ID F7EMA8_MACMU Unreviewed; 2061 AA.
AC F7EMA8;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 3.
DT 24-JAN-2024, entry version 56.
DE SubName: Full=ERCC excision repair 6, chromatin remodeling factor {ECO:0000313|Ensembl:ENSMMUP00000023587.4};
GN Name=ERCC6 {ECO:0000313|Ensembl:ENSMMUP00000023587.4,
GN ECO:0000313|VGNC:VGNC:81396};
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544 {ECO:0000313|Ensembl:ENSMMUP00000023587.4, ECO:0000313|Proteomes:UP000006718};
RN [1] {ECO:0000313|Ensembl:ENSMMUP00000023587.4, ECO:0000313|Proteomes:UP000006718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000023587.4,
RC ECO:0000313|Proteomes:UP000006718};
RX PubMed=17431167; DOI=10.1126/science.1139247;
RA Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M.,
RA Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C., Wilson R.K.,
RA Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W., Hardison R.C.,
RA Makova K.D., Miller W., Milosavljevic A., Palermo R.E., Siepel A.,
RA Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J.,
RA Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y., Dinh H.H.,
RA Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T., Godfrey J.,
RA Hawes A.C., Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N.,
RA Joshi V., Khan Z.M., Kirkness E.F., Cree A., Fowler R.G., Lee S.,
RA Lewis L.R., Li Z., Liu Y.-S., Moore S.M., Muzny D., Nazareth L.V.,
RA Ngo D.N., Okwuonu G.O., Pai G., Parker D., Paul H.A., Pfannkoch C.,
RA Pohl C.S., Rogers Y.-H.C., Ruiz S.J., Sabo A., Santibanez J.,
RA Schneider B.W., Smith S.M., Sodergren E., Svatek A.F., Utterback T.R.,
RA Vattathil S., Warren W., White C.S., Chinwalla A.T., Feng Y., Halpern A.L.,
RA Hillier L.W., Huang X., Minx P., Nelson J.O., Pepin K.H., Qin X.,
RA Sutton G.G., Venter E., Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P.,
RA Jones S.M., Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L.,
RA Csuros M., Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H.,
RA Liu Y., Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E.,
RA Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J.,
RA Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J.,
RA Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A.,
RA Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J., Denby A.,
RA Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A., Marklein A.,
RA Nielsen R., Vallender E.J., Clark A.G., Ferguson B., Hernandez R.D.,
RA Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S., Pu L.-L., Ren Y.,
RA Smith D.G., Wheeler D.A., Schenck I., Ball E.V., Chen R., Cooper D.N.,
RA Giardine B., Hsu F., Kent W.J., Lesk A., Nelson D.L., O'brien W.E.,
RA Pruefer K., Stenson P.D., Wallace J.C., Ke H., Liu X.-M., Wang P.,
RA Xiang A.P., Yang F., Barber G.P., Haussler D., Karolchik D., Kern A.D.,
RA Kuhn R.M., Smith K.E., Zwieg A.S.;
RT "Evolutionary and biomedical insights from the rhesus macaque genome.";
RL Science 316:222-234(2007).
RN [2] {ECO:0000313|Ensembl:ENSMMUP00000023587.4}
RP IDENTIFICATION.
RC STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000023587.4};
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC {ECO:0000256|ARBA:ARBA00007025}.
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DR RefSeq; XP_015002505.1; XM_015147019.1.
DR RefSeq; XP_015002506.1; XM_015147020.1.
DR RefSeq; XP_015002507.1; XM_015147021.1.
DR RefSeq; XP_015002508.1; XM_015147022.1.
DR STRING; 9544.ENSMMUP00000023587; -.
DR Ensembl; ENSMMUT00000025211.4; ENSMMUP00000023587.4; ENSMMUG00000017943.4.
DR VEuPathDB; HostDB:ENSMMUG00000017943; -.
DR VGNC; VGNC:81396; ERCC6.
DR GeneTree; ENSGT00940000158057; -.
DR HOGENOM; CLU_000315_7_3_1; -.
DR InParanoid; F7EMA8; -.
DR OMA; VKHDAIM; -.
DR Proteomes; UP000006718; Chromosome 9.
DR Bgee; ENSMMUG00000017943; Expressed in fibroblast and 22 other cell types or tissues.
DR ExpressionAtlas; F7EMA8; baseline.
DR GO; GO:0110016; C:B-WICH complex; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:UniProtKB-KW.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IBA:GO_Central.
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; IBA:GO_Central.
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; IPR029526; PGBD.
DR InterPro; IPR038718; SNF2-like_sf.
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; PF13843; DDE_Tnp_1_7; 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 Reference proteome {ECO:0000313|Proteomes:UP000006718}.
