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Database: UniProt
Entry: A8XF30_CAEBR
LinkDB: A8XF30_CAEBR
Original site: A8XF30_CAEBR 
ID   A8XF30_CAEBR            Unreviewed;       978 AA.
AC   A8XF30;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 2.
DT   24-JAN-2024, entry version 101.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   Name=ncl-1 {ECO:0000313|WormBase:CBG12245};
GN   Synonyms=Cbr-ncl-1 {ECO:0000313|EMBL:CAP31252.2};
GN   ORFNames=CBG12245 {ECO:0000313|WormBase:CBG12245}, CBG_12245
GN   {ECO:0000313|EMBL:CAP31252.2};
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238 {ECO:0000313|EMBL:CAP31252.2, ECO:0000313|Proteomes:UP000008549};
RN   [1] {ECO:0000313|EMBL:CAP31252.2, ECO:0000313|Proteomes:UP000008549}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16 {ECO:0000313|EMBL:CAP31252.2,
RC   ECO:0000313|Proteomes:UP000008549};
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
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   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
CC   -!- SIMILARITY: Belongs to the TRIM/RBCC family.
CC       {ECO:0000256|ARBA:ARBA00008518}.
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DR   EMBL; HE600962; CAP31252.2; -; Genomic_DNA.
DR   AlphaFoldDB; A8XF30; -.
DR   STRING; 6238.A8XF30; -.
DR   WormBase; CBG12245; CBP43525; WBGene00033222; Cbr-ncl-1.
DR   eggNOG; KOG2177; Eukaryota.
DR   HOGENOM; CLU_007697_0_0_1; -.
DR   InParanoid; A8XF30; -.
DR   OMA; CCTLVCK; -.
DR   OrthoDB; 5387006at2759; -.
DR   Proteomes; UP000008549; Chromosome III.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd19813; Bbox1_BRAT-like; 1.
DR   CDD; cd19798; Bbox2_BRAT-like; 1.
DR   CDD; cd14959; NHL_brat_like; 1.
DR   Gene3D; 4.10.830.40; -; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR   Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR003649; Bbox_C.
DR   InterPro; IPR001258; NHL_repeat.
DR   InterPro; IPR027370; Znf-RING_euk.
DR   InterPro; IPR000315; Znf_B-box.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR24104:SF41; BRAIN TUMOR PROTEIN; 1.
DR   PANTHER; PTHR24104; E3 UBIQUITIN-PROTEIN LIGASE NHLRC1-RELATED; 1.
DR   Pfam; PF01436; NHL; 4.
DR   Pfam; PF00643; zf-B_box; 1.
DR   Pfam; PF13445; zf-RING_UBOX; 1.
DR   SMART; SM00502; BBC; 1.
DR   SMART; SM00336; BBOX; 2.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR   SUPFAM; SSF101898; NHL repeat; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS51125; NHL; 5.
DR   PROSITE; PS50119; ZF_BBOX; 2.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008549};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00024}.
FT   DOMAIN          79..119
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          244..291
FT                   /note="B box-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50119"
FT   DOMAIN          339..382
FT                   /note="B box-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50119"
FT   REPEAT          700..743
FT                   /note="NHL"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT   REPEAT          747..792
FT                   /note="NHL"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT   REPEAT          793..834
FT                   /note="NHL"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT   REPEAT          835..877
FT                   /note="NHL"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT   REPEAT          878..921
FT                   /note="NHL"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT   REGION          195..214
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          294..320
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          429..460
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   978 AA;  105246 MW;  8EACD2A7367A7A39 CRC64;
     MSESESLGGS SASTTTTAGS DEYTMSQIFG TAGRPIPLST FAGVAIPNSW GSAVSQPMLA
     GSFGLAPTPP PVIQEIIKCT LCLEPYRDPK VLACFHSFCK GCLAKHLEQP ERIICPQCNM
     ETQLSVQLGL DSLLTDFGLE SVMNKQQQLF ANLALSENGN GGAPTPSAAI PVPNAHLRPS
     MVAGSDPSNP VVGFGFSSPT SSTSGSPPLS DSPTIEEQHQ AQIAAMMQGL LNNNAAVAPV
     IAPVPAVHCN GCKSNETATS FCQDCNANLC DNCTMAHKYM HCFADHRVVE LTPAGSSASS
     TTSSTPSSSD SERSQLLASL GGKHSPQAAA AMMLLGNGKR PVLCLQHRAS ELVFFCVTCN
     LAICRDCTQA DHPAGTHQYE LISDVADKQL LKMEQLIADA RNKHADMLDM FKQVDSKQQI
     LTASLHNAHA QLDETVSTLL QAIQEQKKQL SKEIDNAFAA KQVIQLTMVD KRIQSMADKL
     SQTIEFSRRL MSFSSPAEVM VFKQLLDTRL QLFLGFNPDT SGVLNTSCEI EYLGAAGLYS
     NSSSAVQQLL GSVRGGNSNP IAIPNDFLMP SAQTGMPPTP IGRAPGSTRG IQIEQNGLSR
     SPPHHVAASL PMNAFSDSNL LRPNKDFGGS SQSLGPFSAL NGAAASADPF SSQYDKWSLG
     VEPVGSVGGL LEGGNVDEEK FQTLFPPSRS QIKRQKMIYH CKFGEFGVME GQFTEPSGVA
     VNGQGDIVVA DTNNHRIQVF DKDGRFKFQF GECGKRDGQL LYPNRVAVNR TTGDFVVTER
     SPTHQIQVYN QYGQFLRKFG ANILQHPRGV CVDNKGRIIV VECKVMRVII FDMFGNILQK
     FSCSRYLEFP NGVCTNDKNE ILISDNRAHC IKVFSYEGQY LRQIGGEGVT NYPIGVGINS
     LGEVVVADNH NNFNLTVFSQ DGTMIGALES RVKHAQCFDV ALVDDGSVVL ASKDYRLYLY
     RFLPASPSTA AAAGTGQI
//
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