ID A0A1S3GTU8_DIPOR Unreviewed; 1243 AA.
AC A0A1S3GTU8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=DNA excision repair protein ERCC-6-like {ECO:0000313|RefSeq:XP_012891387.1};
GN Name=Ercc6l {ECO:0000313|RefSeq:XP_012891387.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012891387.1};
RN [1] {ECO:0000313|RefSeq:XP_012891387.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012891387.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC {ECO:0000256|ARBA:ARBA00007025}.
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DR RefSeq; XP_012891387.1; XM_013035933.1.
DR AlphaFoldDB; A0A1S3GTU8; -.
DR STRING; 10020.ENSDORP00000007376; -.
DR GeneID; 106000644; -.
DR KEGG; dord:106000644; -.
DR CTD; 54821; -.
DR InParanoid; A0A1S3GTU8; -.
DR OrthoDB; 5485325at2759; -.
DR Proteomes; UP000081671; Unplaced.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR CDD; cd18001; DEXHc_ERCC6L; 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 InterPro; IPR019734; TPR_repeat.
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 SMART; SM00028; TPR; 2.
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 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:UP000081671}.
FT DOMAIN 110..278
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 466..626
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 333..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 737..759
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 974..1008
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1022..1091
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1110..1187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 54..81
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1036..1091
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1123..1138
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1139..1153
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1154..1171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1243 AA; 140101 MW; BD43AF3F405D61BF CRC64;
MMEVSRNSAE IQNLSSIQAA QYLRYVKEAK EAAKNGDLEE ALKLFNLAKD IFPNEKVMSR
IQKLQEALEE LAEEENDEFT DVCNSGLLLY RELYNQLFEY QKEGVAFLYS LYRDGKKGGI
LADDMGLGKT VQIIAFLSGM FDASFVKHVL LIMPTSLINT WIKEFARWTP GMRVKTFHGP
SKDERTRNLR RIQQRNGIVI TTYQMLINNW QHLASFNGGE FVWDYVILDE AHKIKSSSTK
TAICARIVPA RNRLLLTGTP IQNNLQELWS LFDFACQGSL LGTLKTFKIE YENPIVRARE
KDATPGEKAL GFKISENLMA IIKPYFLRRT KEEVQKKKPS DPEVRPNENT PGVNPICEMP
SLSRKNDLIV WIRLVPLQEE IYRKFTSLDH IKELLMETRS PLAELGVLKK LCDHPRLLSA
RVCGLLNLGN IRFSAQDVNE EDPSEVHNID HITDETLMNE SGKMIFLMDL LNRLRDEGHQ
TLVFSQSRQI LNIIERLLKS KYFKVLRIDG TVTHLWEREK RIQLFQQNKE YSVFLLTTLV
GGVGLTLTAA TRVVIFDPSW NPATDAQAVD RVYRIGQKEN VVIYRLITCG TVEEKIYRRQ
VFKDSLIRQT TGDKKNPFRY FTKQELRELF TIEDLQNSAT QLQLQSLHAA QRRSDEKLDE
HIAYLHSLGI AGISDHDLMY TRDLSVKEEL DVIEESQYIQ QRVQKAQFLV EFESQNTMGK
QRTENEEAWQ RASILASQTK KRGPGLNKPQ HQPSPFRTTH YTQEDDISSQ MANISLDDQS
QESEPQDLSS VAVNVTMMQD GSHPYENKFD ADSASTLPTG VGSAERMWTE SSLGTAEVCA
IEDEAVQKEA LQERPRQAAL QESPLGSLLS QSVRAEAEPG PIRDLQDSEI LHSCSSWPIN
PMTKENKSQE SNTSIIKISD DSLSASHSTL QVAQVNGANT KEKSLSSSPQ YACDFNLFLE
DSADNRQNLS DQSLEHVGKE EGPCGSAVNS RAESVHHSSL SSGKDEAEEV VINVKTRSKA
RRIISDDEDE DDPFKSTSST SPFSTSPFEF TSVKQFDAST PKHDTSQSGR LFSPKMPDSG
NKSTTSRRSL ASRRSLINVV LDHVEDMEEE LGNHHEAEDA ADDPQGETSC DECTEEDLPS
ETLPSKDKSS ELKMSEPSSP VLQTSSGATP EPLSGEPLVA SPQEKAVEAT DDYETLVARG
KELKECGKIQ EALNCFVKAL DIKSADPEVM LMTLSLYKQL SNT
//
