ID E3QCS2_COLGM Unreviewed; 628 AA. AC E3QCS2; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 08-NOV-2023, entry version 40. DE SubName: Full=Ubiquitin interaction domain-containing protein {ECO:0000313|EMBL:EFQ28660.1}; GN ORFNames=GLRG_03804 {ECO:0000313|EMBL:EFQ28660.1}; OS Colletotrichum graminicola (strain M1.001 / M2 / FGSC 10212) (Maize OS anthracnose fungus) (Glomerella graminicola). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum; OC Colletotrichum graminicola species complex. OX NCBI_TaxID=645133 {ECO:0000313|Proteomes:UP000008782}; RN [1] {ECO:0000313|Proteomes:UP000008782} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M1.001 / M2 / FGSC 10212 {ECO:0000313|Proteomes:UP000008782}; RX PubMed=22885923; DOI=10.1038/ng.2372; RA O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J., RA Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J., RA Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z., RA Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D., RA Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y., RA Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U., RA Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H., RA Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L., RA Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K., RA Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F., RA van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J., RA Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E., RA Ma L.-J., Vaillancourt L.J.; RT "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered RT by genome and transcriptome analyses."; RL Nat. Genet. 44:1060-1065(2012). CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}. CC -!- SIMILARITY: Belongs to the tyrosyl-DNA phosphodiesterase family. CC {ECO:0000256|ARBA:ARBA00010205}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; GG697341; EFQ28660.1; -; Genomic_DNA. DR RefSeq; XP_008092680.1; XM_008094489.1. DR AlphaFoldDB; E3QCS2; -. DR STRING; 31870.EFQ28660; -. DR EnsemblFungi; EFQ28660; EFQ28660; GLRG_03804. DR GeneID; 24409169; -. DR VEuPathDB; FungiDB:GLRG_03804; -. DR eggNOG; KOG2031; Eukaryota. DR HOGENOM; CLU_007773_2_0_1; -. DR OrthoDB; 930461at2759; -. DR Proteomes; UP000008782; Unassembled WGS sequence. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. 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 Gene3D; 3.30.870.10; Endonuclease Chain A; 2. DR InterPro; IPR001736; PLipase_D/transphosphatidylase. DR InterPro; IPR010347; Tdp1. DR InterPro; IPR003903; UIM_dom. DR PANTHER; PTHR12415; TYROSYL-DNA PHOSPHODIESTERASE 1; 1. DR PANTHER; PTHR12415:SF4; TYROSYL-DNA PHOSPHODIESTERASE DOMAIN-CONTAINING PROTEIN; 1. DR Pfam; PF06087; Tyr-DNA_phospho; 1. DR Pfam; PF02809; UIM; 1. DR SMART; SM00726; UIM; 1. DR SUPFAM; SSF56024; Phospholipase D/nuclease; 2. DR PROSITE; PS50035; PLD; 1. DR PROSITE; PS50330; UIM; 1. 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 Nucleus {ECO:0000256|ARBA:ARBA00023242}; KW Reference proteome {ECO:0000313|Proteomes:UP000008782}. FT DOMAIN 476..507 FT /note="PLD phosphodiesterase" FT /evidence="ECO:0000259|PROSITE:PS50035" FT REGION 1..115 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 540..591 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 36..62 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 69..107 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 228 FT /note="Nucleophile" FT /evidence="ECO:0000256|PIRSR:PIRSR610347-1" FT ACT_SITE 481 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR610347-1" FT BINDING 230 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR610347-2" FT BINDING 483 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR610347-2" FT SITE 504 FT /note="Interaction with DNA" FT /evidence="ECO:0000256|PIRSR:PIRSR610347-3" SQ SEQUENCE 628 AA; 69083 MW; 7355C1D0DA00ECD3 CRC64; MSMASNRERA RSSSPGPDDD PDLALAIALS LQEQENPKIG GMTTTSSTER PSEQTPKSAP ATNFGSLVLD RKRMEEERLA RLKKRSATQA QLDDQHQRPK TQRAEAPKGH RPSSATFGSL EAATAARDVP QLPFPKGAFK RTWALGYPRT GEDIKIEEIL QKDKLQLAVL SSFQWDEEWL LSKVDVRQTR LLLVAYANNE AEKAAIRANA PTGLVRFCFP PMYGGYMHSK LQILKYEGYL RIVIPSGNLV PYDWGETGVL ENMVFLIDLP KLESTQQAAP PAETLFGTEL RRFLRALGLD EKLVKSLDSY DFTETSRYGF VHSIAGSHAN DSWQHTGQST RGYCGLGSTV RSLGLATEDA VDIDYVASSL GSLNDASLKA IYYACQGDSG MKEYDARKPK PARSKAAKAG LDGSRPVFNE PLQLQRHFRI YFPTEHTVSS SRGGRSSAGT ICFQEKWWKS STFPRELLRD CQSVRSGLLL HTKAIFVQAR DGAAWAYMGS ANLSESAWGR LVKERDSGAP KLTCRNWECG VLVAVDGNLP GSADTGTRPG VDQDAQGQAP MSKGEGGPAV TVTDSEEKQR HQQLGQDEPR CLEGVFGTTM PIPMKVPAGR YTSDESAASR PWFFMKAD //