ID A0A0A0AZ79_CHAVO Unreviewed; 590 AA.
AC A0A0A0AZ79;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=E3 ubiquitin-protein ligase TRIM71 {ECO:0000256|ARBA:ARBA00040205};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
DE AltName: Full=Protein lin-41 homolog {ECO:0000256|ARBA:ARBA00043228};
DE AltName: Full=RING-type E3 ubiquitin transferase TRIM71 {ECO:0000256|ARBA:ARBA00041679};
DE AltName: Full=Tripartite motif-containing protein 71 {ECO:0000256|ARBA:ARBA00042007};
DE Flags: Fragment;
GN ORFNames=N301_08807 {ECO:0000313|EMBL:KGL98833.1};
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:KGL98833.1, ECO:0000313|Proteomes:UP000053858};
RN [1] {ECO:0000313|EMBL:KGL98833.1, ECO:0000313|Proteomes:UP000053858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N301 {ECO:0000313|EMBL:KGL98833.1};
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 -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body
CC {ECO:0000256|ARBA:ARBA00004201}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KL873473; KGL98833.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A0AZ79; -.
DR STRING; 50402.A0A0A0AZ79; -.
DR Proteomes; UP000053858; Unassembled WGS sequence.
DR GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0031047; P:regulatory ncRNA-mediated gene silencing; IEA:UniProtKB-KW.
DR CDD; cd19796; Bbox2_TRIM71_C-VII; 1.
DR CDD; cd14954; NHL_TRIM71_like; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 2.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR017868; Filamin/ABP280_repeat-like.
DR InterPro; IPR001298; Filamin/ABP280_rpt.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR001258; NHL_repeat.
DR InterPro; IPR000315; Znf_B-box.
DR PANTHER; PTHR24104; E3 UBIQUITIN-PROTEIN LIGASE NHLRC1-RELATED; 1.
DR PANTHER; PTHR24104:SF48; RING-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00630; Filamin; 1.
DR Pfam; PF01436; NHL; 6.
DR Pfam; PF00643; zf-B_box; 1.
DR SMART; SM00557; IG_FLMN; 1.
DR SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF101898; NHL repeat; 1.
DR PROSITE; PS50194; FILAMIN_REPEAT; 1.
DR PROSITE; PS51125; NHL; 6.
DR PROSITE; PS50119; ZF_BBOX; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00024}; Reference proteome {ECO:0000313|Proteomes:UP000053858};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW RNA-mediated gene silencing {ECO:0000256|ARBA:ARBA00023158};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00024}.
FT DOMAIN 1..30
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT REPEAT 201..302
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT REPEAT 315..358
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 362..405
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 411..452
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 456..499
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 503..546
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 550..590
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT COILED 52..79
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 116..143
FT /evidence="ECO:0000256|SAM:Coils"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KGL98833.1"
FT NON_TER 590
FT /evidence="ECO:0000313|EMBL:KGL98833.1"
SQ SEQUENCE 590 AA; 65166 MW; D172E669E67D9018 CRC64;
VLHFYCDTCS VPICRECTMG RHVGHSFIYL QDALQDSRTL TIQLLADAQQ GRQAIQLSIE
QAQAVAEQVE MKAKVVQSEV KAVTTRHKKA LEELCFSLSP LSPPPPKVEK IRQVKAKSLY
LQVEKLRQNL NKLDNTISAV QQVLEEGRTM DILLARDRQL AQVQELKNVR GLLQPQEDDR
IMFTPPDQAL YMAIKSMGFV SSGAFAPLTK ATGEGLKRAL QGKVASFTVI GYDHDGEPRL
SGGDMISAVV MGPDGNLFGA DVSDQQNGTY LVSYRPQLEG EHLVSVMMCN QHIENSPFKV
VVKSGRSYIG IGLPGLSFGS EGDSDGKLCR PWGVSVDKEG YIIVADRSNN RIQVFKPCGT
FHHKFGTLGS RPGQFDRPAG VACDISRRIV VADKDNHRIQ IFTFEGQFIL KFGEKGTKNG
QFNYPWDVAV NAEGKILVSD TRNHRVQLFG PDGVFLNKYG FEGALWKHFD SPRGVTFNHE
GHLVVTDFNN HRLLVIHPDC QSARFLGSEG TGNGQFLRPQ GVAVDQEGRI IVADSRNHRV
QIFESNGSFL CKFGTQGSGF GQMDRPSGIA VTPDGMIVVV DFGNNRILVF
//