ID A0A409YK10_9AGAR Unreviewed; 1024 AA.
AC A0A409YK10;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=DNA repair protein RAD16 {ECO:0008006|Google:ProtNLM};
GN ORFNames=CVT24_012502 {ECO:0000313|EMBL:PPR03377.1};
OS Panaeolus cyanescens.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Galeropsidaceae; Panaeolus.
OX NCBI_TaxID=181874 {ECO:0000313|EMBL:PPR03377.1, ECO:0000313|Proteomes:UP000284842};
RN [1] {ECO:0000313|EMBL:PPR03377.1, ECO:0000313|Proteomes:UP000284842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2629 {ECO:0000313|EMBL:PPR03377.1,
RC ECO:0000313|Proteomes:UP000284842};
RX PubMed=30283667; DOI=10.1002/evl3.42;
RA Reynolds H.T., Vijayakumar V., Gluck-Thaler E., Korotkin H.B.,
RA Matheny P.B., Slot J.C.;
RT "Horizontal gene cluster transfer increased hallucinogenic mushroom
RT diversity.";
RL Evol. Lett. 2:88-101(2018).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC {ECO:0000256|ARBA:ARBA00007025}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PPR03377.1}.
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DR EMBL; NHTK01001069; PPR03377.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A409YK10; -.
DR STRING; 181874.A0A409YK10; -.
DR InParanoid; A0A409YK10; -.
DR OrthoDB; 200191at2759; -.
DR Proteomes; UP000284842; 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:UP000284842};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT DOMAIN 434..589
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 771..815
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 854..1010
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..92
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..181
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..247
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1024 AA; 115327 MW; 34455A6AC1E2EEFD CRC64;
MARATRLSSR IASKASSATA TPISYASSTF DSRPESVATD EPVETPATSD EEELPAPKTR
RASLKMSKRG KRAASSDLDA SDVQETRAPK RRAVSQRAYV AVPQTPNTKG KGKGWAATPP
ARRSARAVGK GKGKVISPPS VASDEEVVEE PDVVEISESD DIGSNAEENL DQDEEDEEIM
LQEAIRESIR HANGSKAGSS SKVINRGPSA ATVAKAKAAE RRISRQAAKR DDDDDDDDDD
EFNSENMDED RGSDSDVSSL SEPVTDDSSE EEALSSKAKG KQKVNTFKRV PFGRRKRKTA
DELSATKYRK KEERELAQKL GRRLTHAEKT TLSLHRHHPE LRGVWGDLES NVPIVQPRKA
EQPANLKVTL LPFQQESLFW MREQEKTVWA GGMLAVGIFH SSLTCSHSYV FRTRWGAENH
ATLLAFKLTK YYRMGKTIQI ISLLVSDGTK PNLVIAPTVA VMQWRNEIDA HTSGMKVLVW
HGSSRETNHD ELKKYDVVIT TYSVVESCFR KQVQGFTRKG VIIKEDSPIH RIHWNRIILD
EAHNIKERST NTAKAAFELK GTYRWCLSGT PLQNRVGELY SLVRFLGGDP FAYYFCKNCD
CKSLHWKFSD KRTCDGKLHM THFPAIDLHF FQIATTTCFW NNEILTPIQK HGMVGPGHTA
FKKLRVLLDR MMLRRTKLQR ADDLGLPPRT VIVRKDYFSP EEKELYLSLF SDAKRQFSTY
LDQGTVLNNY SNIFSLLTRM RQMACHPDLV LRSKTNASQF LPDEYDEATV CRICNDIAED
AIQSKCRHIF DRECIRQYLE TTPSDTKGPV CPVCHLPLTI DLEAPALEID ESNVKARQGI
LGRLNLDNWR SSSKIEALIE ELSNLRLKDA TTKSLVFSQF VNFLDLIAFR LQRAGFKVCR
LEGTMTPQAR DATIKHFMNN VDVTVFLVSL KAGGVALNLT EASRVYLMDS WWNPAVEYQA
MDRIHRLGQK RPVEAIKLVI EDSIESRIVQ LQEKKSAMVD ATLSSDDSAM GRLTPEDLGF
LFRL
//
