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Database: UniProt
Entry: A7EBB7_SCLS1
LinkDB: A7EBB7_SCLS1
Original site: A7EBB7_SCLS1 
ID   A7EBB7_SCLS1            Unreviewed;       322 AA.
AC   A7EBB7;
DT   11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT   11-SEP-2007, sequence version 1.
DT   24-JAN-2024, entry version 82.
DE   RecName: Full=Non-structural maintenance of chromosomes element 1 homolog {ECO:0000256|ARBA:ARBA00019422, ECO:0000256|RuleBase:RU368018};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483, ECO:0000256|RuleBase:RU368018};
GN   ORFNames=SS1G_02603 {ECO:0000313|EMBL:EDN99745.1};
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:EDN99745.1, 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   -!- FUNCTION: Acts in a DNA repair pathway for removal of UV-induced DNA
CC       damage that is distinct from classical nucleotide excision repair and
CC       in repair of ionizing radiation damage. Functions in homologous
CC       recombination repair of DNA double strand breaks and in recovery of
CC       stalled replication forks. {ECO:0000256|RuleBase:RU368018}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900,
CC         ECO:0000256|RuleBase:RU368018};
CC   -!- SUBUNIT: Component of the Smc5-Smc6 complex.
CC       {ECO:0000256|RuleBase:RU368018}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|RuleBase:RU368018}.
CC   -!- SIMILARITY: Belongs to the NSE1 family. {ECO:0000256|ARBA:ARBA00010258,
CC       ECO:0000256|RuleBase:RU368018}.
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DR   EMBL; CH476623; EDN99745.1; -; Genomic_DNA.
DR   RefSeq; XP_001596383.1; XM_001596333.1.
DR   AlphaFoldDB; A7EBB7; -.
DR   STRING; 665079.A7EBB7; -.
DR   EnsemblFungi; EDN99745; EDN99745; SS1G_02603.
DR   GeneID; 5492144; -.
DR   KEGG; ssl:SS1G_02603; -.
DR   VEuPathDB; FungiDB:sscle_04g035800; -.
DR   eggNOG; KOG4718; Eukaryota.
DR   HOGENOM; CLU_045153_0_0_1; -.
DR   InParanoid; A7EBB7; -.
DR   OMA; WPGDKFV; -.
DR   OrthoDB; 316902at2759; -.
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:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IBA:GO_Central.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   CDD; cd16493; RING-CH-C4HC3_NSE1; 1.
DR   Gene3D; 3.90.1150.220; -; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR003533; Doublecortin_dom.
DR   InterPro; IPR011513; Nse1.
DR   InterPro; IPR014857; Nse1_RING_C4HC3-type.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR20973; NON-SMC ELEMENT 1-RELATED; 1.
DR   PANTHER; PTHR20973:SF0; NON-STRUCTURAL MAINTENANCE OF CHROMOSOMES ELEMENT 1 HOMOLOG; 1.
DR   Pfam; PF07574; SMC_Nse1; 1.
DR   Pfam; PF08746; zf-RING-like; 1.
DR   PROSITE; PS50309; DC; 1.
PE   3: Inferred from homology;
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU368018};
KW   DNA recombination {ECO:0000256|ARBA:ARBA00023172,
KW   ECO:0000256|RuleBase:RU368018};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|RuleBase:RU368018};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU368018};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU368018};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001312};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU368018};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|RuleBase:RU368018};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU368018};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|RuleBase:RU368018}.
FT   DOMAIN          14..73
FT                   /note="Doublecortin"
FT                   /evidence="ECO:0000259|PROSITE:PS50309"
FT   REGION          280..322
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        282..305
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        306..322
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   322 AA;  36541 MW;  DB924BB69C5A25F7 CRC64;
     MEDALEGYDD TNRAFLQALL ARGSLDLDEG KELLAHIFTV KDERVTSKDD VTLDDLKSYI
     ASAAQALSPF DYEIRSMRHQ LSNKQTWALV NSASDPLTQL ATTFTTEEMF YIKRLLDAMF
     ETFNTKGKEL MAITSTQAIH SSIIGGSGRQ SIGDEDMQVV DNGVKRSDGE RILSELIAQG
     WFERSERGYY SLTPRAILEL RSWLIDTYND SDDPDEWQPI KNCEACKGIV TVGLRCSKRD
     CIVRLHKICQ SAYFNSRPNK NCPRCETEWD GKNYVGEKVV TSTEDNLREK RRSSASSRGR
     GAPVEEEEAE EEEQDEDENE QE
//
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