UniProt: A0A093GZH0

Database: UniProt
Entry: A0A093GZH0_STRCA

LinkDB:  A0A093GZH0_STRCA 
Original site:  A0A093GZH0_STRCA

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Ontology (7)   
   GO (7)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (8)   
   InterPro (5)   
   Pfam (2)   
   PROSITE (1)   
All databases (17)   

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ID   A0A093GZH0_STRCA        Unreviewed;       239 AA.
AC   A0A093GZH0;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 27.
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};
DE   Flags: Fragment;
GN   ORFNames=N308_13150 {ECO:0000313|EMBL:KFV72515.1};
OS   Struthio camelus australis.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Palaeognathae; Struthioniformes; Struthionidae;
OC   Struthio.
OX   NCBI_TaxID=441894 {ECO:0000313|EMBL:KFV72515.1, ECO:0000313|Proteomes:UP000053584};
RN   [1] {ECO:0000313|EMBL:KFV72515.1, ECO:0000313|Proteomes:UP000053584}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N308 {ECO:0000313|EMBL:KFV72515.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) 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. Involved in maintenance of genome integrity, DNA
CC       damage response and DNA repair. {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: Chromosome, telomere
CC       {ECO:0000256|ARBA:ARBA00004574}. Nucleus
CC       {ECO:0000256|ARBA:ARBA00004123, 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; KL205656; KFV72515.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093GZH0; -.
DR   STRING; 441894.ENSSCUP00000001888; -.
DR   Proteomes; UP000053584; Unassembled WGS sequence.
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; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-UniRule.
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   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   Chromosome {ECO:0000256|ARBA:ARBA00022895};
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:UP000053584};
KW   Telomere {ECO:0000256|ARBA:ARBA00022895};
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          185..226
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   NON_TER         239
FT                   /evidence="ECO:0000313|EMBL:KFV72515.1"
SQ   SEQUENCE   239 AA;  27777 MW;  EAE8D6DDD4E346B5 CRC64;
     MAVQMTDGHR RFLQVLMSHG IMEGSEARKL HRHCCEIHKV YYAHDKLDDF INTINIHLQP
     LFMQIRKGMS EDDGRVRYAL VNLAETEITK MASDYTENEL ELFRKTMDLI ILSENGFASS
     TEILNFADQL KTKKMKKKEA EQVLKLFVED KWLSERNGEY TLHTRCIMEM EQYILSNYQD
     VARKCNICHS LAIQSQVCET CGIGMHLPCV GKYFKAQTEP HCPHCNDFWP HEIPGTSNL
//

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