ID G4ZKP0_PHYSP Unreviewed; 742 AA.
AC G4ZKP0;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=SUMO ligase {ECO:0008006|Google:ProtNLM};
GN ORFNames=PHYSODRAFT_351727 {ECO:0000313|EMBL:EGZ16221.1};
OS Phytophthora sojae (strain P6497) (Soybean stem and root rot agent)
OS (Phytophthora megasperma f. sp. glycines).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=1094619 {ECO:0000313|EMBL:EGZ16221.1, ECO:0000313|Proteomes:UP000002640};
RN [1] {ECO:0000313|EMBL:EGZ16221.1, ECO:0000313|Proteomes:UP000002640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P6497 {ECO:0000313|EMBL:EGZ16221.1,
RC ECO:0000313|Proteomes:UP000002640};
RX PubMed=16946064; DOI=10.1126/science.1128796;
RA Tyler B.M., Tripathy S., Zhang X., Dehal P., Jiang R.H., Aerts A.,
RA Arredondo F.D., Baxter L., Bensasson D., Beynon J.L., Chapman J.,
RA Damasceno C.M., Dorrance A.E., Dou D., Dickerman A.W., Dubchak I.L.,
RA Garbelotto M., Gijzen M., Gordon S.G., Govers F., Grunwald N.J., Huang W.,
RA Ivors K.L., Jones R.W., Kamoun S., Krampis K., Lamour K.H., Lee M.K.,
RA McDonald W.H., Medina M., Meijer H.J., Nordberg E.K., Maclean D.J.,
RA Ospina-Giraldo M.D., Morris P.F., Phuntumart V., Putnam N.H., Rash S.,
RA Rose J.K., Sakihama Y., Salamov A.A., Savidor A., Scheuring C.F.,
RA Smith B.M., Sobral B.W., Terry A., Torto-Alalibo T.A., Win J., Xu Z.,
RA Zhang H., Grigoriev I.V., Rokhsar D.S., Boore J.L.;
RT "Phytophthora genome sequences uncover evolutionary origins and mechanisms
RT of pathogenesis.";
RL Science 313:1261-1266(2006).
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; JH159155; EGZ16221.1; -; Genomic_DNA.
DR RefSeq; XP_009529970.1; XM_009531675.1.
DR AlphaFoldDB; G4ZKP0; -.
DR STRING; 1094619.G4ZKP0; -.
DR EnsemblProtists; EGZ16221; EGZ16221; PHYSODRAFT_351727.
DR GeneID; 20649241; -.
DR KEGG; psoj:PHYSODRAFT_351727; -.
DR InParanoid; G4ZKP0; -.
DR OMA; CWPASTQ; -.
DR UniPathway; UPA00886; -.
DR Proteomes; UP000002640; Unassembled WGS sequence.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016925; P:protein sumoylation; IEA:UniProtKB-UniPathway.
DR CDD; cd15489; PHD_SF; 1.
DR CDD; cd16650; SP-RING_PIAS-like; 1.
DR Gene3D; 2.60.120.780; PINIT domain; 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; IPR038654; PINIT_sf.
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; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000002640};
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 17..51
FT /note="SAP"
FT /evidence="ECO:0000259|PROSITE:PS50800"
FT DOMAIN 403..486
FT /note="SP-RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51044"
FT REGION 506..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 697..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..523
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..585
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..714
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 742 AA; 80133 MW; 74FDF24C71EF7BB5 CRC64;
MSDAATRQQL RDIRARLNQL RMPELRNILM DLNLARSGRK SELVERVAAE LESFAEKARG
TTSAAFYAER LSAGLRSVDQ QYRGRLSYAP PPTPAPPAPH NGYHGANVAP QHMAPRYPSM
PPTPPPTRSI PVPMYGRNGA PRTAMGVPQY GAVNVAGAGN GVIPLTSGVD LYNPTKAAAL
DGARCFCVMQ GVSGKVVKCV DCGLAVHAKC HQLITLSGEW YCEMCRSKTY DPFYRVQKTV
LDPNFVRFAK TSSSFRLEYY ITDNDLYANR DPKPGSMTPG NLELQLRCFA VKEDLAAGHC
WPASTQLSVN GFGVPITQRA PPGHANPSKV LRELPANIFQ YSRVGRNVVD IRTTENPSVF
GFMVQIVEVR DINDLVTEVK EASKNLTYEG AKQEVIKSFG SEDEDDVVAT VTILSVRCPL
GLSVISLPAR GLHCKHLQCF DLKTFMLFSK KARSKAWRCT VCHQFIKASD LRIDPYLKKL
LAEVEGEDEL EEVEIFPDGS WKRRLDEELV PEPPAKKVKA EEAEVSAAST NGASAPATSA
DDAQGPPGSS AAAPVEIDLL SSDDEDEETA NTSSATTTTT AAASASSPIL LDDDIDILTV
GSDAWDAPAT SSAANPTSDG NCGEYFPFPL DENLFPSSNA AASNTGNLPS WMYSISASTI
VNSMPPPAPT VAVTSAPAVS PPQEVLNQAE STLASSMASL SRNHNVSNPF DQRQRRQARP
PPKPVAMPSD MDIICLLDSD SD
//
