ID A0A1E4TZE2_PACTA Unreviewed; 270 AA.
AC A0A1E4TZE2;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=SP-RING-type domain-containing protein {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=PACTADRAFT_48871 {ECO:0000313|EMBL:ODV97115.1};
OS Pachysolen tannophilus NRRL Y-2460.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetales incertae sedis; Pachysolen.
OX NCBI_TaxID=669874 {ECO:0000313|EMBL:ODV97115.1, ECO:0000313|Proteomes:UP000094236};
RN [1] {ECO:0000313|Proteomes:UP000094236}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-2460 {ECO:0000313|Proteomes:UP000094236};
RG DOE Joint Genome Institute;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goker M.,
RA Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K., Choi C.,
RA Clum A., Coughlan A.Y., Deshpande S., Douglass A.P., Hanson S.J.,
RA Klenk H.-P., Labutti K., Lapidus A., Lindquist E., Lipzen A.,
RA Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J., Peng Y.,
RA Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C., Stielow J.B.,
RA Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V., Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; KV454012; ODV97115.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E4TZE2; -.
DR STRING; 669874.A0A1E4TZE2; -.
DR OrthoDB; 2728856at2759; -.
DR Proteomes; UP000094236; Unassembled WGS sequence.
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:0004842; F:ubiquitin-protein 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:0016567; P:protein ubiquitination; IEA:InterPro.
DR Gene3D; 1.20.120.1010; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR026846; Nse2(Mms21).
DR InterPro; IPR003613; Ubox_domain.
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.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51698; U_BOX; 1.
DR PROSITE; PS51044; ZF_SP_RING; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000094236};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00452}.
FT DOMAIN 206..270
FT /note="SP-RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51044"
FT DOMAIN 214..270
FT /note="U-box"
FT /evidence="ECO:0000259|PROSITE:PS51698"
FT NON_TER 270
FT /evidence="ECO:0000313|EMBL:ODV97115.1"
SQ SEQUENCE 270 AA; 30642 MW; 3DCBC9E86A122961 CRC64;
MSESDVGIGT GADVEVQDGS LIDLPKYYPL HKKLIQEMNN IKAVDFSPLL TFAESEIDSS
LNRYIDSTLE LNEGEDDFED NLKKKLLLKD EVIINGTNTY ELLSKIIMDD EALREALRAT
KGEINNRFRN EEPLSFETLK LYQDYSSNDI PMEIVDLLNE KNIQSQQKNL SSAKFKKFHN
RLQVYIDPFA VVTDNGNNND NDNDDNDEDV EIAGGSVELT CPISKQIMEN PVITECGHTF
EQTSLRQYKN EASQADKDRC PVCGQKMKNI
//
