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Database: UniProt
Entry: A0A165K8A7_EXIGL
LinkDB: A0A165K8A7_EXIGL
Original site: A0A165K8A7_EXIGL 
ID   A0A165K8A7_EXIGL        Unreviewed;       330 AA.
AC   A0A165K8A7;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   28-JUN-2023, entry version 17.
DE   RecName: Full=PARP-type domain-containing protein {ECO:0000259|PROSITE:PS50064};
GN   ORFNames=EXIGLDRAFT_449476 {ECO:0000313|EMBL:KZV95948.1};
OS   Exidia glandulosa HHB12029.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Auriculariales; Exidiaceae; Exidia.
OX   NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV95948.1, ECO:0000313|Proteomes:UP000077266};
RN   [1] {ECO:0000313|EMBL:KZV95948.1, ECO:0000313|Proteomes:UP000077266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB12029 {ECO:0000313|EMBL:KZV95948.1,
RC   ECO:0000313|Proteomes:UP000077266};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
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DR   EMBL; KV425949; KZV95948.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165K8A7; -.
DR   STRING; 1314781.A0A165K8A7; -.
DR   InParanoid; A0A165K8A7; -.
DR   OrthoDB; 123752at2759; -.
DR   Proteomes; UP000077266; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   Gene3D; 3.30.70.2330; -; 1.
DR   Gene3D; 3.30.1740.10; Zinc finger, PARP-type; 1.
DR   InterPro; IPR014905; HIRAN.
DR   InterPro; IPR001510; Znf_PARP.
DR   InterPro; IPR036957; Znf_PARP_sf.
DR   Pfam; PF08797; HIRAN; 1.
DR   Pfam; PF00645; zf-PARP; 1.
DR   SMART; SM01336; zf-PARP; 1.
DR   SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR   PROSITE; PS50064; ZF_PARP_2; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077266};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          5..94
FT                   /note="PARP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50064"
FT   REGION          95..120
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          249..330
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        98..120
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        251..270
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        284..305
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   330 AA;  36300 MW;  2DD011511D6D2AE4 CRC64;
     MANRHCVEYS RTGRAKCISP TCNEVILKGG LRFGTLVPNP FDPTTEVFRF YHWECTPTVV
     VQMLKDIKLE AVAEWNNLQP DDKKRLKDDI ARVASAPAHG ATSSNSVTPS QNSTQPRDSL
     SLRTSVVGTQ YWQKATVSRG EKVRIVRTPK NKFDNNACNV ATAAGDIFGS VPHGLCAQIS
     PLLDRKEGDF TVEGTMLEGH AEKAKVYELA MELKLTFPLV PAVRNAIPLA LVHAALQYGS
     TAPVVEQHQA VKRARAADDS SDEEPLHKRQ RQGPASSVDA TLPAEKESPR KRPHVPLDIW
     DKLNRVREST ASPPSREPMA VDAHGQIIYG
//
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