ID A0A3B3Y9A1_9TELE Unreviewed; 1388 AA.
AC A0A3B3Y9A1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Excision repair cross-complementation group 6 {ECO:0008006|Google:ProtNLM};
OS Poecilia mexicana.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48701 {ECO:0000313|Ensembl:ENSPMEP00000023665.1, ECO:0000313|Proteomes:UP000261480};
RN [1] {ECO:0000313|Ensembl:ENSPMEP00000023665.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR Ensembl; ENSPMET00000009577.1; ENSPMEP00000023665.1; ENSPMEG00000005496.1.
DR Proteomes; UP000261480; Unplaced.
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}.
FT DOMAIN 456..632
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 781..940
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 245..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 353..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 964..1141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1286..1319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 107..141
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 281..306
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..337
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..392
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 999..1052
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1072..1093
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1094..1110
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1111..1141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1388 AA; 157686 MW; A146E90B807A4385 CRC64;
MICVARLAGK RSGTLLQIDR QRIQVASASS GADELQGLGV FVYDQDVLEQ GVLQQVDEAI
HEASQAAAKA EAEKEYQSVL DDVRSVTASL KHINKIIEQL SPYAASSKDI SRKIESVKRQ
KENKEKQLKK VRAKQKRLQA ILGGEDIQRV EAELLAEDDG EEESGPSTLG SMLMPAQETE
WEELIRKGHM TPFGTRIPQK EVKKEPRKLM LAENSAFDQY LADQAKLATE RKKVPLLKKK
KSSALHVYER TKTGKNVSSS KDNKLKKRMR KLQINALKTH SKARPKTEPK LPKPRRKRHT
EGEQTDSEGS EYLPSDEGLD LDQEEREAME EGFWDGNEDD EYELKLYKKK TVGTGRKKMK
KNDSEDEYSP ESSDDDDGDN NRGRSKKHKD DGDVDYYRQR IRKWKRQRIR EREEKRERGE
ELTDDSDAEF DEGFKVPGFL WKKLYKYQQT GVRWMWELHC QQAGGILGDE MGLGKTIQVI
SFLAGLSYSK LRTRGSNYRY VGLGPTVIVC PATVMHQWVK EFHTWWPPFR VAVLHETGSF
TSNKEKLIPE IAACHGILIT SYSAVRNLQD ILQRYDWHYV ILDEGHKIRN PNAGVTVACK
QFRTPHRFIL SGSPMQNNLK ELWSLFDFVF PGKLGTLPVF MEQFSVPITM GGYSNASPVQ
VQTAFKCACV LRDTINPYLL RRMKDDVKAN LSLPDKNEQV LFCRLTEEQR QVYQSFLDSK
EVYQILNGDM QVFSGLIALR KICNHPDLFS GGPRILRGIP EDQLTEEEHF GFWKRSGKLM
VVESLLRLWF KQGQRVLLFT QSRQMLDILE VFVREKDYSY LKMDGTTAIA SRQPLIARYN
EDKSIFIFLL TTKVGGLGVN LTGANRVIIY DPDWNPSTDT QARERAWRIG QKQQVTIYRL
LTAGTIEEKI YHRQIFKQFL TNRVLKDPKQ RRFFKSNDIY ELFTLADPDG TQGTETSAIF
AGTGSDVKVP KKPDRLKSSP FINGVSHDYR RSPGKQRESG AENRNSLSLG HSSISPSSGN
SQGKSNTPTD SRSANQNAKD IEMSNTPNML LIRDGNDSGL VERANRSPTS TSCHQHRDKD
RGKHREKRKH CDSTGTDKRR HKRRKHSRDA RFEGHRISHL VKKRTFNKQE NEETSTEDQK
KSDDYVLAKL FRKSGIHSVM QHDSIMESSN PDYVLVEAEA NRVAKDALKA LKISRQQCRL
PYNRPPPPPT KKRFGQKKNS LLVTSSAQPV ATSVKCKDAA VVKKSISKKP TAGAHFSGEG
GDDDSNSALL SSASLLAKMK ARNHIAMPSS QGAAAAEEEE ENGPGAPATS SPPAPPTEHD
ELLVDLRNFV AFQASVDGEA TTQEVLEYFK PRLTQKQAPV FRELLRSICD FHRTSGQEGI
WRLKENFR
//
