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Database: UniProt
Entry: A0A0U1LMM8_TALIS
LinkDB: A0A0U1LMM8_TALIS
Original site: A0A0U1LMM8_TALIS 
ID   A0A0U1LMM8_TALIS        Unreviewed;       540 AA.
AC   A0A0U1LMM8;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   03-MAY-2023, entry version 29.
DE   RecName: Full=SP-RING-type domain-containing protein {ECO:0000259|PROSITE:PS51044};
GN   ORFNames=PISL3812_01398 {ECO:0000313|EMBL:CRG84059.1};
OS   Talaromyces islandicus (Penicillium islandicum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Islandici.
OX   NCBI_TaxID=28573 {ECO:0000313|EMBL:CRG84059.1, ECO:0000313|Proteomes:UP000054383};
RN   [1] {ECO:0000313|EMBL:CRG84059.1, ECO:0000313|Proteomes:UP000054383}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WF-38-12 {ECO:0000313|EMBL:CRG84059.1};
RA   Syromyatnikov M.Y., Popov V.N.;
RL   Submitted (APR-2015) 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; CVMT01000001; CRG84059.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0U1LMM8; -.
DR   STRING; 28573.A0A0U1LMM8; -.
DR   OMA; QCPQAGC; -.
DR   OrthoDB; 2726194at2759; -.
DR   UniPathway; UPA00886; -.
DR   Proteomes; UP000054383; 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: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   CDD; cd16651; SPL-RING_NSE2; 1.
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.
DR   SUPFAM; SSF57850; RING/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:UP000054383};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00452}.
FT   DOMAIN          355..463
FT                   /note="SP-RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51044"
FT   REGION          1..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          98..187
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          219..264
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          332..357
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          459..540
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..47
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        98..112
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        113..128
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        142..169
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        170..187
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        228..246
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        247..264
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        491..508
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        509..540
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   540 AA;  61059 MW;  847BAF505D92A7B5 CRC64;
     MPSIASSSRR PQVHSSRVAA TPSRTPASSR HGRNQNNPSN NNNGDRRRPS TPEYEPLCTP
     LNAAGQRALA VLLSASSFQQ MKKHLNQAGE RVTEIAAEVN ERATDSRVRH ENSMRKKRGV
     RNKKKASAAA ASRRGNGEGE EGTDDEGQDD DDEMKEDEDE GEDEEEEDDV DISRARKLEQ
     LEDKVKEVTV QLEEKMRGIV DGDYKLNAMR EVIEDVQKTA EQAGAEANAR ERQSRLRSRR
     HIDVDEDEEM EDPDMEEDGD EEETVTVVPT QVINDKLNEF DANWEEQSLA QRYTQNNSYV
     GFYRIVHDSK HPGDEIPPVP HPSTWFSHLE STTGADGSAS PVHGRIRDDQ SPDDEDEEIS
     IERERISLKC PLTFSTFEDP VKSTKCVHSF ERQAIEDLIR NSTMTIAAGE HDFQGGGRGA
     RARRVRAVRC PVCSVTLTLN DLKRDPVLLR RVLRAKAAEQ REEEEARFEG RHHHHRKGGR
     KSGFTIASDD DDQVSIDDDD DKENEDEDDQ EGAKNRVHIK RERSRFSSRA PHSVDEIEDD
//
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