ID A0A2H3EQE6_ARMGA Unreviewed; 664 AA.
AC A0A2H3EQE6;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Nucleotide excision repair protein {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=ARMGADRAFT_1108065 {ECO:0000313|EMBL:PBL01974.1};
OS Armillaria gallica (Bulbous honey fungus) (Armillaria bulbosa).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Physalacriaceae; Armillaria.
OX NCBI_TaxID=47427 {ECO:0000313|EMBL:PBL01974.1, ECO:0000313|Proteomes:UP000217790};
RN [1] {ECO:0000313|Proteomes:UP000217790}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ar21-2 {ECO:0000313|Proteomes:UP000217790};
RX PubMed=29085064; DOI=10.1038/s41559-017-0347-8;
RA Sipos G., Prasanna A.N., Walter M.C., O'Connor E., Balint B., Krizsan K.,
RA Kiss B., Hess J., Varga T., Slot J., Riley R., Boka B., Rigling D.,
RA Barry K., Lee J., Mihaltcheva S., LaButti K., Lipzen A., Waldron R.,
RA Moloney N.M., Sperisen C., Kredics L., Vagvoelgyi C., Patrignani A.,
RA Fitzpatrick D., Nagy I., Doyle S., Anderson J.B., Grigoriev I.V.,
RA Gueldener U., Muensterkoetter M., Nagy L.G.;
RT "Genome expansion and lineage-specific genetic innovations in the forest
RT pathogenic fungi Armillaria.";
RL Nat. Ecol. Evol. 1:1931-1941(2017).
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; KZ293645; PBL01974.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3EQE6; -.
DR STRING; 47427.A0A2H3EQE6; -.
DR InParanoid; A0A2H3EQE6; -.
DR OMA; YFCKQCD; -.
DR OrthoDB; 200191at2759; -.
DR Proteomes; UP000217790; 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:UP000217790};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT DOMAIN 64..233
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 403..445
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 484..647
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:PBL01974.1"
SQ SEQUENCE 664 AA; 75859 MW; 09F7BB982C7F1DF1 CRC64;
AEKSTIALHY HHEELCNVWG NLEESIPVVV PIKADQPADI KLTLLPFQRE GLYWMKQQEQ
GVWNGGMLAD EMGMGKTIQI IALLISDRKK PNLVIAPTVA IMQWKNEIEA HTDGMKVLIW
HGHARESDVK ELKKYDVVLS TYAVLESSFR KQEKGFERKK GDRKMLITEK SPVHQIQWNR
IILDEAHNIK ERATNTAKAA FELQGNYRWC LSGTPLQNRV GELYSLVRFL GGDPFSYYFC
KRCPCKSLHW RFKDKRTCDD CGHSPMQHTC FWNNEILTPI QKHGMQGPGK PAFKKLKVLL
DRMMLRRTKL QRADDLGLPP RTVIVRRDYF SPEEKELYTS LFSDAKRQFN TYLDHGTILN
NYSNIFSLLT RMRQMACHPD LVIRSKTNAN KFIQEDESEA TVCRLCNDIA EDAIQSKCRH
IFDRECIKQY LNTAVEQNPA CPVCHLVLTI DLEAPALELG EEQAQARQGI LGRLNIDTWR
SSTKIEALVE ELSNLRMQDS TTKSLVFSQF VNFLDLIAFR LQKAGFTICR LEGTMSPQAR
DATIKHFMNN VDVTVFLVSL KAGGVALNLT EASRVYLMDS WWNPAVTLLT GRDAEAMDRI
HRLGQHRPVK AIKLVVEDSI ESRIVQLQEK KSAMVDATLS PDDSAMGRLT PADVRFFSTS
CHSS
//
