ID D7G9B1_ECTSI Unreviewed; 1644 AA.
AC D7G9B1;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=Esi_0097_0033 {ECO:0000313|EMBL:CBJ28254.1};
OS Ectocarpus siliculosus (Brown alga) (Conferva siliculosa).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; PX clade; Phaeophyceae;
OC Ectocarpales; Ectocarpaceae; Ectocarpus.
OX NCBI_TaxID=2880 {ECO:0000313|EMBL:CBJ28254.1, ECO:0000313|Proteomes:UP000002630};
RN [1] {ECO:0000313|EMBL:CBJ28254.1, ECO:0000313|Proteomes:UP000002630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ec32 / CCAP1310/4 {ECO:0000313|Proteomes:UP000002630};
RX PubMed=20520714; DOI=10.1038/nature09016;
RA Cock J.M., Sterck L., Rouze P., Scornet D., Allen A.E., Amoutzias G.,
RA Anthouard V., Artiguenave F., Aury J.M., Badger J.H., Beszteri B.,
RA Billiau K., Bonnet E., Bothwell J.H., Bowler C., Boyen C., Brownlee C.,
RA Carrano C.J., Charrier B., Cho G.Y., Coelho S.M., Collen J., Corre E.,
RA Da Silva C., Delage L., Delaroque N., Dittami S.M., Doulbeau S., Elias M.,
RA Farnham G., Gachon C.M., Gschloessl B., Heesch S., Jabbari K., Jubin C.,
RA Kawai H., Kimura K., Kloareg B., Kupper F.C., Lang D., Le Bail A.,
RA Leblanc C., Lerouge P., Lohr M., Lopez P.J., Martens C., Maumus F.,
RA Michel G., Miranda-Saavedra D., Morales J., Moreau H., Motomura T.,
RA Nagasato C., Napoli C.A., Nelson D.R., Nyvall-Collen P., Peters A.F.,
RA Pommier C., Potin P., Poulain J., Quesneville H., Read B., Rensing S.A.,
RA Ritter A., Rousvoal S., Samanta M., Samson G., Schroeder D.C., Segurens B.,
RA Strittmatter M., Tonon T., Tregear J.W., Valentin K., von Dassow P.,
RA Yamagishi T., Van de Peer Y., Wincker P.;
RT "The Ectocarpus genome and the independent evolution of multicellularity in
RT brown algae.";
RL Nature 465:617-621(2010).
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: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; FN649212; CBJ28254.1; -; Genomic_DNA.
DR STRING; 2880.D7G9B1; -.
DR EnsemblProtists; CBJ28254; CBJ28254; Esi_0097_0033.
DR eggNOG; KOG1609; Eukaryota.
DR InParanoid; D7G9B1; -.
DR OrthoDB; 1342875at2759; -.
DR Proteomes; UP000002630; Chromosome LG09.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR011016; Znf_RING-CH.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR13145:SF0; E3 UBIQUITIN-PROTEIN LIGASE MARCHF6; 1.
DR PANTHER; PTHR13145; SSM4 PROTEIN; 1.
DR Pfam; PF12906; RINGv; 1.
