ID W5KZ98_ASTMX Unreviewed; 1400 AA.
AC W5KZ98;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Excision repair cross-complementation group 6 {ECO:0000313|Ensembl:ENSAMXP00000012910.2};
GN Name=ERCC6 {ECO:0000313|Ensembl:ENSAMXP00000012910.2};
OS Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Characidae; Astyanax.
OX NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000012910.2, ECO:0000313|Proteomes:UP000018467};
RN [1] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA Jeffery W., Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX PubMed=25329095; DOI=10.1038/ncomms6307;
RA McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA Yoshizawa M., Warren W.C.;
RT "The cavefish genome reveals candidate genes for eye loss.";
RL Nat. Commun. 5:5307-5307(2014).
RN [3] {ECO:0000313|Ensembl:ENSAMXP00000012910.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR STRING; 7994.ENSAMXP00000012910; -.
DR Ensembl; ENSAMXT00000012910.2; ENSAMXP00000012910.2; ENSAMXG00000012559.2.
DR eggNOG; KOG0387; Eukaryota.
DR GeneTree; ENSGT00940000158057; -.
DR HOGENOM; CLU_000315_7_2_1; -.
DR InParanoid; W5KZ98; -.
DR Proteomes; UP000018467; Unassembled WGS sequence.
DR Bgee; ENSAMXG00000012559; Expressed in camera-type eye and 14 other cell types or tissues.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
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:UP000018467}.
FT DOMAIN 497..673
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 822..979
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 242..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 984..1156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1214..1255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1262..1281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1306..1331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 160..194
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..263
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..327
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..353
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..379
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..429
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 984..1002
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1018..1085
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1095..1109
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1137..1156
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1400 AA; 159004 MW; 4D45D01CDE19512D CRC64;
MPVDNNEDQD SPALSSPVSA LTPGGQEENN GINRGTAGLS IPGRGLEEPA AACPETVGPE
ISRKSQLLLQ INRQQIQAVA QNAQAAELQG LGVDVYDQDV LEQGVLQQVD RAIHEANQAA
AKAEAEKEYE SVLDDVRSCT NALKQINKII EQLTPYATSS KDISRKIESV KRQKENKEKQ
LKKIRAKQRR LQAVLGGEDI LKLEAEVLTE DDEEPGPSTL GSMLMPAQET EWEELIRTGH
MTPFGTRIPQ KEEKKEPRKV MLSENSGFDK YLADQASMAE QRKKTPQKKK AKKTSLSEAP
KNGVSTKQEK KLQKRMRKLQ RTALKAHPKA RPKVEKEFPQ TKKKRHREGD SDSEGSVYVP
SDELMDPDEP EPDDEFWVDE NEEYKLKPYK KKKEAKPRKP RKEDDSDEYL PSSSEEDEES
GKNGKMKKYK DDGDIEYYRQ RIRKWKRQRL QDKERRRQAG EDESEESDVE FDEGFKMPGF
LWKKLFKYQQ TGVRWMWELH CQQAGGILGD EMGLGKTIQV IAFLAGLSYS KLRTRGSNYR
YAGLGPTVIV CPATVMHQWV KEFHTWWPPF RVAVLHETGS FTSKREKLIP EIAAGHGILI
TSYSYVRIMQ DYIQKYDWHY VILDEGHKIR NPNAGVTVAC KQFRTPHRFI LSGSPMQNNL
KELWSLFDFV FPGKLGTLPV FMEQFSVPIT MGGYSNASPV QVQTAYKCAC VLRDSINPYL
LRRMKADVKA NLALPDKSEQ VLFCRLTEDQ RKVYQDFLDS KEVYQILNGD MQVFSGLIAL
RKICNHPDLF SGGPRLLKGV PEEELSEEEH FGYWKRSGKL IVVESLLRLW YKQGHRVLLF
TQSRQMLEIL EVFVRGNGYS FLKMDGTTTI ASRQPLIARY NEDIFVFLLT TKVGGLGVNL
TGANRVIIYD PDWNPSTDTQ ARERAWRIGQ KQQVTVYRLL TAGTIEEKIY HRQIFKQFLT
NRVLKDPKQR RFFKSNDIYE LFTLSSPDGS QGTETSAIFA GTGSDVQIPK RHKTPQMPSK
PAESQSSSLH VKDQNASSDP SSHRGTTSLR LSNNNSKIDS LNVESTQNSS AGSLTNSPQN
DRFGPSTSQK HREKKKHCDK TDTTSVPSDT HKHKHKKRKH REDARFEGHR ISHLVKKRQY
KKEDNEEQEE KKDERKSDDY VLAKLFKKSG IHSVMKHDTI MEASNPDYVL VEAEANRVAK
DALRALKVSR QQCRLPYSRG PAQATPAPAR KRFGQKKNPV LAQPSGPTQK STEKCKDAAI
IKKSGIKKPG SSAHFSGEGV EEESVSASLS SSSLLAKMKA RNHLSLPQGQ EEEEEVEGSQ
SSAPPAPPTE HDELLVDLRN FVAFQAQVDG QASTKEILEY FTPRLTSSQT PVFRELLRNI
CDFHRTPGQE GMWKLKTDYR
//
