ID A0A3B3ZU03_9GOBI Unreviewed; 664 AA.
AC A0A3B3ZU03;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
OS Periophthalmus magnuspinnatus.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Gobiaria; Gobiiformes; Gobioidei; Gobiidae; Oxudercinae; Periophthalmus.
OX NCBI_TaxID=409849 {ECO:0000313|Ensembl:ENSPMGP00000008188.1, ECO:0000313|Proteomes:UP000261520};
RN [1] {ECO:0000313|Ensembl:ENSPMGP00000008188.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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};
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 AlphaFoldDB; A0A3B3ZU03; -.
DR STRING; 409849.ENSPMGP00000008188; -.
DR Ensembl; ENSPMGT00000008715.1; ENSPMGP00000008188.1; ENSPMGG00000006784.1.
DR Proteomes; UP000261520; Unplaced.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd14961; NHL_TRIM32_like; 1.
DR CDD; cd16587; RING-HC_TRIM32_C-VII; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 2.
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; 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; PTHR25464:SF3; E3 UBIQUITIN-PROTEIN LIGASE TRIM32; 1.
DR PANTHER; PTHR25464; TRIPARTITE MOTIF-CONTAINING PROTEIN 2-LIKE PROTEIN; 1.
DR Pfam; PF01436; NHL; 3.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR SMART; SM00336; BBOX; 1.
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; 1.
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 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 20..65
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 96..139
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT REPEAT 368..411
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 425..468
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 474..509
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 572..615
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 623..656
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT COILED 140..167
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 664 AA; 73071 MW; 79D091F866996F6E CRC64;
MMAVECPQLD PDLMREVLEC PICLETYNQD QLRPKLLQCG HTVCRQCLEK LLANTINGVR
CPFCSKVSRM SSISQLADNL TVLKILDCTT SCSAAAAALM CKSCCTRLPR QYCHECAVVL
CELCKADGHM LQGHNVQPIR VAAEQRRKEL GAKLESLRDV MGEIQKKKTV IENISKTLIC
KYRAVRLQEE LGRSRRTFTA TMSELEKTNG QVLEEQTYLL NIAEVKVVSR CDYLTMRVRQ
SDTALLKEDG GSSDEDEELD IKSSLPTTFN LQEPELVVIE QSKTLEVGKL TAKAYTVSTA
DEESTLDTAL EGAEGAMGPS LDLYRDVDMS ASVDEAICGS PAHFKSKSLD AAEPPGGTNS
ELPACQFVKR MGCKGTLPGL FNLPVSICVT PQGEVLVADR GNYRIQIFNR KGFQREIRRN
ASSIDNFVLS FLGADLPNLI PLSIAVTPQG LIGVTDNYDN SVKVYTMDGQ CVACHKNQLI
KPWGIAAMPT GQFVVSDVEG GKLWCLAVDR NIGVVSYTRL CSAVRPKFVT CDPSGTVYFT
QGLALNFEKR HNEPHLEGGF SIGSVGSDGQ LGKQLSHFFS ENEDFRCITG MCVDNNGDLL
VTDSGRKEIL QFPKEGGYKI LIQEGLTCPV GVATTQKGQL LVLDCWDHCV KVYTYIQRRH
SSTS
//