DR SMART; SM00744; RINGv; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51292; ZF_RING_CH; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000002630};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 177..201
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 564..589
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 842..862
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 994..1017
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1037..1057
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1098..1118
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1156..1174
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1375..1399
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1419..1439
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1460..1479
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1499..1521
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1589..1609
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 48..137
FT /note="RING-CH-type"
FT /evidence="ECO:0000259|PROSITE:PS51292"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 415..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 628..668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 765..808
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 886..913
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 945..964
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1212..1360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..62
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..668
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 765..781
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1226..1247
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1644 AA; 166320 MW; 2333E398C41694A9 CRC64;
MKGGWAKSYG GSAGAEGSGG RGGDGDGGEE EGAEGRGGDG AVRGDAGSDS EEEPECRVCR
GDDEGGARPL VHPCRCRGSI KYVHQDCLVE WLRSRGGGGG AARGGGGAEG GAGGVPDDAS
ALQAQRCELC REKLVFKARY RPGAPAKLGI YQFVRGAVRR ATPRLLDAFR GALNMQMWGL
AIPVLYCLLF RLGIGLSLLL AQEFSAIFLG AGGGGPPSAV AGGGRGVSLP GLERVGWGSW
MDILGDWCGG VGLMIGVMCL GPPCVELALE FVNLVKALPV VLERWWLGDE DELRVAGGPR
NEQDPPDDIL VEVMLDRVRD RALHAAAAAH DAAAAAHGAA AAARDAAAAA TLPLPAGRAA
AVPPIGEEGG EAAAPAAAGG EVEASGVPSV GGGGGDVGDY DGRAVAAAAE VPIPPERGVM
DGEPPVVGRG TGGPVDGNNG GGGGGGGGGG GGAELPRDGG GAAAGGGEED NAVPAGVGGN
GAPQAGEHGV GVAVPPVGDG GEGRVLAVGG GGVAAGIQGA GGGEGEGGVH VVLGLLGRVE
WFLAGVLEQL AAPPRDEDVD GEALFLWGWP AVGAAGSFLA FMALLLLFAQ TVPYATFHVA
SGAVNRSRPL PLRQQRDTSW SPYSFFFRDS SSPPPPPPPS SSSSSSSSSS PEGPFSPAPL
RSTPDWSSVF RPSPAADAAL FVLARPPHVE THGGGGGGGG GGGGWGERGG LLLLPTASSR
AWWSISPSGR LARVSSSAWE TAAAGVSAGA GPSAVAPAAA TASSCNTQQG SANSSSGSSG
VAGAAAGGRR GETEGRRGDG AAAGGGSEGR EEWYAMTLLF LRGPVIPGTS GLRAGAVIWQ
TVQGHCILAL TLLLLLALYS VVRLRFVVLA RHLEVAATAG NNGGVDSGLA TGGNGVRGQR
EMGAGAGDPN NDAGGGVGDE AAAAVAVANA GNAFRRGRDG FIPGMGPRLG GGGPGGGGRL
WMRGGGPAAE ARAAGGGGGG MLERDGQMGL DLKVLTMGLL ELLVLPLWVG VAADLFSLPL
LASTLEARAA WALANPFSSL ALHWGAGSMA VGVVSCLGRE IGRALKPDLL PPWANRPAEQ
GLEEVLVRMT NENFLAQLRS FLVSVVAYPA ALALMVMVPT HCKGFLAPRL TSRFLPEFWL
SPMVLGIGEP TQGDRLGMDL VIVHFILPVV MEHLKIRGPV RRAACWVLSA ACGATGTRGL
LLHPALVAGR GAAANDPDDL DDLELPQPQA PPPPPPQIPP LPVLGNPQPP AGGGAQQQQA
GDGELNDNEG GAADERGVGE GGGGGGGGDA YGVGGEAPRA VRGEGGALGE GGEGIGRVEE
EGGDGGGVVG GGVEREEEGG GGGAVAQEQE EEEEEGGEGY ERRGAFAHVV EAMRVYAAGS
LVCIALAVVP AATVLLPLVT GRSLFAAMGL PLDDDLPPLV AGGLLCAAWA WALSALIRLQ
VAAGQHRRLL CNALMLAGKW FVIGALLVGA LPGLTGLLVH DALRGPLPPT EETAALTWGK
IWALGLVCVK LWARCVLAGA VRDEAWQGRL RRLRENGFRG VDFKFTMLEV CFPLLDVVGQ
FYFWPHLLNR FALPLLVANQ RDLRVIQKGM PFVFLLLKAL WSAAMFVVNK MKALHDLIRD
DEYLVGLELE NMPPQGHADD ATTS
//
