ID A0A1L9UUI8_ASPBC Unreviewed; 348 AA.
AC A0A1L9UUI8;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=ASPBRDRAFT_40590 {ECO:0000313|EMBL:OJJ75311.1};
OS Aspergillus brasiliensis (strain CBS 101740 / IMI 381727 / IBT 21946).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=767769 {ECO:0000313|EMBL:OJJ75311.1, ECO:0000313|Proteomes:UP000184499};
RN [1] {ECO:0000313|Proteomes:UP000184499}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101740 / IMI 381727 / IBT 21946
RC {ECO:0000313|Proteomes:UP000184499};
RX PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT "Comparative genomics reveals high biological diversity and specific
RT adaptations in the industrially and medically important fungal genus
RT Aspergillus.";
RL Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
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; KV878681; OJJ75311.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L9UUI8; -.
DR STRING; 767769.A0A1L9UUI8; -.
DR VEuPathDB; FungiDB:ASPBRDRAFT_40590; -.
DR OMA; WPGDKFV; -.
DR OrthoDB; 316902at2759; -.
DR Proteomes; UP000184499; 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; IPR001841; Znf_RING.
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 SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 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:UP000184499};
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|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 241..284
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 161..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 301..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..348
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 348 AA; 38733 MW; E2E582231FE03ACA CRC64;
MSRYAEDHDR YDDSNRAFLQ AFMARSTMTF AQAKPVLAAI FSVRDDEQVS PEDITEDDLQ
TYIAAANSAI SPFDLEIRSI LPQIEINNNN DPDAPPPPAP ERVYALVNTT SDALTQLATT
YSADEIAFVK RILDAMFDTY NTRRQEAMVI SSMQALQLAK AGAGDASRRE SGTQQQATQG
GAAHSLTMTQ AETMLKQLVE QGWFEKSRRG YYRLSPRGLM ELRGWLVAAY NDEGIRKIKF
CAACRDIITA GQRCEDRDCP GRLHDHCMRN FFRMQKSESC PVCKNAWPGD KFVGERAVTM
SDPAAQRARR SAANTRQQAD AGPSTKFTLP ELDVEDEADD GEEEAGSD
//
