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Database: UniProt
Entry: A0A0A0A312_CHAVO
LinkDB: A0A0A0A312_CHAVO
Original site: A0A0A0A312_CHAVO 
ID   A0A0A0A312_CHAVO        Unreviewed;       545 AA.
AC   A0A0A0A312;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   RecName: Full=TNF receptor-associated factor {ECO:0000256|PIRNR:PIRNR015614};
DE            EC=2.3.2.27 {ECO:0000256|PIRNR:PIRNR015614};
GN   ORFNames=N301_14638 {ECO:0000313|EMBL:KGL88436.1};
OS   Charadrius vociferus (Killdeer) (Aegialitis vocifera).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Charadriiformes; Charadriidae; Charadrius.
OX   NCBI_TaxID=50402 {ECO:0000313|EMBL:KGL88436.1, ECO:0000313|Proteomes:UP000053858};
RN   [1] {ECO:0000313|EMBL:KGL88436.1, ECO:0000313|Proteomes:UP000053858}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N301 {ECO:0000313|EMBL:KGL88436.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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|PIRNR:PIRNR015614};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC       {ECO:0000256|ARBA:ARBA00004544}. Lipid droplet
CC       {ECO:0000256|ARBA:ARBA00004502}. Nucleus
CC       {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the TNF receptor-associated factor family. A
CC       subfamily. {ECO:0000256|ARBA:ARBA00006608}.
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DR   EMBL; KL870437; KGL88436.1; -; Genomic_DNA.
DR   RefSeq; XP_009893892.1; XM_009895590.1.
DR   AlphaFoldDB; A0A0A0A312; -.
DR   STRING; 50402.A0A0A0A312; -.
DR   GeneID; 104295805; -.
DR   KEGG; cvf:104295805; -.
DR   CTD; 7189; -.
DR   OrthoDB; 2913784at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000053858; Unassembled WGS sequence.
DR   GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR   GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005164; F:tumor necrosis factor receptor binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:UniProt.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
DR   GO; GO:0043122; P:regulation of canonical NF-kappaB signal transduction; IEA:InterPro.
DR   CDD; cd03776; MATH_TRAF6; 1.
DR   CDD; cd16643; mRING-HC-C3HC3D_TRAF6; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 3.
DR   InterPro; IPR002083; MATH/TRAF_dom.
DR   InterPro; IPR012227; TNF_rcpt-assoc_TRAF_met.
DR   InterPro; IPR008974; TRAF-like.
DR   InterPro; IPR037309; TRAF6_MATH.
DR   InterPro; IPR027139; TRAF6_RING-HC.
DR   InterPro; IPR041310; TRAF6_Z2.
DR   InterPro; IPR049342; TRAF_MEP1_MATH_dom.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   InterPro; IPR001293; Znf_TRAF.
DR   PANTHER; PTHR10131; TNF RECEPTOR ASSOCIATED FACTOR; 1.
DR   PANTHER; PTHR10131:SF152; TNF RECEPTOR-ASSOCIATED FACTOR 6; 1.
DR   Pfam; PF21355; TRAF-mep_MATH; 1.
DR   Pfam; PF18048; TRAF6_Z2; 1.
DR   Pfam; PF13923; zf-C3HC4_2; 1.
DR   Pfam; PF02176; zf-TRAF; 1.
DR   PIRSF; PIRSF015614; TRAF; 1.
DR   SMART; SM00061; MATH; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF49599; TRAF domain-like; 3.
DR   PROSITE; PS50144; MATH; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
DR   PROSITE; PS50145; ZF_TRAF; 2.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|PIRNR:PIRNR015614};
KW   Lipid droplet {ECO:0000256|ARBA:ARBA00022677};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRNR:PIRNR015614}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Receptor {ECO:0000313|EMBL:KGL88436.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053858};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRNR:PIRNR015614};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00207}.
FT   DOMAIN          70..109
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          151..199
FT                   /note="TRAF-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50145"
FT   DOMAIN          204..258
FT                   /note="TRAF-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50145"
FT   DOMAIN          373..522
FT                   /note="MATH"
FT                   /evidence="ECO:0000259|PROSITE:PS50144"
FT   ZN_FING         151..199
FT                   /note="TRAF-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00207"
FT   ZN_FING         204..258
FT                   /note="TRAF-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00207"
FT   COILED          315..370
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   545 AA;  62082 MW;  99311A70EF5A8922 CRC64;
     MSLLYSDNSC GARDVESGCC AAMASACSVG AKEDSVSVSS ATGNPPSSFT EETQGYDVEF
     DPPLESKYEC PICLMALREA VQTPCGHRFC KGCIVKSIRD AGHKCPVDNE ILLENQLFPD
     NFAKREILSL TVKCPNKGCS MKMELRHLED HQLQCDFSAV ECPQCQGAFQ KNHLKEHMTQ
     ECPRRQVCCP NCATSMAYED KELHDQTCPL ANVFCEYCNT VLIREQMPNH YDNDCPTAPV
     PCFYSAFGCP EKMQRNELAR HMQEFTQVHM RMMAQSFQNI SVTATNPVPF INGLTFEPAV
     FSHMSHAAYD CNPEVENFKE TIQQLEGRLV RQDHQIRELI AKMETQNTHM AELKRTIRNL
     EVKITEMEAQ QCNGIYIWKI ENFSGLQKAQ EEERPVVMHS PGFYTGKPGY KLCLRLHIQL
     PNAQRCANFI SLFVHTMQGE YDSHLPWPFQ GTIRLSILDQ SEGPERQNHE EVMEAKPELL
     AFQRPTIHRN PKGFGYVTFM HLQTLKQRTF VKDDTLLVRC EVLTRLDLNS LRREGFQARS
     TDGAM
//
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