ID A0A151Z5A1_TIELA Unreviewed; 1355 AA.
AC A0A151Z5A1;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 18-JUN-2025, entry version 42.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN ORFNames=DLAC_10317 {ECO:0000313|EMBL:KYQ89087.1};
OS Tieghemostelium lacteum (Slime mold) (Dictyostelium lacteum).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Raperosteliaceae; Tieghemostelium.
OX NCBI_TaxID=361077 {ECO:0000313|EMBL:KYQ89087.1, ECO:0000313|Proteomes:UP000076078};
RN [1] {ECO:0000313|EMBL:KYQ89087.1, ECO:0000313|Proteomes:UP000076078}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TK {ECO:0000313|EMBL:KYQ89087.1,
RC ECO:0000313|Proteomes:UP000076078};
RA Gloeckner G., Schaap P.;
RT "Dictyostelia acquired genes for synthesis and detection of signals that
RT induce cell-type specialization by lateral gene transfer from
RT prokaryotes.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KYQ89087.1}.
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DR EMBL; LODT01000042; KYQ89087.1; -; Genomic_DNA.
DR FunCoup; A0A151Z5A1; 304.
DR STRING; 361077.A0A151Z5A1; -.
DR EnsemblProtists; KYQ89087; KYQ89087; DLAC_10317.
DR InParanoid; A0A151Z5A1; -.
DR OMA; PWSEHGD; -.
DR OrthoDB; 10009520at2759; -.
DR Proteomes; UP000076078; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR CDD; cd22583; Rcat_RBR_ARI7-like; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR003892; CUE.
DR InterPro; IPR031127; E3_UB_ligase_RBR.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR Pfam; PF01485; IBR; 1.
DR Pfam; PF22191; IBR_1; 1.
DR SMART; SM00647; IBR; 2.
DR SUPFAM; SSF57850; RING/U-box; 3.
DR SUPFAM; SSF46934; UBA-like; 1.
DR PROSITE; PS51140; CUE; 1.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000076078};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
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 TRANSMEM 1330..1351
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 424..467
FT /note="CUE"
FT /evidence="ECO:0000259|PROSITE:PS51140"
FT DOMAIN 830..1049
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 834..874
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 306..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 479..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 562..613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 665..696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 766..810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..324
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..375
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..392
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..414
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..499
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 685..696
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 776..791
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1355 AA; 153503 MW; 147E32358E78C7D4 CRC64;
MGIQTSKLNK LKKNSFSNNH STNVKYPKKS SKTPNSNVST PTIVKPSVTT QRKSNTTNSD
TSKDDNSEYD NSTGDDDNEE DIIDDTWDDI AFLPTKISDQ NVPIIAASQL FYLSEHISVG
NSPMESNSST PYQQQQQQQH PTPRLLTMSR DTIQSVGNQS GSFYQQYNSN SQLLLNSSSS
ISSRSKSNWN WYSMENFNEG LIGTENDKRV LILTVDDIIY VVDNQIKRAS EIIGLSSALT
SVLLLQYKWN YDLLIQQFID KGADHLFLTA GLPPNPTPFT VNDTIIELLK PIKDLQKLNT
QTLLMNSKSN SLSPSPSTLT NISSRRVRWE NSDTQSQLHT QNARFSSRNN RSSKNGAGSI
GSGSNSSSNR YALSSFGDDY DDNTNDNDDE YQHDDNLSIP SNNQDISNNS NNSNTIKQQE
RNVFIQSLIT LIQEVFPYFN SEDIAEILPR YDNNHERVIN SILEGSLIIP IRITNSNTNT
NNDRNQLFIN NLSNNNNNNY QQDKKSSTNT RKNPIQHLKY DIENPPPSPK PIRRMGFISQ
LHRDSRDDLM ILANTRSTFS NFSNSPSLFT ADNNNNNINN NNNNNYNNNN NRTTTNNSSS
GSSGLASSKS TTNLMKNSNS INFMISEEDK NFNNLPQSPS TSTHKPLSYS SDSFLSNLED
KFTSTFSNND LSDTDSDNYS YKKPTTTTTT TTTTTSNFTT YNNNNNYNNN NNNNNYNNFN
FIIRNTNVGI PFSLTRSALI NTDDIENDDN DESSKDGADI QVLEDGAGSQ HEDLQNESND
NSETNSYTNQ MPPMEIAMDT DDQHSPPSSF QLPKAINNFN KPKDGSVTEE IITCMVCLSE
YEKSQTFSLS CQHYYCLDCW RSYIYTKINE GNSCLFTKCI NPQCKFILDI SVFRHLLDEG
KYQKYIWLFI KSFIENCPKT SWCTNPESCG MVIYYNGIDL PSNMNITCTC KWRFCFHCGD
EYHLPSNCKQ ISDWKQLKNK EGQNAIWLTQ NTKKCPQCKI HIEKNEGCMH MTCRKNAGGC
GFEFCWLCKG PWSEHGDRTG GFFSCNRYDS LKHDTPDLDK TFGTYVHHFQ RYNYHHNAKK
VANQKQSQLC TIRDIILQLQ KNNDTSNGDL SPSSASLINV ILSPITNSSN SNSNNNNIYS
GGWNKEYLLD CVNLIIECRH TLKYTYVYGF YLADEKEREL FEFLQEDLEK STEHLCEVLY
REIDNLDALL QSQSNHMSSL SSSSSFSSSL SLSNSTPNFG NLPTNQIQQN SSTINGAISQ
NTENHIKNYH KVTKKFLENL LSGCQNGLIS NYGPPSDKPP SHTKKHSKNS LQQLLKRKLT
RNSNASLSSL LSYIFKMIIV VGYCCCCYYI WYTGV
//
