; cd18793; SF2_C_SNF; 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 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 PANTHER; PTHR45629:SF7; DNA EXCISION REPAIR PROTEIN ERCC-6-RELATED; 1.
DR PANTHER; PTHR45629; SNF2/RAD54 FAMILY MEMBER; 1.
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; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000233060}.
FT DOMAIN 521..697
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 845..1004
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 346..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1044..1249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1321..1385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..398
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1082..1143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1144..1158
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1160..1176
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1177..1204
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1213..1249
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1333..1354
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1356..1377
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1495 AA; 168774 MW; E4FD76C785B2BFDD CRC64;
MPNEGIPHSS QTQEQDYLQS QPVSNNEEMA IKQESGGDGE VEEYLPFSSV GDGLSTSAEG
CASAAPRRGP ALLRINRHQI QAVEPSAQAL ELQGLGVDVY DQDVLEQGVL RQVDNAIHEA
SCTSQLADVE KEYRSVLDDL MSCTTSLRQI NKIIEQLSPQ AATSRDINRK LDSVKRQKYN
KEQQLKKITA KQKHLQAILG GAEVKIELDH ASLEEDAEPG PSSLGSMLMP VQETAWEELI
RTGQMTPFGT QIPQKQEKKP RKIMLNEASG FEKYLADQAK LSFERKKQAT CNKRPARKAP
ASVTPPAPTQ SKNKPNKKAK VLSKKEERLK KHIKKLQKRA LQFQGKVGLP KARRPWESDM
RPEAEGDSEG EESEYFPTEG EEEEEEDDEV EGVEADLSGD GTDYELKPLP KGRKRQKKVP
VQEIDDDFFP SSGEEAEASL IGEGGGGGRK VGRYRDDGDE DYYKQRLRRW NKLRLQDKEK
RLKLEDDSEE SDAEFDEGFK VPGFLFKKLF KYQQTGVRWL WELHCQQAGG ILGDEMGLGK
TIQIIAFLAG LSYSKIRTRG SNYRFEGLGP TVIVCPTTVM HQWVKEFHTW WPPFRVAILH
ETGSYTHKKE KLIRDVAHCH GILITSYSYI RLMQDDISRY DWHYVILDEG HKIRNPNAAV
TLACKQFRTP HRIILSGSPM QNNLRELWSL FDFIFPGKLG TLPVFMEQFS VPITMGGYSN
ASPVQVKTAY KCACVLRDTI NPYLLRRMKS DVKMSLSLPD KNEQVLFCRL TDEQHKVYQN
FVDSKEVYRI LNGEMQIFSG LIALRKICNH PDLFSGGPKN LKGLPDDELE EDQFGYWKRS
GKMIVVESLL KIWHKQGQRV LLFSQSRQML DILEVFLRAQ KYTYLKMDGT TTIASRQPLI
TRYNEDTSIF VFLLTTRVGG LGVNLTGANR VVIYDPDWNP STDTQARERA WRIGQKKQVT
VYRLLTAGTI EEKIYHRQIF KQFLTNRVLK DPKQRRFFKS NDLYELFTLT SPDASQSTET
SAIFAGTGSD VQTPKCHLKR KIQPAFGADH DVPKRKKFPA SNISINDATS SEEKSEAKGA
EVNVVPSNQS DPLKDDPHMS SNIASNDRLG EETNAVSGPE ESSVISGNGE CSNSSGTGKT
SRPSGDESID EKLGLSYKRE RPSQAQTESF WENKQMENNF YKHKSKTKHH SVAEEETLEK
HLRPKQKPKN PKHCRDAKFE GTRIPHLVKK RRYQKQDSEN KSEAKEQSND DYVLEKLFKK
SVGVHSVMKH DAIMDGANPD YVLVEAEANR VAQDALKALR LSRQRCLGAV SGVPTWTGHR
GISGAPAGTK SRFGKKRNSN FSVQHSSSTS PAEKCQDGIM KKEGKDNVPE HFSGRAEDTD
SSSGALASSS LLAKMRARNH LILPERLESE SGHLQEASAL LPTTEHDDLL VEMRNFIAFQ
AHTDGQASTR EILREFESKL SASQSCVFRE LLRNLCTFHR TSGGEGIWKL KPEYC
//