ID A7EAT3_SCLS1 Unreviewed; 427 AA.
AC A7EAT3;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE RecName: Full=SP-RING-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=SS1G_02415 {ECO:0000313|EMBL:EDN99561.1};
OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=665079 {ECO:0000313|EMBL:EDN99561.1, ECO:0000313|Proteomes:UP000001312};
RN [1] {ECO:0000313|Proteomes:UP000001312}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18683 / 1980 / Ss-1 {ECO:0000313|Proteomes:UP000001312};
RX PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
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; CH476623; EDN99561.1; -; Genomic_DNA.
DR RefSeq; XP_001596199.1; XM_001596149.1.
DR AlphaFoldDB; A7EAT3; -.
DR STRING; 665079.A7EAT3; -.
DR EnsemblFungi; EDN99561; EDN99561; SS1G_02415.
DR GeneID; 5492495; -.
DR KEGG; ssl:SS1G_02415; -.
DR VEuPathDB; FungiDB:sscle_04g034470; -.
DR eggNOG; KOG2979; Eukaryota.
DR HOGENOM; CLU_028753_0_0_1; -.
DR InParanoid; A7EAT3; -.
DR OMA; TWFSHLE; -.
DR OrthoDB; 2726194at2759; -.
DR UniPathway; UPA00886; -.
DR Proteomes; UP000001312; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0030915; C:Smc5-Smc6 complex; IBA:GO_Central.
DR GO; GO:0061665; F:SUMO ligase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR GO; GO:0016925; P:protein sumoylation; IBA:GO_Central.
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; IPR013087; Znf_C2H2_type.
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.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000001312};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00452}.
FT DOMAIN 271..363
FT /note="SP-RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51044"
FT DOMAIN 297..327
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 90..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..273
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..407
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 427 AA; 49459 MW; 586FF5F85C9683FD CRC64;
MSVLRRLQTG AERNAPQSSP APVRSGPSHQ NEPSSLPEYT PPTCPLSTNA QRAIANIRTL
HNTTKLKKHL SAAIKNITDT TVANNDRLWE RKRQVEKNAR KRERDGQQDE EMPSEHKDLE
IHTRHMAKKV KAWTEQAEIA MRILIDKGDE VERNDMVIRD VCDKLVEANP PPSNRRIRGQ
EYEEEAKQDG EVISAVELLD QIKEEYKTKY EAETMTKRYA SHNDYKSFKR VVHDSLYPDQ
DVPLAKESTW FPSDRSHPSA QEDHRGEDES SDDEIVIEKI VKDLKCPLTF ATFREPYTNN
KCNHSFEKEA IVEYHRKNAT IHKGERVIKC PAMGCENFIA MKNMYDDQLL LRQVRRATER
ERNHDSEDDD DAPRGTQRNR PEELVDESAF LDVDDEDRRK SVKRERMSIR GAPNLTQVST
DDEDEDE
//
