UniProt: A0A0K3AXB1

Database: UniProt
Entry: A0A0K3AXB1_CAEEL

LinkDB:  A0A0K3AXB1_CAEEL 
Original site:  A0A0K3AXB1_CAEEL

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Ontology (2)   
   GO (2)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   NCBI-Gene (1)   
   WORMBASE (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (19)   
   InterPro (9)   
   Pfam (3)   
   PROSITE (4)   
   SMART (3)   
Literature (1)   
   PubMed (1)   
All databases (27)   

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ID   A0A0K3AXB1_CAEEL        Unreviewed;       913 AA.
AC   A0A0K3AXB1;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 52.
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|EMBL:CTQ86627.1,
GN   ECO:0000313|WormBase:ZK112.2f};
GN   ORFNames=CELE_ZK112.2 {ECO:0000313|EMBL:CTQ86627.1}, ZK112.2
GN   {ECO:0000313|WormBase:ZK112.2f};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239 {ECO:0000313|EMBL:CTQ86627.1, ECO:0000313|Proteomes:UP000001940};
RN   [1] {ECO:0000313|EMBL:CTQ86627.1, ECO:0000313|Proteomes:UP000001940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2 {ECO:0000313|EMBL:CTQ86627.1,
RC   ECO:0000313|Proteomes:UP000001940};
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RA   Sulson J.E., Waterston R.;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the TRIM/RBCC family.
CC       {ECO:0000256|ARBA:ARBA00008518}.
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DR   EMBL; BX284603; CTQ86627.1; -; Genomic_DNA.
DR   RefSeq; NP_001299927.1; NM_001312998.1.
DR   AlphaFoldDB; A0A0K3AXB1; -.
DR   SMR; A0A0K3AXB1; -.
DR   EnsemblMetazoa; ZK112.2f.1; ZK112.2f.1; WBGene00003559.
DR   GeneID; 176084; -.
DR   AGR; WB:WBGene00003559; -.
DR   WormBase; ZK112.2f; CE50296; WBGene00003559; ncl-1.
DR   OrthoDB; 5387006at2759; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00003559; Expressed in pharyngeal muscle cell (C elegans) and 4 other cell types or tissues.
DR   ExpressionAtlas; A0A0K3AXB1; baseline and differential.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
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; IPR047153; TRIM45/56/19.
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; PTHR25462; BONUS, ISOFORM C-RELATED; 1.
DR   PANTHER; PTHR25462:SF300; PROTEIN CBR-NCL-1; 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   1: Evidence at protein level;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Proteomics identification {ECO:0007829|EPD:A0A0K3AXB1,
KW   ECO:0007829|PeptideAtlas:A0A0K3AXB1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001940};
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          22..62
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          189..236
FT                   /note="B box-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50119"
FT   DOMAIN          280..323
FT                   /note="B box-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50119"
FT   REPEAT          635..678
FT                   /note="NHL"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT   REPEAT          682..727
FT                   /note="NHL"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT   REPEAT          728..769
FT                   /note="NHL"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT   REPEAT          770..812
FT                   /note="NHL"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT   REPEAT          813..856
FT                   /note="NHL"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT   REGION          238..273
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        238..268
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   913 AA;  98816 MW;  60B7FA7C034C0C59 CRC64;
     MLAGSFGLAP TPPPVIQEIV KCTLCLEPYR DPKVLACFHS FCKGCLAKHL EQPERIICPQ
     CHMETQLSVQ LGLDSLLTDF GLESVMNKQQ QLFANMGLSD IGAPTPSTAI PVPNAHLHPS
     MVAGSDPSNP VVGFGFGSPS STTSSSPPLS NSPTIEQQQH AQLTAMMQGI MSNNNVAVSN
     GSGVQVASVP AVHCSGCKSN ETATSFCQDC NANLCDNCTM AHKFMHCFAD HRVVSLTTPG
     TGSSSSSTSS SSSASSTSSH QVPSLGGKQS PDSMMLGSGK RSVLCLQHRA SELVFFCVSC
     NLAICRDCTV SDHPSGTHQY ELIADVADKQ MLKMEQLIAD ARSKHADMLD MFKQVDNKQQ
     VLTASLHNAH AQLEETVSNL INVIQDQKKT LAKDIDNAFA AKQIQLTMVD KRIQSMADKL
     SQTIEFSRRL MSFASPAEVM VFKQLLDTRL QLFLGFNPDT SGVLMTPCEI EYLGAAGLFN
     NSASTVSQLL GSVHGGSPIN NAPAANDFLM PQAGLAPIGR AQSRIIPIEQ NQLARSPPHH
     IAGSLPMNAY SDSNLLRPNK DFGGSSQSLG PFNPLGASVP GAAADPFSSQ YDKWSLGVEP
     SVGGLLEGGN VDEEKFQTLF PPSRSQIKRQ KMIYHCKFGE FGVMEGQFTE PSGVAVNGQG
     DIVVADTNNH RIQVFDKEGR FKFQFGECGK RDGQLLYPNR VAVNRTTGDF VVTERSPTHQ
     IQVYNQYGQF LRKFGANILQ HPRGVCVDSK GRIIVVECKV MRVIIFDMFG NILQKFSCSR
     YLEFPNGVCT NDKNEILISD NRAHCIKVFS YEGQYLRQIG GEGVTNYPIG VGINSLGEVV
     VADNHNNFNL TVFSQDGTMI GALESRVKHA QCFDVALVDD GSVVLASKDY RLYLYRFLPA
     TSGQSTSSAS SQI
//

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