ID A0A2I3G178_NOMLE Unreviewed; 684 AA.
AC A0A2I3G178;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN Name=TRIM3 {ECO:0000313|Ensembl:ENSNLEP00000025963.1};
OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Nomascus.
OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000025963.1, ECO:0000313|Proteomes:UP000001073};
RN [1] {ECO:0000313|Ensembl:ENSNLEP00000025963.1, ECO:0000313|Proteomes:UP000001073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Gibbon Genome Sequencing Consortium;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSNLEP00000025963.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
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};
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DR EMBL; ADFV01111983; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01111984; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A2I3G178; -.
DR Ensembl; ENSNLET00000046943.1; ENSNLEP00000025963.1; ENSNLEG00000017418.3.
DR GeneTree; ENSGT00940000158173; -.
DR Proteomes; UP000001073; Chromosome 15.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd14960; NHL_TRIM2_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; IPR003649; Bbox_C.
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:SF21; TRIPARTITE MOTIF-CONTAINING PROTEIN 3; 1.
DR Pfam; PF00630; Filamin; 1.
DR Pfam; PF01436; NHL; 6.
DR Pfam; PF00643; zf-B_box; 1.
DR SMART; SM00502; BBC; 1.
DR SMART; SM00336; BBOX; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000001073};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00024}.
FT DOMAIN 63..107
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT REPEAT 261..362
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT REPEAT 417..460
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 464..507
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 508..545
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 549..592
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 596..639
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 640..683
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REGION 363..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 131..162
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 684 AA; 73882 MW; 0006D145734C8400 CRC64;
CHPTHSSLTL SCPVCRQTSI LPEQGVSALQ NNFFISSLME AMQQAPDGAH DPEDPHPLSA
VAGRPLSCPN HEGKTMEFYC EACETAMCGE CRAGEHREHG THKAALQRQL EAVRGRLPQL
SAAIALVGGI SQQLQERKAE ALAQISAAFE DLEQALQQRK QALVSDLETI CGAKQKVLQT
QLDTLRQGQE HIGSSCSFAE QALRLGSAPE VLLVRKHMRE RLAALAAQAF PERPHENAQL
ELVLEVDGLR RSVLNLGALL TTSATAHETV ATGEGLRQAL VGQPASLTVT TKDKDGRLVR
TGSAELRAEI TGPDGTRLPV PVVDHKNGTY ELVYTARTEG ELLLSVLLYG QPVRGSPFRV
RALRPGDLPP SPDDVKRRVK SPGGPGSHVR QKAVRRPSSM YSTGGKRKDN PIEDELVFRV
GSRGREKGEF TNLQGVSAAS SGRIVVADSN NQCIQVFSNE GQFKFRFGVR GRSPGQLQRP
TGVAVDTNGD IIVADYDNRW VSIFSLRTKI GAGRLMGPKG VAVDRNGHII VVDNKSCCVF
TFQPNGKLVG RFGGRGATDR HFAGPHFVAV NNKNEIVVTD FHNHSVKVYS ADGEFLFKFG
SHGEGNGQFN APTGVAVDSN GNIIVADWGN SRIQVFDSSG SFLSYINTSA EPLYGPQGLA
LTSDGHVVVA DAGNHCFKAY RYLQ
//