NSE1_DANRE
ID NSE1_DANRE Reviewed; 239 AA.
AC Q6DGT7;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Non-structural maintenance of chromosomes element 1 homolog;
DE Short=Non-SMC element 1 homolog;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q8WV22};
GN Name=nsmce1; ORFNames=zgc:92777;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: RING-type zinc finger-containing E3 ubiquitin ligase that
CC assembles with melanoma antigen protein (MAGE) to catalyze the direct
CC transfer of ubiquitin from E2 ubiquitin-conjugating enzyme to a
CC specific substrate. Within MAGE-RING ubiquitin ligase complex, MAGE
CC stimulates and specifies ubiquitin ligase activity likely through
CC recruitment and/or stabilization of the E2 ubiquitin-conjugating enzyme
CC at the E3:substrate complex. Involved in maintenance of genome
CC integrity, DNA damage response and DNA repair.
CC {ECO:0000250|UniProtKB:Q8WV22}.
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:0000250|UniProtKB:Q8WV22};
CC -!- SUBUNIT: Component of the SMC5-SMC6 complex.
CC {ECO:0000250|UniProtKB:Q8WV22}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8WV22}.
CC Chromosome, telomere {ECO:0000250|UniProtKB:Q8WV22}.
CC -!- SIMILARITY: Belongs to the NSE1 family. {ECO:0000305}.
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DR EMBL; BC076252; AAH76252.1; -; mRNA.
DR RefSeq; NP_001002551.1; NM_001002551.1.
DR AlphaFoldDB; Q6DGT7; -.
DR SMR; Q6DGT7; -.
DR GeneID; 436824; -.
DR KEGG; dre:436824; -.
DR CTD; 197370; -.
DR ZFIN; ZDB-GENE-040718-289; nsmce1.
DR InParanoid; Q6DGT7; -.
DR OrthoDB; 1159451at2759; -.
DR PhylomeDB; Q6DGT7; -.
DR Reactome; R-DRE-3108214; SUMOylation of DNA damage response and repair proteins.
DR PRO; PR:Q6DGT7; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0030915; C:Smc5-Smc6 complex; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046983; F:protein dimerization activity; ISS:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IBA:GO_Central.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR GO; GO:2001022; P:positive regulation of response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0006301; P:postreplication repair; IBA:GO_Central.
DR CDD; cd16493; RING-CH-C4HC3_NSE1; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR011513; Nse1.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR014857; Znf_RING-like.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR20973; PTHR20973; 2.
DR Pfam; PF07574; SMC_Nse1; 1.
DR Pfam; PF08746; zf-RING-like; 1.
PE 2: Evidence at transcript level;
KW Chromosome; DNA damage; DNA recombination; DNA repair; Metal-binding;
KW Nucleus; Reference proteome; Telomere; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..239
FT /note="Non-structural maintenance of chromosomes element 1
FT homolog"
FT /id="PRO_0000270948"
FT ZN_FING 156..199
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 212..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 239 AA; 27205 MW; 3B4BAB7814D2A28B CRC64;
MSRQMGDGHR LFLQNMMTNG IVSAAQAGML HKKCCELHGG QEKIDDFINV VNTHLQPLFM
HIRKGMSEED GQEHFVLMDL IVESDSGSAS STAILNSADK LISKKLKKKE AELVLNKFVQ
DKWLKEQDGE YTLSVRCIVE MEPYMRTIYQ DMIKVCYVCH NIALQCQVCE NPSCEIKVHL
PCVARYFRAR SDPHCPACND FWPHEIPEMQ AAQSQSSQNL PSSSKENTAP TQTRRSRRV