ID F0ZGB9_DICPU Unreviewed; 794 AA.
AC F0ZGB9;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=PARP-type domain-containing protein {ECO:0000259|PROSITE:PS50064};
GN ORFNames=DICPUDRAFT_87156 {ECO:0000313|EMBL:EGC37015.1};
OS Dictyostelium purpureum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=5786 {ECO:0000313|EMBL:EGC37015.1, ECO:0000313|Proteomes:UP000001064};
RN [1] {ECO:0000313|Proteomes:UP000001064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QSDP1 {ECO:0000313|Proteomes:UP000001064};
RX PubMed=21356102; DOI=10.1186/gb-2011-12-2-r20;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Sucgang R., Kuo A., Tian X., Salerno W., Parikh A., Feasley C.L., Dalin E.,
RA Tu H., Huang E., Barry K., Lindquist E., Shapiro H., Bruce D., Schmutz J.,
RA Salamov A., Fey P., Gaudet P., Anjard C., Babu M.M., Basu S.,
RA Bushmanova Y., van der Wel H., Katoh-Kurasawa M., Dinh C., Coutinho P.M.,
RA Saito T., Elias M., Schaap P., Kay R.R., Henrissat B., Eichinger L.,
RA Rivero F., Putnam N.H., West C.M., Loomis W.F., Chisholm R.L., Shaulsky G.,
RA Strassmann J.E., Queller D.C., Kuspa A., Grigoriev I.V.;
RT "Comparative genomics of the social amoebae Dictyostelium discoideum and
RT Dictyostelium purpureum.";
RL Genome Biol. 12:R20.1-R20.23(2011).
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DR EMBL; GL871010; EGC37015.1; -; Genomic_DNA.
DR RefSeq; XP_003286443.1; XM_003286395.1.
DR AlphaFoldDB; F0ZGB9; -.
DR STRING; 5786.F0ZGB9; -.
DR EnsemblProtists; EGC37015; EGC37015; DICPUDRAFT_87156.
DR GeneID; 10503859; -.
DR KEGG; dpp:DICPUDRAFT_87156; -.
DR eggNOG; KOG4437; Eukaryota.
DR InParanoid; F0ZGB9; -.
DR OMA; WKPKEDD; -.
DR OrthoDB; 11658at2759; -.
DR Proteomes; UP000001064; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0004844; F:uracil DNA N-glycosylase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0097510; P:base-excision repair, AP site formation via deaminated base removal; IBA:GO_Central.
DR GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR CDD; cd22671; FHA_APTX-like; 1.
DR Gene3D; 2.60.200.20; -; 1.
DR Gene3D; 3.40.470.10; Uracil-DNA glycosylase-like domain; 1.
DR Gene3D; 3.30.1740.10; Zinc finger, PARP-type; 1.
DR InterPro; IPR019406; APLF_PBZ.
DR InterPro; IPR005819; H1/H5.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR InterPro; IPR002043; UDG_fam1.
DR InterPro; IPR036895; Uracil-DNA_glycosylase-like_sf.
DR InterPro; IPR001510; Znf_PARP.
DR InterPro; IPR036957; Znf_PARP_sf.
DR PANTHER; PTHR11264; URACIL-DNA GLYCOSYLASE; 1.
DR PANTHER; PTHR11264:SF0; URACIL-DNA GLYCOSYLASE; 1.
DR Pfam; PF10283; zf-CCHH; 1.
DR Pfam; PF00645; zf-PARP; 1.
DR PRINTS; PR00624; HISTONEH5.
DR SMART; SM01336; zf-PARP; 1.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR SUPFAM; SSF52141; Uracil-DNA glycosylase-like; 1.
DR PROSITE; PS50064; ZF_PARP_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000001064};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 6..100
FT /note="PARP-type"
FT /evidence="ECO:0000259|PROSITE:PS50064"
FT REGION 97..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 458..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 660..758
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..487
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..533
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 660..688
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 689..707
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 717..735
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..751
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 794 AA; 90545 MW; 630F04B85C301210 CRC64;
MSNNTYRVEY AGSGRSSCKH SKCKKQIEKT SLRIGKLYPS DRFETDGQAI DWFHPNCFFE
KQKNARKTTK KVDEIDDLEG FDDIKKSDQK LIEELINDHR DSILSKPKSK SKSKPKAKES
KPTKSAASSW FVDDSGNIAN SDDEDSHKNK STSKHNHSKK QAAFEPNEQD DDDIFDDVDA
SKSLTSTVQS TKTSASTSKS NKKPFLLSSV LSKKWFDSLD TVLTQNKPLF EEIVGEKRNS
SYLPISSQIF SSLNFVGSPK DCKVVFFGLS PNNKKETSCG FSFCDASADK WKLYNIKAST
KNLIRAALID RGFITKDDTL DSIQEALKEV DLPSDNPRDW FKSTAKQGVL WLNSSLTSVE
DEDKVPVKVE NYWKPVVNEI IRAIFNNKLE EENPSPTVVV LLGKQLSQLK NEIELIHSEF
MGAVPVEYVE GVSPFLETFL NENYFKKINS YLETHGSKPI DWWKPKEDDE EEEEQEEQQE
EQHEEQHEEE QQEEKGMIPE KKIGNKKSNI FDQDDFEEGP KDIDMEEKPI KSKSKSSSQP
SNDFLSDTAE DIKPESKPIC NLIQENGDKI QLKLDEPFTL GRNILEIKDK LVSRNQAVIK
FVKSFSDTYC VELTPKGQNP IHIDKNGSLE PLAIDTPIYL NDGQQFLLCS QKYPFTVQLI
KPSSTPKKQT PTKQAPTKQT PTKQTPSKQV TKRKYDDFEE EPQHNTKSTS STKKVATESK
PKPKSKPKKK DDFIDFEEED DSGDDYIPSG SDDDSEFVGL KPFVKSRSQD KPACKYWDTC
YRNNPQHFKD FRHP
//
