ID A0A165JNX3_EXIGL Unreviewed; 671 AA.
AC A0A165JNX3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Nucleotide excision repair protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=EXIGLDRAFT_610904 {ECO:0000313|EMBL:KZV95120.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV95120.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZV95120.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZV95120.1,
RC ECO:0000313|Proteomes:UP000077266};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC {ECO:0000256|ARBA:ARBA00007025}.
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DR EMBL; KV425962; KZV95120.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165JNX3; -.
DR STRING; 1314781.A0A165JNX3; -.
DR InParanoid; A0A165JNX3; -.
DR OrthoDB; 200191at2759; -.
DR Proteomes; UP000077266; 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 GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR CDD; cd18008; DEXDc_SHPRH-like; 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 Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45626:SF12; DNA REPAIR PROTEIN RAD16; 1.
DR PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 2.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000077266};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT DOMAIN 89..261
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 427..469
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 508..670
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 671 AA; 76892 MW; 78B070D56C80FF45 CRC64;
MKEKRLAQRR LAQANRAEER ALVKKLGRRL THAERTTLKL HKHHPELKDV WGDLEAKIAV
NVPVRGPQPA ELQVTLLPFQ LESLSWMRMQ EDSQWKGGML ADEMGMGKTI QTIALLVHDR
RKPNLVVAPT VAVVQWKNEI EANTKDFKVY LWHGSVREQD IKELKKYDVI LTTYAVLESA
YRKEVDGFKR KGNIVKQKSA LHAFEWERII LDEAHNIKER STNTAKAAFA LKSRYKWCLS
GTPLQNRVGE LYSLVRFLGG DPFSYYFCKS CPCKSLHWRF KNNKECVECG HTPMHHTCLW
NNEILTPIQK HGMVGPGKPA FKKLKVLLDR MMLRRTKLER ADDLGLPPRT VIVRRDYFSE
EEKELYLSLF SDATRQFSTY VDSGTVLNNY SNIFSLITRM RQMACHPDLV LKSKKNGYVE
MDEATVCRLC NDIAEDAIQS KCRHIFDREC IKQYLNTAVE QTPACPVCHV ALSIDLEAPA
LEIEESSTKA RQGILGRLDL DTWRSSSKIE ALVEELTNLR RRDATTKSIV FSQFVNFLDL
IAFRLQRAGF NICRLEGTMS PMARDATIKH FMNNVEVTVF LVSLKAGGVA LNLTEASRVY
LMDSWWNPAV EYQAMDRIHR LGQHRPVQAI KLVIEDSIES RIVQVSSRCH SASVSHPRIA
AAREEVRDVS A
//
