ID A5K2L3_PLAVS Unreviewed; 1060 AA.
AC A5K2L3;
DT 10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 10-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE RecName: Full=E3 SUMO-protein ligase PIAS {ECO:0008006|Google:ProtNLM};
GN ORFNames=PVX_114995 {ECO:0000313|EMBL:EDL46663.1};
OS Plasmodium vivax (strain Salvador I).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX NCBI_TaxID=126793 {ECO:0000313|EMBL:EDL46663.1, ECO:0000313|Proteomes:UP000008333};
RN [1] {ECO:0000313|EMBL:EDL46663.1, ECO:0000313|Proteomes:UP000008333}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Salvador I {ECO:0000313|EMBL:EDL46663.1,
RC ECO:0000313|Proteomes:UP000008333};
RX PubMed=18843361; DOI=10.1038/nature07327;
RA Carlton J.M., Adams J.H., Silva J.C., Bidwell S.L., Lorenzi H., Caler E.,
RA Crabtree J., Angiuoli S.V., Merino E.F., Amedeo P., Cheng Q., Coulson R.M.,
RA Crabb B.S., Del Portillo H.A., Essien K., Feldblyum T.V.,
RA Fernandez-Becerra C., Gilson P.R., Gueye A.H., Guo X., Kang'a S.,
RA Kooij T.W., Korsinczky M., Meyer E.V., Nene V., Paulsen I., White O.,
RA Ralph S.A., Ren Q., Sargeant T.J., Salzberg S.L., Stoeckert C.J.,
RA Sullivan S.A., Yamamoto M.M., Hoffman S.L., Wortman J.R., Gardner M.J.,
RA Galinski M.R., Barnwell J.W., Fraser-Liggett C.M.;
RT "Comparative genomics of the neglected human malaria parasite Plasmodium
RT vivax.";
RL Nature 455:757-763(2008).
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC {ECO:0000256|ARBA:ARBA00004718}.
CC -!- SIMILARITY: Belongs to the PIAS family.
CC {ECO:0000256|ARBA:ARBA00005383}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EDL46663.1}.
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DR EMBL; AAKM01000003; EDL46663.1; -; Genomic_DNA.
DR RefSeq; XP_001616390.1; XM_001616340.1.
DR AlphaFoldDB; A5K2L3; -.
DR STRING; 126793.A5K2L3; -.
DR EnsemblProtists; EDL46663; EDL46663; PVX_114995.
DR GeneID; 5475689; -.
DR KEGG; pvx:PVX_114995; -.
DR VEuPathDB; PlasmoDB:PVX_114995; -.
DR InParanoid; A5K2L3; -.
DR OMA; QQEVICI; -.
DR PhylomeDB; A5K2L3; -.
DR UniPathway; UPA00886; -.
DR Proteomes; UP000008333; Chromosome 11.
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; cd16650; SP-RING_PIAS-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR003034; SAP_dom.
DR InterPro; IPR036361; SAP_dom_sf.
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 SUPFAM; SSF68906; SAP domain; 1.
DR PROSITE; PS50800; SAP; 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:UP000008333};
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 14..48
FT /note="SAP"
FT /evidence="ECO:0000259|PROSITE:PS50800"
FT DOMAIN 397..484
FT /note="SP-RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51044"
FT REGION 88..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 776..864
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 940..974
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 995..1014
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1027..1060
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 776..793
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 837..851
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 940..955
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 995..1009
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1029..1047
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1060 AA; 120500 MW; 3B352B54D0F3A045 CRC64;
MSYNVYKTNM ADCLNKLRVY DLNQLCRKFL LPQHGKKVAI VERILEYITD VEREEQIYEF
ILAIKPSIFE LINGKRINNA FNNSNVNNVQ SSAHSSAHSS THNSTHNSTH SNNSGSNKYL
SSSNNFFLAS NNGNGTFFCN NNDNLNFANN EILAAKKGGT SPVVRKGKAV KIYQEDSDFS
SCVCGGMSKN ISSKNGIVKC IECNKLQHVS CYVQNPGTNK DMENYKILCV VCRLKDMDPF
YPMKKVLWLK SLTVNSEKLV INACDIKSWK NENKEVIIFC IHLDKKNLST NISIKQEWPK
TFVLKVNGNI IEKIFEPSWE HKRRDSPLKI THTLKTGHNN IDISMTNYET PKLFVVAFLL
CKIETEQNII QQVISKSELN FKDSKERIIT ILCTKHDDDE VMCMEINRRI SLNCPFALDR
IEIPCRGIKC CHIQCFDLKS FIDVTKKTKA FNNRWKCPIC SLFLRPKDLI VDMFITYILT
QVPKDIKEVE LSKSGEIIFN QSTVEGKVVK QIDDMDTSAQ QKSRVEIKTE TSMDNIKEYQ
PVKDNNTFSK NEIIIVDSDP EDNDAGAAPQ NVNLQKNRNF VQGQQEVICI SDSDEEENFN
LAPHNRDQKM KEKNTFLIEM KNFENSKCVN DFFLRNMKSL EKRNIVPNSH MLFNDMVLDV
LNDINKIHVN ENLSSCNVQN FDAMQKERIA ELNRSFHEIA SDPLLTYYNK PSLLSKDLYF
LNTSLDALGM KPIRDISTFA DSMYHVDRVD QVDHPNHVDR ADDAEKSDLH MLELAKKGLS
TDPCEEEVNN HVGDDGGGRS NAQDVGEKGV QTGAKEDTTN GEDGEDAPPQ GKHDSSTPIG
VEHKRPRDNS SVNETDPVVG ENKTPPVLNE IGCVDQSKGN FCLKFEDNKP LFDGNKLAAN
EIAALGSQLS SQFNNQLNSQ LNCQLNCQLD SQLRILLQEQ NSPSSHNTQV TPDAQSRSKK
KTKRKKRSNT SENLRKYDSM CSNFNLSLTN YKNKRERAKQ LKDSSKGKNA SSHKYCSFSS
IHAINKTDRC VNGGRDSKKI NKKNDNFKEK KKQRKKKGKK
//
