ID A0A316Z724_9BASI Unreviewed; 1068 AA.
AC A0A316Z724;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=P-loop containing nucleoside triphosphate hydrolase protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=FA09DRAFT_331572 {ECO:0000313|EMBL:PWN95963.1};
OS Tilletiopsis washingtonensis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Entylomatales; Entylomatales incertae sedis;
OC Tilletiopsis.
OX NCBI_TaxID=58919 {ECO:0000313|EMBL:PWN95963.1, ECO:0000313|Proteomes:UP000245946};
RN [1] {ECO:0000313|EMBL:PWN95963.1, ECO:0000313|Proteomes:UP000245946}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 4186 {ECO:0000313|EMBL:PWN95963.1,
RC ECO:0000313|Proteomes:UP000245946};
RX PubMed=29771364; DOI=10.1093/molbev/msy072;
RA Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA Spatafora J.W., Aime M.C.;
RT "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT clade Ustilaginomycotina.";
RL Mol. Biol. Evol. 0:0-0(2018).
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; KZ819301; PWN95963.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A316Z724; -.
DR STRING; 58919.A0A316Z724; -.
DR OrthoDB; 200191at2759; -.
DR Proteomes; UP000245946; 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; 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; IPR002464; DNA/RNA_helicase_DEAH_CS.
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 InterPro; IPR017907; Znf_RING_CS.
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; 1.
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; PS00690; DEAH_ATP_HELICASE; 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 Reference proteome {ECO:0000313|Proteomes:UP000245946};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 467..639
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 812..856
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 898..1058
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 210..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 301..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..147
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..252
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..397
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1068 AA; 117359 MW; 004B2ECAF0FBA560 CRC64;
MPPRRSARAS AAGSAPAPAP AAQRYADSPE SPATTTATTT APASGLSTPA TSVGGAASVA
ARHPREGSLD SYASSDGSLP ERRFAVIPPL PASRKRKAAA PVFAAAAPDA AEASGGSDIE
FVSHAAAPKV KAEPKRSLRR TKPQRVVSPE DDGFLSGPSL GDASFSGGGG GGFFAADAPH
DEPPAKSAAR GNKAVPRRIE ALKPLAELYS DEEEEAETTR LLAQSRAARA GETPRQLAAL
TANASANAPS SGSRPRPARA ARPKSFKGLL SEDEEAVADS WDALSEALAL RLQAEEDERV
GAGGFVKHEG GFDDDDDDGG SDFGTPAPRA GPSRIKAAAA PKPRARGRAT KKARIETSEE
YEAPLLGSDL SDAPSDDEGA EGLQEDQRWE TAIQREKRLK RRKTKKGKQS QYERAHGQFS
VHHPELATVW TDLAATAEPV PQQAAQPEGL TIKLLPFQLE GLHWLKAQEA SAWKGGLLAD
EMGMGKTIQM ISLFLSDRKK PVLVVIPTVA IMQWKNEIAK YTENFKVLVW HGSDRETDAA
EVQKYDVVLA TYAVLESSFR KEHQGFKRKG VTIKEPSAVH AIHWHRIVLD EAHNIKERST
NTAKAAFELK GTFRWCLSGT PLQNRVGDLY SQIKFLGGDP FSFYLCKKCP CKSAYWSFEN
NRYCRTCGHT AMSHGNFWNQ EVLKPIQRGG ASHGEGGDAF KRMRLLLSRI MLRRTKIERA
DDMGLPPRTI VVRQDKFSEE EEDLYTSLYQ EGTRKFNTYL DQGTVLNNYS NIFTLLTRMR
QMACHPDLVL RSKTGMAAKM LGEAAGEGVH VCRLCTDEAE DAIMSKCRHI FCRECVRTYY
ESSTAEGGVP DCPQCHARLT IDLEQEELEP PAQLAEHQKG RQGILERLDM DKWRSSSKIE
ALVEELERSK RDDSTTKSIV FSQFVNFLDL IAFRLQRAGY KICRLEGGMS PQARDNTIQH
FMKNADVTVF LVSLKAGGVA LNLTEASRVY LMDPWWNGSV MAQSADRIHR LGQYRPIVIR
YMVIEDSIES RILELQYKKQ NMINAALSSD DAAMSRLSVA DLQFLFQL
//
