ID   NSE1_PONAB              Reviewed;         266 AA.
AC   Q5RAZ5;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 91.
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;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-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. NSMCE3/MAGEG1 and NSMCE1
CC       ubiquitin ligase are components of SMC5-SMC6 complex and may positively
CC       regulate homologous recombination-mediated 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 which consists at least of
CC       SMC5, SMC6, NSMCE2, NSMCE1, NSMCE4A or EID3 and NSMCE3. NSMCE1, NSMCE4A
CC       or EID3 and NSMCE3 probably form a subcomplex that bridges the head
CC       domains of the SMC5-SMC6 heterodimer. Interacts with NSMCE3.
CC       {ECO:0000250|UniProtKB:Q8WV22}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8WV22}.
CC       Chromosome, telomere {ECO:0000250|UniProtKB:Q8WV22}.
CC   -!- PTM: Ubiquitinated. {ECO:0000250|UniProtKB:Q8WV22}.
CC   -!- SIMILARITY: Belongs to the NSE1 family. {ECO:0000305}.
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DR   EMBL; CR858866; CAH91065.1; -; mRNA.
DR   RefSeq; NP_001125616.1; NM_001132144.1.
DR   AlphaFoldDB; Q5RAZ5; -.
DR   BMRB; Q5RAZ5; -.
DR   SMR; Q5RAZ5; -.
DR   GeneID; 100172534; -.
DR   KEGG; pon:100172534; -.
DR   CTD; 197370; -.
DR   InParanoid; Q5RAZ5; -.
DR   OrthoDB; 1159451at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:2001022; P:positive regulation of response to DNA damage stimulus; ISS:UniProtKB.
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; IPR002219; PE/DAG-bd.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR014857; Znf_RING-like.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR20973; PTHR20973; 1.
DR   Pfam; PF07574; SMC_Nse1; 1.
DR   Pfam; PF08746; zf-RING-like; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   2: Evidence at transcript level;
KW   Chromosome; DNA damage; DNA recombination; DNA repair; Metal-binding;
KW   Nucleus; Phosphoprotein; Reference proteome; Telomere; Transferase;
KW   Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN           1..266
FT                   /note="Non-structural maintenance of chromosomes element 1
FT                   homolog"
FT                   /id="PRO_0000270946"
FT   ZN_FING         191..232
FT                   /note="RING-type; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          1..102
FT                   /note="Interaction with NSMCE3"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WV22"
FT   REGION          245..266
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         251
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WV22"
SQ   SEQUENCE   266 AA;  30900 MW;  B4C513C1D70E6FE7 CRC64;
     MQGSTRRMSV MTDVHRRFLQ LLMTHGVLEE WDVKRLQRHC YKVHDRNATV DKLEDFINNI
     NSVLESLYIE IKRGVTEDDG RPIYALVNLA TTSISKMATD FAENELDLFR KALELIIDSE
     TGFGSSTNIL NLVDQLKGKK MRKKEAEQVL QKFVQNKWLI EKEGEFTLHG RAILEMEQYI
     RETYPDAVKI CNICHSLLIQ GQSCETCGIR MHLPCVAKYF QSNAEPRCPH CNDYWPHEIP
     KVFDPEKERE SGVSKSNKKS LRSRQH