ID L8GB37_PSED2 Unreviewed; 1241 AA.
AC L8GB37;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=DNA repair and recombination protein RAD26 {ECO:0008006|Google:ProtNLM};
GN ORFNames=GMDG_04676 {ECO:0000313|EMBL:ELR10292.1};
OS Pseudogymnoascus destructans (strain ATCC MYA-4855 / 20631-21) (Bat
OS white-nose syndrome fungus) (Geomyces destructans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=658429 {ECO:0000313|EMBL:ELR10292.1, ECO:0000313|Proteomes:UP000011064};
RN [1] {ECO:0000313|Proteomes:UP000011064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4855 / 20631-21 {ECO:0000313|Proteomes:UP000011064};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C.A., Blehert D.S., Lorch J.M., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E.,
RA Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The genome sequence of Geomyces destructans 20631-21.";
RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; GL573256; ELR10292.1; -; Genomic_DNA.
DR RefSeq; XP_012743098.1; XM_012887644.1.
DR AlphaFoldDB; L8GB37; -.
DR STRING; 658429.L8GB37; -.
DR VEuPathDB; FungiDB:GMDG_04676; -.
DR HOGENOM; CLU_000315_7_0_1; -.
DR InParanoid; L8GB37; -.
DR OrthoDB; 5488252at2759; -.
DR Proteomes; UP000011064; 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:UP000011064}.
FT DOMAIN 439..634
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 771..932
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 233..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1109..1173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 104..162
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 27..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..283
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1141..1167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1241 AA; 138109 MW; E729E57449225666 CRC64;
MPLNSTAQAD VEPNHSSHDR PSEGVTNIDG DAKNTTAEAD TATTPPHAPP PDADGTTSPG
DSMDEILGGL TEGIRNQEDI QRDITARANI ALVAQEDERD EKRIERATTN RDRLVNQKQK
QLRRLDLITT TSTQKKAIRE EIADIDEKVA GLNNDIVQSQ ERIQLRHMQK DGADKNDGEV
STANRRMPNE SQRDFLIRTG KITPFSRMEA RPTEGPTGEL TNILMEAEQA AELPGVTDDQ
SAEQRSHQFL RKPGFEDISE VSSPTDEDSG LSRPRKKRRV GDGSAITSAE ASDGEIIPDS
ARPRKSPGAD SSYTPDIIDG DFIVGDEEEE DDDEGILDIG RAVKKAAKGK AKAKDLIEKV
VDDGNEADYQ KRLKSWVAKR SRARRMKLGE AADIDDGEEE WFKRSPDAPD HHLPNDLRLP
GDIYPALYDY QKTGVQWLGE LYASQVGGIV GDEMGLGKTI QVVSFIAALH FSKQLNKPVI
VVAPATVLQQ WVNEFHRWWP ALRVSILHTS GSGMLNVRQE GRVEDEEEDI TRTRGGKKEP
KAKKAAKRIV DRVIKQGHVL VTTYAGLQTY GDLLVPVEWG YAVLDEGHKI RNPNTTVTIY
CKELQTPNRI ILSGTPLQNN LIELWSLFDF IYPMRLGTLV NFRNQFEIPI KLGGYANATN
LQILTATKCA ETLKEVIGPY LIQRLKADVA SDLPKKTEQV LFCKLTKPQR QAYEEFLKSE
EMVSILNRTR QSLYGIDILR KVCNHPDLLE PRLRNRAGYK WGNANKSGKM QVVKALIMMW
KAKGDKILLF SQGVQMLNII EEFVKSLGGF TYLRMDGGTP IKERQTMVTN FNENPGINIF
LLTTKVGGLG VNLTGANRVI IFDPDWNPST DVQARERAWR LGQKKEVTIY RLMSAGTIEE
KIYHRQIFKQ FLADKILKDP KQRQTFHMKD LYDLFTLGSS EDSTTETGEI FKGTEVKFKR
EVEPVLDYDG TSIMPSQDIP LRNAVSQAAN AETAKNLIAG KVTDPLASTD GEVLPSNLER
DEVGNFIGIA KMEDFHDEDE GKTSTEESRI MEGIFARSGV HSVLQHDKII NGKRVVQADR
IIIEREAKRI AAEAAAELRR SGEEARNVPI GTVTWTGQVG EAGRPAPARR RGPGASGVLQ
GLNERQGSGS ALSSSGSSRS GTPTSGTRGP RGKDFLKLIR DYIRIQGGSV PSQMLVVHFG
NMCRTPQQTA DFKAMLDEVA EIKRPNGLNS RGRWELRDEF K
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