ID   A0A059D529_EUCGR        Unreviewed;       872 AA.
AC   A0A059D529;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=E3 SUMO-protein ligase SIZ1 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=EUGRSUZ_B02478 {ECO:0000313|EMBL:KCW85702.1};
OS   Eucalyptus grandis (Flooded gum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX   NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW85702.1};
RN   [1] {ECO:0000313|EMBL:KCW85702.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW85702.1};
RA   Schmutz J., Hayes R., Myburg A., Tuskan G., Grattapaglia D., Rokhsar D.S.;
RT   "The genome of Eucalyptus grandis.";
RL   Submitted (JUL-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; KK198754; KCW85702.1; -; Genomic_DNA.
DR   RefSeq; XP_010043707.1; XM_010045405.2.
DR   AlphaFoldDB; A0A059D529; -.
DR   STRING; 71139.A0A059D529; -.
DR   EnsemblPlants; KCW85702; KCW85702; EUGRSUZ_B02478.
DR   GeneID; 104432848; -.
DR   Gramene; KCW85702; KCW85702; EUGRSUZ_B02478.
DR   KEGG; egr:104432848; -.
DR   eggNOG; KOG2169; Eukaryota.
DR   InParanoid; A0A059D529; -.
DR   OMA; PHGSINC; -.
DR   OrthoDB; 921278at2759; -.
DR   UniPathway; UPA00886; -.
DR   GO; GO:0061665; F:SUMO ligase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0016925; P:protein sumoylation; IBA:GO_Central.
DR   CDD; cd15570; PHD_Bye1p_SIZ1_like; 1.
DR   CDD; cd16792; SP-RING_Siz-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; IPR031141; SIZ1/2_SP-RING.
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   Pfam; PF02891; zf-MIZ; 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   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
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          11..45
FT                   /note="SAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50800"
FT   DOMAIN          339..422
FT                   /note="SP-RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51044"
FT   REGION          536..563
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          789..817
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          832..872
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        803..817
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   872 AA;  95744 MW;  A759C981F12B9FB7 CRC64;
     MDLVSSCKDK LAYFRIKELK DVLTQLGLSK QGRKQDLVER ILSALSDEQV SKMWAKKHVG
     KEDVAKLVDD IYRKMQVSGA PDLASNGQGA SDCSNVKVKG ESIDPYRSDA KVRCPCGNSL
     ETETMIMCED PRCHVWQHMS CVIFPEKPEE APENFYCELC RLSRADPFWV SVGHPLQPVK
     MVTTNIPADG TNPIQSVERT FQLTRADRDL LVKQEFGLQA WCMLLSDKVS YRMHWPQYAD
     LQINGSPVRA INRPGSQLLG ANGRDDGPII TQIVKDGINK ISLTGCDARI FCLGVRIVKR
     RNVQQILNLI PKESDGERFE DALARVCRCV GGGATEADSD SDLEVVADSF AVNLRCPMSG
     SRMKVAGRFK PCLHMGCFDL EVYVEMNQRS RKWQCPVCMK NYSLENIIID PYFNRVTSLM
     RNCGEDVTEI EVKPDGSWRV KTKTESERRD LGNLSQWHLP DSTLCLLTEE NSPPNAEYLK
     QIKQEGVSDS HTGLKLGIRK NRDGIWEVSK PDELNNSSSN RLLDKFGDHE LKVIPMSSSA
     TGSGRDGEDP SVNQEGGGNF DFSTHNGIEL DSITLNVDPS FGYTDQIPSA PMGDAEIIVL
     SDSDEENDIL VSPRSIYKND HSEPSGINFS MPHAGIADTF EDPALGTGAN SCLGLFNSNT
     DDFENMHLWS LPPGTQGGPA FQLFGSDGDV SDALADLQHG SMNCTSSTNG YALAPVTMTE
     APALVPDPSV GHADDSLNDN LVDNPLALGR VDPSLQLFPS AASLQPNIRD QSDMSNAPRT
     EDWISLRLGD GATGGHCEPP TANGFTPGQQ IPSGEGSMET LADTASLLLG MNDGRSEKAS
     RQRSGSPLSF PRQKRSVRPR PRLYLSIESD SE
//