ID D5GDM7_TUBMM Unreviewed; 1062 AA.
AC D5GDM7;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=(Perigord truffle) hypothetical protein {ECO:0000313|EMBL:CAZ82620.1};
GN ORFNames=GSTUM_00001123001 {ECO:0000313|EMBL:CAZ82620.1};
OS Tuber melanosporum (strain Mel28) (Perigord black truffle).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Tuberaceae; Tuber.
OX NCBI_TaxID=656061 {ECO:0000313|EMBL:CAZ82620.1, ECO:0000313|Proteomes:UP000006911};
RN [1] {ECO:0000313|EMBL:CAZ82620.1, ECO:0000313|Proteomes:UP000006911}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mel28 {ECO:0000313|EMBL:CAZ82620.1,
RC ECO:0000313|Proteomes:UP000006911};
RX PubMed=20348908; DOI=10.1038/nature08867;
RA Martin F., Kohler A., Murat C., Balestrini R., Coutinho P.M., Jaillon O.,
RA Montanini B., Morin E., Noel B., Percudani R., Porcel B., Rubini A.,
RA Amicucci A., Amselem J., Anthouard V., Arcioni S., Artiguenave F.,
RA Aury J.M., Ballario P., Bolchi A., Brenna A., Brun A., Buee M.,
RA Cantarel B., Chevalier G., Couloux A., Da Silva C., Denoeud F.,
RA Duplessis S., Ghignone S., Hilselberger B., Iotti M., Marcais B., Mello A.,
RA Miranda M., Pacioni G., Quesneville H., Riccioni C., Ruotolo R.,
RA Splivallo R., Stocchi V., Tisserant E., Viscomi A.R., Zambonelli A.,
RA Zampieri E., Henrissat B., Lebrun M.H., Paolocci F., Bonfante P.,
RA Ottonello S., Wincker P.;
RT "Perigord black truffle genome uncovers evolutionary origins and mechanisms
RT of symbiosis.";
RL Nature 464:1033-1038(2010).
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; FN430152; CAZ82620.1; -; Genomic_DNA.
DR RefSeq; XP_002838429.1; XM_002838383.1.
DR AlphaFoldDB; D5GDM7; -.
DR STRING; 656061.D5GDM7; -.
DR EnsemblFungi; CAZ82620; CAZ82620; GSTUM_00001123001.
DR GeneID; 9181624; -.
DR KEGG; tml:GSTUM_00001123001; -.
DR eggNOG; KOG1001; Eukaryota.
DR HOGENOM; CLU_000315_2_0_1; -.
DR InParanoid; D5GDM7; -.
DR OMA; CHPHLIN; -.
DR OrthoDB; 200191at2759; -.
DR Proteomes; UP000006911; 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:UniProtKB-KW.
DR CDD; cd18008; DEXDc_SHPRH-like; 1.
DR CDD; cd16449; RING-HC; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
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; IPR027370; Znf-RING_euk.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR45626:SF24; ATP-DEPENDENT HELICASE ULS1; 1.
DR PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF13445; zf-RING_UBOX; 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; PS00518; ZF_RING_1; 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|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000006911};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 362..547
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 706..758
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 889..1049
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 65..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 797..876
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 797..831
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1062 AA; 117491 MW; E177702C38BABD43 CRC64;
MKRNREDAFD HFHQDFPETK SQRTTPSPSL QSALLNPNFA GVRHSPLSRD TGISDEELAR
SLHAELNSPR VGNGMSFNNP GGSSDQSLPS INSGLAGMCQ SNSDASYSGR NLHPRRHEEY
MPRASLRHVG SSNGASSSYL SEYDDGYNYS DSGYLDNTLS PALLGGLPKP SATPLRFPHV
SANEVIELLD SDEESEAAVS QSSIGSLLPA QDSRAGSVRP FDYSNYDNLA TTNGWNNNNG
GGFDDPIIVP NQMPQTPDPA TASNDNGNQT PQASDSSAYG GIVDRDGNPL NSGWPSTYRP
EIGNYINHIR NDPTKTLDQL KTLMENIRPD MEIPPENREG TPDDMTYPLM EHQKLGLAWL
KGMEDGSNKG GILADDMGLG KTIQALALIV SRKSKDPDRK TTLIVAPIAL LKQWEREIER
KLKAEHRLKV IIHHGNQKKC RSFEGFKDYD VVLTTFGTIG TEYKKKQALL ESEDPEATKN
ANFFFVGDHC EWYRVIIDEA QCIKNKDTQS AKGCCALNAK FRLCLSGTPM QNSCDEMFSL
LRFLRIEPYS SWSEFSNTFS RPLKSKSERA VSSALLKLQA LMKAVLLRRT KDSTIDGKPI
LTLPDKSIEM VYAVLSPDEQ QFYQALQDKS KILYNKYLRA GTVGRNYSNI LVLLLRLRQA
CCHPHLIRDI EVADAKKPFD DQMIELAKSL SPEAVARLKD PDAFECPICL DAADNPSIVI
PCGHQFCSEC LVQLHTQHVD AAIASGNEEG GARCPGCRGA FQLNKVIDLR TFQKVHMSEG
EEAAPEEPEE EYDDDLIYDT DSSEDSDDDG DTGSDLEGFI VNDEEVDSDE QGEGSATVGA
SEDGGQAPAR KAAAPKKKKD VKGKGKAKEK SRPRTLAEVR KDAMRNAKSK KQYMKHLQKR
WISSAKKTIV FSQFTSLLDL IEIPIHQKGW TYRRYDGGMT STARNEALTE FTDDPSVNII
LVSLKAGNSG LNLVAASQVI ILDPFYNPFI ENQAIDRAHR IGQQRKVRVH KLIVAGTVED
RVLALQEEKR KLIEGALDEK ASQGIGRLSS KDLGFLFGIE SR
//