FT DOMAIN 1087..1263
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1411..1570
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 540..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1610..1815
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1887..1949
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 324..339
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..399
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..425
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..468
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..573
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1648..1709
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1710..1724
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1726..1742
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1743..1770
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1779..1815
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1899..1921
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1922..1943
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2061 AA; 233145 MW; 067FEDDA9FA6B022 CRC64;
MPNEGIPHSS QTQEQDYLQS QPVSNNEEMA IKQESGGDGE VEEYLPFSSV GDGPSTSAEG
CASAASRRGP ALLHINRHQI QAVEPSAQAL ELQGLGVDVY DQDVLEQGVL RQVDNAIHEA
SRTSQLADVE KEYRSVLDDL TSCTTSLRQI NKIIEQLSPQ AATSRDINRK LDSVKRQKYN
KEQQLKKITA KQKHLQAILG GAEVKIELDH ASLEEDAEPG PSSLGSMLMP VQETAWEELI
RTGQMTPFGT QIPQKQEKKP RKIMLNEASG FEKYLADQAK LSFERKKQAT CNKRPARKAP
ASVTPPAPTQ SKNKPNKKAK VLSKKEERLK KHIKKLQKRA LQFQGKVGLP KARRPWESDM
RPEAEGDSEG EESEYFPTEE EEEEEEEDDE VEGVEADLSG DGTDYELKPL PKGRKRQKKV
PVQEIDDDFF PSSGEEAEAS PIGEGGGGGR KVGRYRDDGD EDYYKQRLSP KMPRTLSLHE
ITDLLETDDS IEASAIVIQP PENATAPVSD EESGDEEGGT INNLPGSLLH TAAYLIQDGS
DAESDSDDPS YAPKDDSPDE VPSTSSVQQP PPSRRRKMTK IVCKWKKADL TVQPVAGRVT
APPNDFFTEM RTPTEILELF LDDEVIELIV KYSNLYADSK GVHLGLTSSE FKCFLGIIFL
SGYVSVPRRR MFWEQRTDVH NVLVSAAMRR DRFETIFSNL HVADNADLDP VDKFSKLRPL
ISKLNERCMK FVPNETYFSF DEFMVPYFGR HGCKQFIRGK PIRFGYKFWC GATCLGYICW
FQPYQGKNPN TKHEEYGVGA SLVLQFSEAL TEAHPGRYHF VFNNFFTSIA LLDKLSSMGH
QATGTVRKDH IDKVPLESDV ALKKKERGTF DYRIDGKGNI VCRWNDNSVV TVASSGAGIH
PLCLVSRYSQ KLKKKIQVQQ PNMIKVYNQF MGGVDRADEN IDKYRASIRG KKWYSSPLLF
CFELVLQNAW QLHKTYDEKP VDFLEFRRRV VCHYLETHGH PPEPGQKGRP QKRNIDSRYD
GINHVIVKQG KQTRRWNKLR LQDKEKRLKL EDDSEESDAE FDEGFKVPGF LFKKLFKYQQ
TGVRWLWELH CQQAGGILGD EMGLGKTIQI IAFLAGLSYS KIRTRGSNYR FEGLGPTVIV
CPTTVMHQWV KEFHTWWPPF RVAILHETGS YTHKKEKLIR DVAHCHGILI TSYSYIRLMQ
DDISRYDWHY VILDEGHKIR NPNAAVTLAC KQFRTPHRII LSGSPMQNNL RELWSLFDFI
FPGKLGTLPV FMEQFSVPIT MGGYSNASPV QVKTAYKCAC VLRDTINPYL LRRMKSDVKM
SLSLPDKNEQ VLFCRLTDEQ HKVYQNFVDS KEVYRILNGE MQIFSGLIAL RKICNHPDLF
SGGPKNLKGL PDDELEEDQF GYWKRSGKMI VVESLLKIWH KQGQRVLLFS QSRQMLDILE
VFLRAQKYTY LKMDGTTTIA SRQPLITRYN EDTSIFVFLL TTRVGGLGVN LTGANRVVIY
DPDWNPSTDT QARERAWRIG QKKQVTVYRL LTAGTIEEKI YHRQIFKQFL TNRVLKDPKQ
RRFFKSNDLY ELFTLTSPDA SQSTETSAIF AGTGSDVQTP KCHLKRKIQP AFGADHDVPK
RKKFPASNIS INDATSSEEK SEAKGAEVNV VPSNQSDPLK DDPHMSSNIA SNDRLGGETN
AVSGLEESSV ISGNRECSNS SGTGKTSRPS GDESIDEKLG LSYKRERPSQ AQTESFWENK
QMENNFYKHK SKTKHHSVAE EETLEKHLRP KQKPKNPKHC RDAKFEGTRI PHLVKKRRYQ
KQDSENKSEA KEQSNDDYVL EKLFKKSVGV HSVMKHDAIM DGASPDYVLV EAEANRVAQD
ALKALRLSRQ RCLGAVSGVP TWTGHRGISG APAGTKSRFG KKRNSNFSVQ HSSSTSPTEK
CQDGIMKKEG KDNVPEHFSG RAEDADSSSG ALASSSLLAK MRARNHLILP ERLESESGHL
QEASALLPTT EHDDLLVEMR NFIAFQAHTD GQASTREILQ EFESKLSASQ SCVFRELLRN
LCTFHRTSGG EGIWKLKPEY C
//