NSE1_XENLA
ID NSE1_XENLA Reviewed; 270 AA.
AC Q6PAF4;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 73.
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 Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2003) 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; BC060339; AAH60339.1; -; mRNA.
DR RefSeq; NP_001083134.1; NM_001089665.1.
DR PDB; 7DG2; X-ray; 1.70 A; A=3-248.
DR PDBsum; 7DG2; -.
DR AlphaFoldDB; Q6PAF4; -.
DR SMR; Q6PAF4; -.
DR MaxQB; Q6PAF4; -.
DR DNASU; 398764; -.
DR GeneID; 398764; -.
DR KEGG; xla:398764; -.
DR CTD; 398764; -.
DR Xenbase; XB-GENE-1006461; nsmce1.L.
DR OMA; GRLHDHC; -.
DR OrthoDB; 1159451at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10L.
DR Bgee; 398764; Expressed in testis and 19 other tissues.
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; IPR046349; C1-like_sf.
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; 1.
DR Pfam; PF07574; SMC_Nse1; 1.
DR Pfam; PF08746; zf-RING-like; 1.
DR SUPFAM; SSF57889; SSF57889; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromosome; DNA damage; DNA recombination; DNA repair;
KW Metal-binding; Nucleus; Reference proteome; Telomere; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..270
FT /note="Non-structural maintenance of chromosomes element 1
FT homolog"
FT /id="PRO_0000270949"
FT ZN_FING 185..226
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 236..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 7..19
FT /evidence="ECO:0007829|PDB:7DG2"
FT STRAND 20..23
FT /evidence="ECO:0007829|PDB:7DG2"
FT HELIX 24..37
FT /evidence="ECO:0007829|PDB:7DG2"
FT HELIX 47..58
FT /evidence="ECO:0007829|PDB:7DG2"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:7DG2"
FT STRAND 63..69
FT /evidence="ECO:0007829|PDB:7DG2"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:7DG2"
FT STRAND 76..82
FT /evidence="ECO:0007829|PDB:7DG2"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:7DG2"
FT HELIX 97..112
FT /evidence="ECO:0007829|PDB:7DG2"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:7DG2"
FT HELIX 120..129
FT /evidence="ECO:0007829|PDB:7DG2"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:7DG2"
FT HELIX 137..149
FT /evidence="ECO:0007829|PDB:7DG2"
FT STRAND 152..156
FT /evidence="ECO:0007829|PDB:7DG2"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:7DG2"
FT HELIX 164..177
FT /evidence="ECO:0007829|PDB:7DG2"
FT TURN 178..181
FT /evidence="ECO:0007829|PDB:7DG2"
FT TURN 186..188
FT /evidence="ECO:0007829|PDB:7DG2"
FT STRAND 190..194
FT /evidence="ECO:0007829|PDB:7DG2"
FT TURN 199..201
FT /evidence="ECO:0007829|PDB:7DG2"
FT HELIX 207..213
FT /evidence="ECO:0007829|PDB:7DG2"
FT TURN 223..225
FT /evidence="ECO:0007829|PDB:7DG2"
SQ SEQUENCE 270 AA; 30947 MW; 46ADDF10A31CA556 CRC64;
MADRINESHQ RFLQALMSHG IMEGSAVRAL HRHCCELHKV HYMHDKLDDF VGVLNRHLQP
LFMTIEKGVG EEDGLTYYAL VNRVENDITK MASDYAENEL ELFRKTMELI ILSDNGFATS
ISILNLADEL QSKKMKKKEV EQLLQSFVQE KWLIGRNGEY TLHTRCIMEL EHYIRNTYQD
VAKICNVCRK VAIQSQLCEN CGIPLHLQCA GKYFHGKANP TCPNCNESWP HEIPDLNQVS
SQGPSHSQTE TVRGRNQRSK NTSTASRTSR
