ID B3RPR1_TRIAD Unreviewed; 1207 AA.
AC B3RPR1;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=DNA excision repair protein ERCC-6 {ECO:0008006|Google:ProtNLM};
GN ORFNames=TRIADDRAFT_53632 {ECO:0000313|EMBL:EDV28228.1};
OS Trichoplax adhaerens (Trichoplax reptans).
OC Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC Trichoplax.
OX NCBI_TaxID=10228 {ECO:0000313|EMBL:EDV28228.1, ECO:0000313|Proteomes:UP000009022};
RN [1] {ECO:0000313|EMBL:EDV28228.1, ECO:0000313|Proteomes:UP000009022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV28228.1,
RC ECO:0000313|Proteomes:UP000009022};
RX PubMed=18719581; DOI=10.1038/nature07191;
RA Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U.,
RA Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L.,
RA Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J.,
RA Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., Dellaporta S.L.,
RA Rokhsar D.S.;
RT "The Trichoplax genome and the nature of placozoans.";
RL Nature 454:955-960(2008).
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DR EMBL; DS985242; EDV28228.1; -; Genomic_DNA.
DR RefSeq; XP_002110062.1; XM_002110026.1.
DR AlphaFoldDB; B3RPR1; -.
DR STRING; 10228.B3RPR1; -.
DR EnsemblMetazoa; TriadT53632; TriadP53632; TriadG53632.
DR GeneID; 6750734; -.
DR KEGG; tad:TRIADDRAFT_53632; -.
DR CTD; 6750734; -.
DR eggNOG; KOG0387; Eukaryota.
DR HOGENOM; CLU_000315_7_0_1; -.
DR InParanoid; B3RPR1; -.
DR OMA; PPFRIAI; -.
DR OrthoDB; 5488252at2759; -.
DR PhylomeDB; B3RPR1; -.
DR Proteomes; UP000009022; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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:InterPro.
DR GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; IBA:GO_Central.
DR CDD; cd22254; CSB_WHD; 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; 2.
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; 2.
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 Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000009022}.
FT DOMAIN 443..595
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 744..903
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 130..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 938..958
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..254
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..335
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 938..953
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1207 AA; 137396 MW; 4DD7659F86B45962 CRC64;
MEHQQDMQPS CSHQADIDEI IQNDTTIQVD NPHADGQQQL KALGLTVFNH SDYEQNLINQ
IAQAIKAEEV LAEKEKVQSQ LQILQETMRK RHQQLATVKD EHVRSNVMST LENLRNQENE
LNEKLSVLEK ENTESSNTLN DECSGDSSND VNNKLELLQK QREQTLSYTI PDEKFTSDDV
SVSDEMIETV LGELGDDMSL NDTFYKNWLD DGDFDINSTN NTADQSQVII EPDSSNNVPD
KNEIDKELPS ALSKKRKKNK ITKIDRSRSL RDTSGSDFED QGADSDEYVP NSKELADSFY
DSDENKKRRR KEKRSGTCTP IKNDKKNKMD TKDKQYQDEP ISLHQLSRKR IISTQDKCID
DAYKDVYRTR IRLYKERFQA YNQLLDAVEG NDVGQITSKS DYSSFINCFD NAYDMVLDGG
LSVPGGIWKK LFKYQQDGVR WMWELHRQDA GGIIGDEMGL GKTIQVIAFL AALKYSKLPQ
RHGKYTGLGP VLIVCPATVL EQWVAEFHKW WPPFRIAIFH ETGSYAGSLE SLVKDIVYSR
GILITTYSHV RIYQTLLAQK PWEYVRTPHR VILTGTPMQN NLRDLWSLFD FVFPGKLGTL
PVFMEQFSVP ITMGGYANAT EVQVQTAYKC ACVLRDTINP YLLRRTKAGV QKDCLHLPPK
NEHVLFCRLT DFQRCVYQQY LKSDEVAGII DGRNHAFGGL ITLRKICNHP HLTNISVPRV
AKVNVDSEII RSDGHWLLSG KMIALKTLLS LWRENKHRVL LFTQTRQMAN ILEKFVKSEN
YPYMRMDGTT NISSRQSLVK LFNRNNAIFI FILTTRVGGL GLNLTGADRV VIFDPDWNPS
TDMQARERAW RVGQTKEVTI YRFLTSGTIE EKIYHRQVFK EFLTNRILKN PKQRRFFKSN
DLYELFSLDS TDNNETSAIF AGTGSEIDLH NKIKKYRLAR KSSRKKSKKS SRGKRIEGTR
VDYVDKEDSY HSSSLDAKTG KTGNSDDYVL GALFKKAGVQ SAMKHDKIVD SSNQDYSLVE
SEAKRVAEIA KKVLTNSSQE CKKYSIGIPT WTGKSGIGGA PMAKPKFGKS SVSHSKTKQG
VEQEQNQHFS GKAKNASEVM SSKDLLTQMR TRNMFSSPSG NNTSNNNDVD GVVLDGARNK
ILLELRDFIA GKPNTQATSR AIINKFQSKL RNTDNAAFRA MLNEMCTFRS MTHGEGVWVL
KAQYRPK
//
