ID H2TDG7_TAKRU Unreviewed; 1210 AA.
AC H2TDG7;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 3.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN Name=LOC101077719 {ECO:0000313|Ensembl:ENSTRUP00000022709.3};
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000022709.3, ECO:0000313|Proteomes:UP000005226};
RN [1] {ECO:0000313|Ensembl:ENSTRUP00000022709.3, ECO:0000313|Proteomes:UP000005226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551351;
RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT "Integration of the genetic map and genome assembly of fugu facilitates
RT insights into distinct features of genome evolution in teleosts and
RT mammals.";
RL Genome Biol. Evol. 3:424-442(2011).
RN [2] {ECO:0000313|Ensembl:ENSTRUP00000022709.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.;
CC EC=2.3.2.31; Evidence={ECO:0000256|ARBA:ARBA00001798};
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DR AlphaFoldDB; H2TDG7; -.
DR Ensembl; ENSTRUT00000022803.3; ENSTRUP00000022709.3; ENSTRUG00000009032.3.
DR GeneTree; ENSGT00940000165758; -.
DR HOGENOM; CLU_009823_1_0_1; -.
DR Proteomes; UP000005226; Chromosome 12.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR CDD; cd20346; BRcat_RBR_ANKIB1; 1.
DR CDD; cd20361; Rcat_RBR_ANKIB1; 1.
DR CDD; cd16774; RING-HC_RBR_ANKIB1; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR045840; Ariadne.
DR InterPro; IPR031127; E3_UB_ligase_RBR.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR047564; Rcat_RBR_ANKIB1.
DR InterPro; IPR047563; RING-HC_RBR_ANKIB1.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR11685:SF465; ANKYRIN REPEAT AND IBR DOMAIN-CONTAINING PROTEIN 1; 1.
DR PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF19422; Ariadne; 1.
DR Pfam; PF01485; IBR; 2.
DR SMART; SM00248; ANK; 2.
DR SMART; SM00647; IBR; 2.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF57850; RING/U-box; 3.
DR PROSITE; PS50088; ANK_REPEAT; 1.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000005226};
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:PRU00175}.
FT REPEAT 146..178
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 338..576
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 342..388
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 768..802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 952..1002
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1016..1037
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1063..1151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 578..639
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 970..984
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1063..1081
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1137..1151
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1210 AA; 135562 MW; CC88D62307936E0B CRC64;
MGNTATKFRK ALVGGDEGLA WQLYEGNPQF REGLDPNASY GEQYQHNTAL HYICRHAMTR
LLRSFLFSKE GNPNKRNVHN ETCLHVLCQG PQILLLSEGA LSPRLARPQR DEQRRAECLQ
MILSWTGARL EGGQYEKANV NATDNHNSTC MHYAAAAGMK ICVELLIQSE ADLFVEDEEK
LTPCDHAERH HHTELALSLE SQMVFSSSSF AYFMIAPYHS NINLALSQPY EGLKLQDLRR
LKDMLIVETA DMLQAPLFTA EALLRAHDWD REKLLEAWML DADGCCQRSG VAMPTPPPCG
YNAWDTLPSP RTPKTPRSPL TLTLTSPTDS CLTPGEEGLS ACGICLCSIS VFEDPVDMSC
GHEFCRACWE GFLNVKIQEG DAHNIFCPAY ECYQLVPVHV IESVVSREMD QRYLQFDIKA
FVENNPAIRW CPAARCERAV RLTRPGPGDS DPQSFPLLPS PAVDCGKGHL FCWECLGEAH
EPCDCQTWRN WLQKVKEMKP EELAGVGEAY EDAANCLWLL TNSKPCANCK SPIQKNEGCN
HMQCAKCKYD FCWICLEEWK KHSSSTGGYY RCTRYEVIQQ LEEQSKEMTE EAEKKHKSFQ
ELDRFMHYYT RFKNHEHSYE LEQKLLKTAK EKMEQLSRAF ISTPPDTRFI EDGVCELLKT
RRILKCSYPY GFFLQQGSTQ KEIFELMQTD LEMVVEDLAQ KVNRPYLRTP CHKIISAARL
VQQKRQEFLA SVARGVAPND SPEPPRRNYP GGSWDWEYLG FASPEEYRRR HRPRRRGDML
SLHSLRSSTP ERGEGRRRAL GSLDEDDPNI LLAIQLSLQE SGHLGHLGAR GSPRSTSLPP
PPPTLSAELL ELGDSLMKLG NITTTNDLDS HAQVQRCSHH VHSTPAGPYN IEPAYSNCSH
RPEENAQSSP YALDHLAITD PCFSSKEQGY RHATGYMVEA DRNQNLAQPS SYMQEHAAVC
DRTAKPDSSY SHLQEHSSSN PQGRPAAYGL KRPSKPDLQP PAQLCLLSPE LEPEHLLSPV
IPRGGPFSPN DPQSLESLDP AASAQLLDNI MAWFNNNINP QNNPQSLALI PSPPTTESDS
SPDTHTEAES KSQASREVTP VPIWQPLEGE PEADTGSSSP CPGALGVEGP KTSRPSSLDL
ENKKAVEEGG EGRCVAELSL DEAYTHTHSH PHCGNSPAHT ATATERDLAF NPQLEGGRSP
EEWEEQVHLV
//
