ID Q5IF59_DROME Unreviewed; 157 AA.
AC Q5IF59;
DT 15-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2005, sequence version 1.
DT 24-JAN-2024, entry version 71.
DE RecName: Full=E3 SUMO-protein ligase NSE2 {ECO:0000256|ARBA:ARBA00020923};
DE AltName: Full=E3 SUMO-protein transferase NSE2 {ECO:0000256|ARBA:ARBA00031731};
DE AltName: Full=Non-structural maintenance of chromosomes element 2 homolog {ECO:0000256|ARBA:ARBA00032533};
DE Flags: Fragment;
GN ORFNames=CG15644 {ECO:0000313|EMBL:AAW32050.1};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000313|EMBL:AAW32050.1};
RN [1] {ECO:0000313|EMBL:AAW32050.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ZH1 {ECO:0000313|EMBL:AAW32054.1}, ZH23
RC {ECO:0000313|EMBL:AAW32056.1}, ZH31 {ECO:0000313|EMBL:AAW32057.1},
RC ZS11 {ECO:0000313|EMBL:AAW32049.1}, ZS2 {ECO:0000313|EMBL:AAW32050.1},
RC ZS24 {ECO:0000313|EMBL:AAW32051.1}, and ZS51
RC {ECO:0000313|EMBL:AAW32053.1};
RX PubMed=15483321; DOI=10.1093/molbev/msi015;
RA Thornton K., Long M.;
RT "Excess of amino acid substitutions relative to polymorphism between X-
RT linked duplications in Drosophila melanogaster.";
RL Mol. Biol. Evol. 22:273-284(2005).
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC {ECO:0000256|ARBA:ARBA00004718}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the NSE2 family.
CC {ECO:0000256|ARBA:ARBA00008212}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY752603; AAW32049.1; -; Genomic_DNA.
DR EMBL; AY752604; AAW32050.1; -; Genomic_DNA.
DR EMBL; AY752605; AAW32051.1; -; Genomic_DNA.
DR EMBL; AY752607; AAW32053.1; -; Genomic_DNA.
DR EMBL; AY752608; AAW32054.1; -; Genomic_DNA.
DR EMBL; AY752610; AAW32056.1; -; Genomic_DNA.
DR EMBL; AY752611; AAW32057.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5IF59; -.
DR EnsemblMetazoa; FBtr0299680; FBpp0288958; FBgn0259196.
DR VEuPathDB; VectorBase:FBgn0259196; -.
DR HOGENOM; CLU_106881_0_0_1; -.
DR UniPathway; UPA00886; -.
DR Bgee; FBgn0259196; Expressed in testis and 5 other cell types or tissues.
DR ExpressionAtlas; Q5IF59; baseline and differential.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0030915; C:Smc5-Smc6 complex; IEA:InterPro.
DR GO; GO:0019789; F:SUMO transferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:InterPro.
DR GO; GO:0016925; P:protein sumoylation; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR026846; Nse2(Mms21).
DR InterPro; IPR004181; Znf_MIZ.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR21330:SF1; E3 SUMO-PROTEIN LIGASE NSE2; 1.
DR PANTHER; PTHR21330; UNCHARACTERIZED; 1.
DR Pfam; PF11789; zf-Nse; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 82..140
FT /note="SP-RING-type"
FT /evidence="ECO:0000259|Pfam:PF11789"
FT REGION 20..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 157
FT /evidence="ECO:0000313|EMBL:AAW32050.1"
SQ SEQUENCE 157 AA; 17870 MW; 45F8F4986B939824 CRC64;
MDPKSHQKLF KEMAEVVSNS SDDGEKLLTK NSSNTIEKSE EVCKERPEAV EQMRIDVNNS
LEDTNMNAVE SEAQKNIAGL DEDLIMEDFG VEVVPFHDPW SKLLIKHPVR NKRCGHIYDR
ETVLMIIKDN IGILCPVRDC PNLSDIKLEH LVKDPDV
//