ID A0A3M2RS09_9HYPO Unreviewed; 692 AA.
AC A0A3M2RS09;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=PLD phosphodiesterase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=CDV36_012398 {ECO:0000313|EMBL:RMJ08009.1};
OS Fusarium kuroshium.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium solani species complex.
OX NCBI_TaxID=2010991 {ECO:0000313|EMBL:RMJ08009.1, ECO:0000313|Proteomes:UP000277212};
RN [1] {ECO:0000313|EMBL:RMJ08009.1, ECO:0000313|Proteomes:UP000277212}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCR3666 {ECO:0000313|EMBL:RMJ08009.1};
RA Stajich J.E., Carrillo J., Kijimoto T., Eskalen A., O'Donnell K.,
RA Kasson M.;
RT "Comparative genomic analysis of Ambrosia Fusariam Clade fungi.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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:RMJ08009.1}.
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DR EMBL; NKUJ01000310; RMJ08009.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M2RS09; -.
DR STRING; 2010991.A0A3M2RS09; -.
DR Proteomes; UP000277212; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:InterPro.
DR GO; GO:0008081; F:phosphoric diester hydrolase activity; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR CDD; cd09122; PLDc_Tdp1_1; 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:SF4; TYROSYL-DNA PHOSPHODIESTERASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF06087; Tyr-DNA_phospho; 1.
DR Pfam; PF02809; UIM; 1.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR PROSITE; PS50330; UIM; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000277212}.
FT REGION 1..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 477..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 570..671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..97
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..131
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..517
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..620
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..662
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 227
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR610347-1"
FT ACT_SITE 465
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR610347-1"
FT BINDING 229
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR610347-2"
FT BINDING 467
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR610347-2"
FT SITE 538
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|PIRSR:PIRSR610347-3"
SQ SEQUENCE 692 AA; 75327 MW; BF61643D118AC0D6 CRC64;
MSGSRQDVPD PGSDMDEDEA LRYAIALSLQ EQEVKESQDQ QTSSQVPPAS ASSASSSRRN
GTGSGGASFG LLSLDRKKME QERLQRLAKR RRSPLDEDDD DDVVEVPPPK RKTPVEPSRS
LPGPWSPSSS PPFPGGVVKR TWARGYPRTS EDIKIEEVFQ KDRLELAVLS SYQWDDEWLL
SKIDLRRTKL LLVAYAADES QKREMQSNTP PGIRFCFPAM NGPGAMHSKL QLLKYPDYLR
VVVPTANLVP YDWGETGVME NMVFLIDLPK LEASVHHQPT PFCTELGRFL SETGVGVGMV
SSLANYDFSR TKHLGFVYTI PGGHVGDSLK RIGYCGLGNS VASLGLATDD PVEVDIVCAS
LGSLNYDLVG AMYNACRGDD GMAEYKSRIG RTGAAAKNKS SSPWQAKLKD RFRIYFPTDE
TVAQSRGGRM AAGTICVQPK WWRSATFPTE LVRDCVNNRE GLLMHSKMIF VRRQVSKSTK
AGAAEQSSAE PRQRRGPGIE PERGQHEPDR HDENDDSAEL NAAVLSPGWA YVGSANLSES
AWGRIVKDRA TGQPKMSCRN WESGVVVRVS SRNSSSSSGI SSSRGTTTNS SMARASANAG
STSKNHHQSQ SSSAVLVSLS GGSTEVKAAE AQARVQAGNP SGEPDKGGDT SHTQQQQVTD
MGIFDGTVPV PVRVPGRRYR AGEEPWFYSG QG
//