ID E5AAR0_LEPMJ Unreviewed; 606 AA.
AC E5AAR0;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=MIZ zinc finger protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=LEMA_P018810.1 {ECO:0000313|EMBL:CBY00751.1};
OS Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8)
OS (Blackleg fungus) (Phoma lingam).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC Plenodomus; Plenodomus lingam/Leptosphaeria maculans species complex.
OX NCBI_TaxID=985895 {ECO:0000313|Proteomes:UP000002668};
RN [1] {ECO:0000313|Proteomes:UP000002668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8
RC {ECO:0000313|Proteomes:UP000002668};
RX PubMed=21326234; DOI=10.1038/ncomms1189;
RA Rouxel T., Grandaubert J., Hane J.K., Hoede C., van de Wouw A.P.,
RA Couloux A., Dominguez V., Anthouard V., Bally P., Bourras S.,
RA Cozijnsen A.J., Ciuffetti L.M., Degrave A., Dilmaghani A., Duret L.,
RA Fudal I., Goodwin S.B., Gout L., Glaser N., Linglin J., Kema G.H.J.,
RA Lapalu N., Lawrence C.B., May K., Meyer M., Ollivier B., Poulain J.,
RA Schoch C.L., Simon A., Spatafora J.W., Stachowiak A., Turgeon B.G.,
RA Tyler B.M., Vincent D., Weissenbach J., Amselem J., Quesneville H.,
RA Oliver R.P., Wincker P., Balesdent M.-H., Howlett B.J.;
RT "Effector diversification within compartments of the Leptosphaeria maculans
RT genome affected by Repeat-Induced Point mutations.";
RL Nat. Commun. 2:202-202(2011).
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC {ECO:0000256|ARBA:ARBA00004718}.
CC -!- SIMILARITY: Belongs to the PIAS family.
CC {ECO:0000256|ARBA:ARBA00005383}.
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DR EMBL; FP929138; CBY00751.1; -; Genomic_DNA.
DR RefSeq; XP_003844230.1; XM_003844182.1.
DR AlphaFoldDB; E5AAR0; -.
DR STRING; 985895.E5AAR0; -.
DR EnsemblFungi; CBY00751; CBY00751; LEMA_P018810.1.
DR GeneID; 13292532; -.
DR eggNOG; KOG2169; Eukaryota.
DR HOGENOM; CLU_020537_1_0_1; -.
DR InParanoid; E5AAR0; -.
DR OMA; ECKVREQ; -.
DR OrthoDB; 20246at2759; -.
DR UniPathway; UPA00886; -.
DR Proteomes; UP000002668; Genome.
DR GO; GO:0019789; F:SUMO transferase activity; IEA:UniProt.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016925; P:protein sumoylation; IEA:UniProtKB-UniPathway.
DR CDD; cd16792; SP-RING_Siz-like; 1.
DR Gene3D; 2.60.120.780; PINIT domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR023321; PINIT.
DR InterPro; IPR038654; PINIT_sf.
DR InterPro; IPR003034; SAP_dom.
DR InterPro; IPR031141; SIZ1/2_SP-RING.
DR InterPro; IPR004181; Znf_MIZ.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10782:SF97; SUPPRESSOR OF VARIEGATION 2-10, ISOFORM I; 1.
DR PANTHER; PTHR10782; ZINC FINGER MIZ DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF14324; PINIT; 1.
DR Pfam; PF02891; zf-MIZ; 1.
DR SMART; SM00513; SAP; 1.
DR PROSITE; PS51466; PINIT; 1.
DR PROSITE; PS51044; ZF_SP_RING; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000002668};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00452}.
FT DOMAIN 122..273
FT /note="PINIT"
FT /evidence="ECO:0000259|PROSITE:PS51466"
FT DOMAIN 302..383
FT /note="SP-RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51044"
FT REGION 73..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 391..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..431
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..468
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..483
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 606 AA; 67132 MW; 5E264B6C49B919AD CRC64;
MASSLQQMAA TITERSRTLI NNDLKKILKE EGSSQTGNKA ALQTRVISLI NNAVQEGNAD
LLRRLQYRIQ HHGEAPRAAA ASSPSTPSFP RPTPPAANGY SMAANGYQAS GSPYSAYQQP
HISTRPNGYF FKDSPFFEIR ELIMSNISLD ASPSHRQSVT RTLIPSEHVA ARLKSDKSLR
LLLFSALEQP LAPYARLDIS FPSQIEVRIN AQEVKANYKG LKNKPGSTRP ADITEFVRIT
PTNHRNSLVI TYALTQKASQ QKYNLFIYMV KKFSVEELTR RIKLRNLITR QSVLNEMLKN
ANDPDIEVGS SVMSLKDPIS TLRIQTPCRS TVCTHNQCFD AESFLQLQEQ APTWTCPICN
KTISYEALAV DQYVEEILNK ARNVDQVTIE PNGDWSLDKE ASPKRNDHSA HGAHDDDSDE
DLVEIPDYRI RAIRSEAIPT PTSLSTPPQL SRDSSMAPRS GQKRTSEVVD LTLSDDEEPV
RPAKKVAYST PNSFPDLPRR QLPPLGHSSY GAHSRPIPPA YGVGSSFPRP SATPTSPPPR
TAFPDDYDEC SSANIAPVGL MASSAKGWSL RGHPLSKPVG QPYTRTFFFQ LVSSLFVIPT
EENFLA
//
