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Database: UniProt
Entry: A0A0N0V8Q9_FUSLA
LinkDB: A0A0N0V8Q9_FUSLA
Original site: A0A0N0V8Q9_FUSLA 
ID   A0A0N0V8Q9_FUSLA        Unreviewed;       383 AA.
AC   A0A0N0V8Q9;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   03-MAY-2023, entry version 21.
DE   SubName: Full=Chromosomal organization and dna repair protein {ECO:0000313|EMBL:KPA46274.1};
GN   ORFNames=FLAG1_00892 {ECO:0000313|EMBL:KPA46274.1};
OS   Fusarium langsethiae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=179993 {ECO:0000313|EMBL:KPA46274.1, ECO:0000313|Proteomes:UP000037904};
RN   [1] {ECO:0000313|EMBL:KPA46274.1, ECO:0000313|Proteomes:UP000037904}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fl201059 {ECO:0000313|EMBL:KPA46274.1,
RC   ECO:0000313|Proteomes:UP000037904};
RA   Lysoe E., Divon H.H., Terzi V., Orru L., Lamontanara A., Kolseth A.-K.,
RA   Frandsen R.J., Nielsen K., Thrane U.;
RT   "The draft genome sequence of Fusarium langsethiae, a T-2/HT-2 mycotoxin
RT   producer.";
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KPA46274.1}.
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DR   EMBL; JXCE01000006; KPA46274.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N0V8Q9; -.
DR   OrthoDB; 2726194at2759; -.
DR   UniPathway; UPA00886; -.
DR   Proteomes; UP000037904; 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:UP000037904};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00452}.
FT   DOMAIN          254..339
FT                   /note="SP-RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51044"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          78..102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          153..176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          335..383
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..24
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        153..170
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        346..360
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        361..383
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   383 AA;  43409 MW;  E5AC4CCC63D93EDA CRC64;
     MSRRLLNRPG GSSNPSSSSS TIALPDYEPP ACPLTDTARR NLNDLSNTRT SAVYQQQVSE
     SIRLLGFSVS DIHERLRTQH ENLESQKARR EEKGTDKTED EQRLEAHLTK LEERVNELTE
     SSEKAVRELI DHRAELEDEA GILSELHDIT SAEAHQQRQD QEEQGEGDDQ KDQVAASSVV
     ETFNDLRVKK EAEYKNMSAH QRYALNNDYA GFKKLWHDAA AGEEGPPLPD ASRWFTQDGE
     PVMDGTAAGA ADDDDDDIAV ARETISINCP LTLQPMKDPY TNRNCKHTFE KSALLEYLPM
     RGESQCPQAG CSQSFSRARF DQDFFHDQAM VRRIKRARQT QAQQEMEMDE DEDEEDADGD
     DEVRVRGQQV APGRVLKRER RDD
//
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