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Database: UniProt
Entry: W9ZVS4_FUSOX
LinkDB: W9ZVS4_FUSOX
Original site: W9ZVS4_FUSOX 
ID   W9ZVS4_FUSOX            Unreviewed;       331 AA.
AC   W9ZVS4;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 27.
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=FOMG_10591 {ECO:0000313|EMBL:EXK35480.1};
OS   Fusarium oxysporum f. sp. melonis 26406.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=1089452 {ECO:0000313|EMBL:EXK35480.1};
RN   [1] {ECO:0000313|EMBL:EXK35480.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=26406 {ECO:0000313|EMBL:EXK35480.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA   Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA   Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA   Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Fusarium oxysporum melonis.";
RL   Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EXK35480.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=26406 {ECO:0000313|EMBL:EXK35480.1};
RG   The Broad Institute Genomics Platform;
RA   Ma L.-J., Corby-Kistler H., Broz K., Gale L.R., Jonkers W., O'Donnell K.,
RA   Ploetz R., Steinberg C., Schwartz D.C., VanEtten H., Zhou S., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "Annotation of the Genome Sequence of Fusarium oxysporum f. sp. melonis
RT   26406.";
RL   Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
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; JH659335; EXK35480.1; -; Genomic_DNA.
DR   AlphaFoldDB; W9ZVS4; -.
DR   VEuPathDB; FungiDB:FOMG_10591; -.
DR   HOGENOM; CLU_045153_0_0_1; -.
DR   Proteomes; UP000030703; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0030915; C:Smc5-Smc6 complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
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; 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.
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   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          230..272
FT                   /note="Non-structural maintenance of chromosomes element 1
FT                   RING C4HC3-type"
FT                   /evidence="ECO:0000259|Pfam:PF08746"
FT   REGION          294..331
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        317..331
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   331 AA;  38019 MW;  4EA4DDC6C018DD10 CRC64;
     MSSHEFNHGD RAFLQAILAR GTITFEEARP ILAAIFNANR RHSGDEEGDE VRTDQITEEH
     FQEAIDKASE AASLFDYEIR STFHQITKRR IWALVNTTSD PQTQLATTYS HEEISFIKRV
     LDAMFEKFNT PRMEVMAITE MQAIKLARPN RRESQIDVET QTQTTVDKGL KHSEVEAVLA
     NLVEGGWFEK SNEGFYTLSP RALLELRPWL VESYNDPDLG LRDWQRIKFC EACKDPVTIG
     LRCAEVDCNF RLHEVCEEAF WRTRRDSKCP RCSTEWSSHK FTGERAVTST DAFQRGRRKN
     GSGWQRSTLA DEVIRDEGGA DEVEDEDVDD A
//
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