ID A0A0C9YBI5_9AGAR Unreviewed; 937 AA.
AC A0A0C9YBI5;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=DNA repair protein RAD16 {ECO:0008006|Google:ProtNLM};
GN ORFNames=K443DRAFT_673209 {ECO:0000313|EMBL:KIK07632.1};
OS Laccaria amethystina LaAM-08-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Hydnangiaceae; Laccaria.
OX NCBI_TaxID=1095629 {ECO:0000313|EMBL:KIK07632.1, ECO:0000313|Proteomes:UP000054477};
RN [1] {ECO:0000313|EMBL:KIK07632.1, ECO:0000313|Proteomes:UP000054477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LaAM-08-1 {ECO:0000313|EMBL:KIK07632.1,
RC ECO:0000313|Proteomes:UP000054477};
RG DOE Joint Genome Institute;
RA Kuo A., Kohler A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000054477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LaAM-08-1 {ECO:0000313|Proteomes:UP000054477};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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; KN838546; KIK07632.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C9YBI5; -.
DR STRING; 1095629.A0A0C9YBI5; -.
DR HOGENOM; CLU_000315_2_1_1; -.
DR OrthoDB; 200191at2759; -.
DR Proteomes; UP000054477; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000054477};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT DOMAIN 345..517
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 686..728
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 767..924
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 213..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 250..277
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 8..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..79
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 937 AA; 105631 MW; 5DEFD57DD7426CE0 CRC64;
MASGIRRSAR FTASTPTTNA SPIFSARTSV VAETETPNTS DAEDEDAKKP AARSTGRSRK
RAAENESDDA EDVKTVKPPP AKRRAVVNKA YVEIPTKNKG KGKAKAMPPT SRAKGKGKAK
APSSDNESES GKVLEYDEGQ DESIEESNDS GSEFMGSEVE VEIPPSPADE GDGDDMFDID
RLNAAVKMSL QCSAAAERRF ARENKDVDVD DYRMEFDSDD SNSSAEARPS QLKKKGKVTI
TSSLKKVMTM SELRQNKREH RKALLAARRA NQKEEQEMMR VLGRRLTHAE KTSFALKRHH
PELNDVWGDL EANIKIIEPT KAKQPANLKL TLLPFQCESL YWMRKQEKGI WHGGMLADEM
GMGKTIQIIS LFVSDSKKPN LVIAPTVAVM QWKNEIAAHT EGLKVLVWHG SSRESNFEEL
KKYDVVLTTY SVMESCFRKQ QSGFKRKGMI VKEKSPIHQV HWNRIVLDEA HNIKERSTNT
AKAAFQLKSD FKWCLSGTPL QNRVGELYSL IRFLGGDPFS FYFCKLCDCK SLHWTFSDKR
TCDDCGHSPM QHTCFWNNEI LTPIQKNGMG GPGKTAFKKL KILLDRMMLR RTKLQKADDL
GLPPRTVIVR RDYFSPEEKE LYLSLFSDAK RQFTTYLDSG TVLNNYSNIF SLLTRMRQMA
CHPDLVLRSK TNATQFVADA DEATVCRICN DVAEDAIQSR CRHIFDRECI KQYLEASPEE
QPACPVCHLP LTIDLEAPAL ELEENLPNAR QGILGRLNLE TWRSSSKIEA LVEELSNLRM
QDATTKSIVF SQFVNFLDLI AFRLQKAGFT LCRLEGTMSP QARDATIKHF MNNVDVTVFL
VSLKAGGVAL NLTEASRVYL MDSWWNPAVE YQAMDRIHRL GQRRPVQAIK LVVEDSIESR
IVQLQEKKSA MVDATLSTDE SAMGRLTPED LGFLFRL
//
