ID D7LNP2_ARALL Unreviewed; 873 AA.
AC D7LNP2;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Predicted protein {ECO:0000313|EMBL:EFH53658.1};
GN ORFNames=ARALYDRAFT_665255 {ECO:0000313|EMBL:EFH53658.1};
OS Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN [1] {ECO:0000313|Proteomes:UP000008694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX PubMed=21478890; DOI=10.1038/ng.807;
RA Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT change.";
RL Nat. Genet. 43:476-481(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; GL348717; EFH53658.1; -; Genomic_DNA.
DR RefSeq; XP_002877399.1; XM_002877353.1.
DR AlphaFoldDB; D7LNP2; -.
DR STRING; 81972.D7LNP2; -.
DR EnsemblPlants; Al_scaffold_0005_1290; Al_scaffold_0005_1290; Al_scaffold_0005_1290.
DR GeneID; 9313467; -.
DR Gramene; Al_scaffold_0005_1290; Al_scaffold_0005_1290; Al_scaffold_0005_1290.
DR KEGG; aly:9313467; -.
DR eggNOG; KOG2169; Eukaryota.
DR HOGENOM; CLU_015870_2_0_1; -.
DR OrthoDB; 921278at2759; -.
DR UniPathway; UPA00886; -.
DR Proteomes; UP000008694; Unassembled WGS sequence.
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 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; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR004181; Znf_MIZ.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10782:SF83; SAP DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR10782; ZINC FINGER MIZ DOMAIN-CONTAINING PROTEIN; 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; 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:UP000008694};
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 346..429
FT /note="SP-RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51044"
FT REGION 764..794
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 832..873
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 764..789
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 873 AA; 97065 MW; A20EE0CBAD3385AF CRC64;
MDLVSSCKEK LAYFRIKELK DVLNQLGLSK QGKKQDLVER ILIILSDEHA ARLWSKKDAV
AREKVAKLVE DAYRRMQACG ASDVASKGQV SSDISTFKVK GELEDHFQPE TKVRCLCGSS
LETESMIQCE DPRCHVWEHV GCVIIPEKPM EVHPPLPESF YCEICRLTRA DPFWVTMAHP
LYPVKMTAMT IPTDGSNPMQ SVDRTFQITR ADKDLLVKHE YDIQAWCMLL NDKVLFRMQW
PQYADLQVNG VPIRAINRPG SQLLGANGRD DGPIITPCVR DGINKISLSG CDSRSFCLGV
RLVKRRTLQQ VLNMIPDEDK GEPFEDALAR VRRCIGGATG NDDADSDSDI EVVADFFGVN
LRCPMSGSRM KVAGRFKLCV HMGCFDLEVF VELNQRSRKW QCPICLKNYS LEHIIIDPYF
NRITSKMRHC DEELTEIEMK PDGSWRVKFK SESERRELGE LSQWHLPDGS LFSTVDEIKP
KMEMLTPVKQ EGCSDGPTPL KLGIRKNRNG IWEVSKPNIN GLSSSNRQEK LEYQEHNVIP
MSSSATGSGR DGDDPSVNQD AVGTFDFGNN GMELDSLSMN VDPSYNFIDR NHQPAATSNN
EVIVLSDSDE ENNVVITGGS AYNENLIDGG VNFPLHPPVI NSYSEDPHTV AGNNSGLGLF
ANIDDDYDMR LWQFPSEPQG GPGFQLFASD ADVSDGLVGL EPGPLDCTPA ISSGYTIAPE
TSSMPSVPMF PESVGRCEAD ANYGLVDNPL AFSREDPSLQ IFLPTRPDTS AQSDLRSQAE
VSNGTPSDDW ISLRLGDHGE TIGVNRDNEN NPVSTRDGTL DTLSQTASLL LGMNDSSKQE
KASRQRSDSP LSFPRQKRSV RPRLYLSIDS DSE
//
