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Database: UniProt
Entry: W9RYJ5_9ROSA
LinkDB: W9RYJ5_9ROSA
Original site: W9RYJ5_9ROSA 
ID   W9RYJ5_9ROSA            Unreviewed;       960 AA.
AC   W9RYJ5;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   SubName: Full=E3 SUMO-protein ligase SIZ1 {ECO:0000313|EMBL:EXB98564.1};
GN   ORFNames=L484_014406 {ECO:0000313|EMBL:EXB98564.1};
OS   Morus notabilis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Moraceae; Moreae; Morus.
OX   NCBI_TaxID=981085 {ECO:0000313|EMBL:EXB98564.1, ECO:0000313|Proteomes:UP000030645};
RN   [1] {ECO:0000313|Proteomes:UP000030645}
RP   NUCLEOTIDE SEQUENCE.
RA   He N., Zhao S.;
RT   "Draft Genome Sequence of a Mulberry Tree, Morus notabilis C.K. Schneid.";
RL   Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
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; KE345290; EXB98564.1; -; Genomic_DNA.
DR   RefSeq; XP_010104123.1; XM_010105821.1.
DR   AlphaFoldDB; W9RYJ5; -.
DR   STRING; 981085.W9RYJ5; -.
DR   eggNOG; KOG2169; Eukaryota.
DR   UniPathway; UPA00886; -.
DR   Proteomes; UP000030645; Unassembled WGS sequence.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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; cd15570; PHD_Bye1p_SIZ1_like; 1.
DR   Gene3D; 1.10.720.30; SAP domain; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR   InterPro; IPR003034; SAP_dom.
DR   InterPro; IPR036361; SAP_dom_sf.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR004181; Znf_MIZ.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR10782:SF4; E3 SUMO-PROTEIN LIGASE SIZ1; 1.
DR   PANTHER; PTHR10782; ZINC FINGER MIZ DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00628; PHD; 1.
DR   Pfam; PF02037; SAP; 1.
DR   SMART; SM00249; PHD; 1.
DR   SMART; SM00513; SAP; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   SUPFAM; SSF68906; SAP domain; 1.
DR   PROSITE; PS50800; SAP; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
DR   PROSITE; PS51044; ZF_SP_RING; 1.
PE   3: Inferred from homology;
KW   Ligase {ECO:0000313|EMBL:EXB98564.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030645};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00452}.
FT   DOMAIN          69..103
FT                   /note="SAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50800"
FT   DOMAIN          405..477
FT                   /note="SP-RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51044"
FT   REGION          841..864
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          887..915
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        846..862
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   960 AA;  105761 MW;  6215A5BC2D215B41 CRC64;
     MSNCNAFQVS RKLEPGNPAL EQKYHDKPTT YFLSRRLPRD LVLQKNQHFV SCIGPGSERL
     YALVSSDKLA YFRIKELKDV LTHLGLSKQG KKQDLVDRIL TILSDDQVSK MWAKKNAVRK
     EQVAQLVDDI YRKMQVSTAT DLASKAQGVS DSSNVKVKVE NDDRSFQSET KIRCVCGNQL
     ETESMIQCED RNCQVWQHIN CVIIPDKPME GSTPYPDPFY CELCRLSRAD PFWHQLGHPL
     PPVKLITTNI PTDGTNPVQS VERTFQLQRS DKELTLKQEF DVQAWCMLLN DKVSFRMQWP
     QYADLQVNGI PVRAINRPGS QLLGANGRDD GPIITTYLKE GLNKISLTGC DARVFCLGVR
     LVKRQTVQKI LSLIPKESEG EQFEDAVARV RRCVGGGTAT DDADSDSDLE VVADSFVVNL
     RCPMSGSRMK VAGRFKPCAH MGCFDLEWQC PICLKNYSLE YIITDPYFNR ITSMMRHCGE
     DATEIEVKPD GSWRVKAKSE SERRELGDLG QWHFPDGTIW LPAGGDVKAK TEMKQVKQEG
     ISDSHPGLKL GIKKNSNGFW EVSKPDDMNN SIDNGLQDGL GNYEQKVIPM SSSATGSCRD
     GEDPSVNQDG GGNFDFTNNG VEMDSLTLNV DSMYGITEQA PPVPIRNSEV IEISDSDDDD
     LFISPRSVYK NHPNDGSGVP FSVSPPVIPD SYAEDPAGGT SCLGLFNGND DEFGIPPLWH
     LPPGNQAGPG FQFFGSEAEV SDALVDLQHG SINCSSSMNG YTLAPETVTG SAPLVQNSSV
     GRSDTDMNDG LVDNPLAFAG DDPSLQIFLP TNPTNASAQS DFRDRADVSN GVRTEDWISL
     RLGGSAGGTN GESATPSGLN SKLQVPARDG AMNSMADHAS LLLGMNDGRP EKGIRQRSDS
     PFTFPRQKRS MQRHPWWKEK VENKNGGTEL APAKFLESVS SEFPSALSSL KFAMYLLTGS
//
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