ID A0A1B8E0J2_9PEZI Unreviewed; 1238 AA.
AC A0A1B8E0J2;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=DNA excision repair protein ERCC-6 {ECO:0008006|Google:ProtNLM};
GN ORFNames=VE03_06456 {ECO:0000313|EMBL:OBT64891.1};
OS Pseudogymnoascus sp. 23342-1-I1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1524831 {ECO:0000313|EMBL:OBT64891.1, ECO:0000313|Proteomes:UP000091879};
RN [1] {ECO:0000313|EMBL:OBT64891.1, ECO:0000313|Proteomes:UP000091879}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=23342-1-I1 {ECO:0000313|EMBL:OBT64891.1,
RC ECO:0000313|Proteomes:UP000091879};
RA Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT "Comparative genomics of Pseudogymnoascus destructans, the fungus causing
RT white-nose syndrome of bats.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000091879}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=23342-1-I1 {ECO:0000313|Proteomes:UP000091879};
RX PubMed=29295979; DOI=10.1038/s41467-017-02441-z;
RA Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT "Extreme sensitivity to ultraviolet light in the fungal pathogen causing
RT white-nose syndrome of bats.";
RL Nat. Commun. 9:35-35(2018).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; KV455008; OBT64891.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B8E0J2; -.
DR STRING; 1524831.A0A1B8E0J2; -.
DR OrthoDB; 5488252at2759; -.
DR Proteomes; UP000091879; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; 1.20.120.850; SWI2/SNF2 ATPases, N-terminal domain; 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 Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000091879}.
FT DOMAIN 438..633
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 770..931
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 164..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 234..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 517..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1113..1168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 104..162
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 19..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..181
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..253
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..282
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..309
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..535
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1143..1162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1238 AA; 138268 MW; 2AE1EAEF5D026DDB CRC64;
MPLNSTAEGD VEPNHLSSDR PSEGVTNIDD DVKNTTAETN TTTTTPPHAP QEADATTSPG
DNMDSIIENL TEGIRNQEDI QRDITARANI ALVAQEDERD EKRIERATTN RDRLANQKQK
QLRRLELNTT TSTQKKAIRE EIADINEKVA GLNNDIVQSQ ERIQLRHVEQ DDTDKNDGEG
STANRRMPNE SQRDFLIRTG KITPFSRMES RPTEGPAGEL TELLMEAEEA AKLPELTDES
AEPRSHQFLR KPGFEDISEI SSPTDEDAGP SRPRKKRRVG DGSAVTSAEA SEREFIPDSA
RRRKSPDADS AYTPDIIDGD FIVGEDEEEE DDEGIVDIGQ AVKKAAKGKA KAKDVIEKVV
DDGNEADYQK RLKSWVTKRS RARRMKLGEA ADVDDGEAEW FKRSPDAPDH ELPNNLRLPG
DIYPALYDYQ KTGVQWLGEL YASQVGGIVG DEMGLGKTIQ VVSFIAALHF SKQLDKPVIV
VAPATVLQQW VNEFHRWWPA LRVSILHTSG SGMLNVRQES RVEDEEEDIR TSRGGKKEPK
AKKAAKRIVD RVVKQGHVLV TTYAGLQTYG DLLVPVQWGY AVLDEGHKIR NPNTTVTIYC
KELQTPNRII LSGTPLQNNL IELWSLFDFI YPMRLGTLVN FRTQFEVPIK LGGYANATNL
QILTATKCAE TLKEAIGPYL IQRLKADVAS DLPKKTEQVL FCKLTRPQRE AYEEFLKSEE
MVSILNRSRQ SLYGIDILRK VCNHPDLLEP RLRNKAGYKW GNPNKSGKMQ VVKALITMWK
AKGDKILLFS QGVQMLNIIE EFVKSLGGFT YLRMDGGTPI KERQTMVTNF NQNPDINIFL
LTTKVGGLGV NLTGANRVII FDPDWNPSTD VQARERAWRL GQKKEVTIYR LMTAGTIEEK
IYHRQIFKQF LADKILKDPK QRQTFHMKDL YDLFTLGSSD DSTTETGEIF KGTEVKFKRE
VEPPLDYDGT SRMPSQDILP KNAASANGEA PKNLIAGKVT DPLASTDGKI VPANRERDEV
GNFIGIAKME DFHDEDEGKT STEESRIMEG IFARSGVHSV LQHDKIINGK RVVQADRGMI
EREAKRIAAE AAAELRRSGE EARNVPIGTV TWTGQVGEAG RPAPARRRGP GASGVLQGLN
DRQGPGSALS SPGRSRSGTP TTGALDPKGK DFMKLIMEYI RIQGGSVPSQ MLVVHFGRMC
RTPQQTADFK AMLDEVAEIK RPNGVNARGR WELRDEFK
//
