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Database: UniProt
Entry: A0A1Y1UQ30_9TREE
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ID   A0A1Y1UQ30_9TREE        Unreviewed;       765 AA.
AC   A0A1Y1UQ30;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Tyrosyl-DNA phosphodiesterase-domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BD324DRAFT_258111 {ECO:0000313|EMBL:ORX40109.1};
OS   Kockovaella imperatae.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cuniculitremaceae; Kockovaella.
OX   NCBI_TaxID=4999 {ECO:0000313|EMBL:ORX40109.1, ECO:0000313|Proteomes:UP000193218};
RN   [1] {ECO:0000313|EMBL:ORX40109.1, ECO:0000313|Proteomes:UP000193218}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL Y-17943 {ECO:0000313|EMBL:ORX40109.1,
RC   ECO:0000313|Proteomes:UP000193218};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Louie K.B., Bewick A.J., Labutti K.,
RA   Haridas S., Kuo A., Salamov A., Ahrendt S.R., Lau R., Bowen B.P.,
RA   Lipzen A., Sullivan W., Andreopoulos W.B., Clum A., Lindquist E., Daum C.,
RA   Northen T.R., Ramamoorthy G., Schmitz R.J., Gryganskyi A., Culley D.,
RA   Magnuson J., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Widespread Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the tyrosyl-DNA phosphodiesterase family.
CC       {ECO:0000256|ARBA:ARBA00010205}.
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:ORX40109.1}.
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DR   EMBL; NBSH01000002; ORX40109.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y1UQ30; -.
DR   STRING; 4999.A0A1Y1UQ30; -.
DR   InParanoid; A0A1Y1UQ30; -.
DR   OrthoDB; 930461at2759; -.
DR   Proteomes; UP000193218; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004518; F:nuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0008081; F:phosphoric diester hydrolase activity; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   CDD; cd09122; PLDc_Tdp1_1; 1.
DR   CDD; cd09123; PLDc_Tdp1_2; 1.
DR   Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
DR   InterPro; IPR010347; Tdp1.
DR   InterPro; IPR003903; UIM_dom.
DR   PANTHER; PTHR12415; TYROSYL-DNA PHOSPHODIESTERASE 1; 1.
DR   PANTHER; PTHR12415:SF0; TYROSYL-DNA PHOSPHODIESTERASE 1; 1.
DR   Pfam; PF06087; Tyr-DNA_phospho; 1.
DR   Pfam; PF02809; UIM; 2.
DR   SMART; SM00726; UIM; 2.
DR   SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR   PROSITE; PS50330; UIM; 2.
PE   3: Inferred from homology;
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193218}.
FT   REGION          53..304
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          741..765
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        62..80
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        106..139
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        174..190
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        229..287
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        403
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR610347-1"
FT   ACT_SITE        646
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR610347-1"
FT   BINDING         405
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR610347-2"
FT   BINDING         648
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR610347-2"
FT   SITE            697
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR610347-3"
SQ   SEQUENCE   765 AA;  84396 MW;  888A3BF33BDD1364 CRC64;
     MDASRSNGIG SSVPARGRDK TFDRYFDEHF GHDSSEDVDI ADLRRAAWAT WKTAPPAGMN
     RPEGTHRRKE EEEDEELARA IAMSVQDQGP SRQNAPIDLT EDSDDEDIQR VLAMSTEEER
     SAKRAKRDET PEEERRMLAE AMAASLQPVT PGMRDASAEA GTSEERARLA DASPTDSSIP
     SSTTEPRTAS GSPARLVHPR SPAPRLQANG VLGDRAQMEK ERLARQAARE AQTQPQASSS
     RSTAPPKVHV SSNLRTFADL SNSSSASSSS TPTAAYSNTQ SADPHHPLQS AGSLPRDAAG
     EYYPNGEMRH SALTIGQPSK QKTFSPKQVM GDTSQISLII MSSYVVDDAW IETFLPPADE
     VPRVVIRPHP QENHPAWNGK VRAEETGGVA CYPLMVGGLG SAHMKFFWIF YKTGRLRVVI
     STGNLVHYDW EWIENTIFIQ DILPIKEPRE TSSASVKMND FAARFCWLFT HLKVHKAVRH
     LIANHERGSD IPLDPADGFE CLNKWDWSKV RVQLLMSVPG TYTGSQVDDF GLCRLGKILH
     QQGWVPQKNE DVKVEFQGSS LGAYTLDWLD LFYQYCRGKT TSSLLNRPKA IAWPPIKILF
     PSLATVDASI LGRDGGGTMF CGKGMNSLTR PLFHDANSKR GGVLMHAKVL IGVFEPRQDN
     LGFVKASPSS SKRKASEMEN ESADVGGWVY VGSHNFSPAA WGRPNLKKNP PSLTIANYEL
     GIVFPLPRTD TQKAADAIAP HVRPPRPYAN NDVPWDQNIR AQNND
//
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