ID   NSE1_BOVIN              Reviewed;         266 AA.
AC   Q3T0X7;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 100.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI02215.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; BC102214; AAI02215.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001030483.1; NM_001035406.1.
DR   AlphaFoldDB; Q3T0X7; -.
DR   SMR; Q3T0X7; -.
DR   STRING; 9913.ENSBTAP00000051539; -.
DR   PaxDb; Q3T0X7; -.
DR   PRIDE; Q3T0X7; -.
DR   GeneID; 534249; -.
DR   KEGG; bta:534249; -.
DR   CTD; 197370; -.
DR   eggNOG; KOG4718; Eukaryota.
DR   InParanoid; Q3T0X7; -.
DR   OrthoDB; 1159451at2759; -.
DR   Proteomes; UP000009136; 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: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; IPR046349; C1-like_sf.
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   SUPFAM; SSF57889; SSF57889; 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; Reference proteome; Telomere; Transferase; Ubl conjugation;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN           1..266
FT                   /note="Non-structural maintenance of chromosomes element 1
FT                   homolog"
FT                   /id="PRO_0000270943"
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          243..266
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        243..257
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   266 AA;  30691 MW;  1A45E50C81BFD45B CRC64;
     MQGNTRRTGV MTDVHRRFLQ LLMTHGVLEE CDVKRLQKHC YKVHDCNATV EKLEDFINTI
     NSVLESLYIE IKKGVTEDDG RPIYALVNLA TTSVSKMASD FAENELDLFR KALELIIDSD
     TGFASSTNIL NLVDQLKGKK MRKKEAEHVL QKFVQNKWLI EKEGEFTLHG RAILEMDQYI
     RETYPDAVKV CNICRSLLIQ GQSCETCGIR MHLPCVAKYF QSSSEPHCPH CNDYWPHEVP
     EVFDPEKERE TGMSRSNKRP SRSRQH