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Database: UniProt
Entry: A0A2K5LL61_CERAT
LinkDB: A0A2K5LL61_CERAT
Original site: A0A2K5LL61_CERAT 
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
//
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