ID A0A1Y2B4X7_9TREE Unreviewed; 1445 AA.
AC A0A1Y2B4X7;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=BCR39DRAFT_532887 {ECO:0000313|EMBL:ORY29145.1};
OS Naematelia encephala.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Naemateliaceae; Naematelia.
OX NCBI_TaxID=71784 {ECO:0000313|EMBL:ORY29145.1, ECO:0000313|Proteomes:UP000193986};
RN [1] {ECO:0000313|EMBL:ORY29145.1, ECO:0000313|Proteomes:UP000193986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=68-887.2 {ECO:0000313|EMBL:ORY29145.1,
RC ECO:0000313|Proteomes:UP000193986};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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:ORY29145.1}.
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DR EMBL; MCFC01000027; ORY29145.1; -; Genomic_DNA.
DR STRING; 71784.A0A1Y2B4X7; -.
DR InParanoid; A0A1Y2B4X7; -.
DR OrthoDB; 1342875at2759; -.
DR Proteomes; UP000193986; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd16702; RING_CH-C4HC3_MARCH6; 1.
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:UP000193986};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 111..135
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 647..670
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 802..823
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 835..855
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 862..880
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 886..909
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1151..1172
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1192..1212
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1245..1268
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1288..1306
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1341..1369
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 14..75
FT /note="RING-CH-type"
FT /evidence="ECO:0000259|PROSITE:PS51292"
FT REGION 321..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 374..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..517
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..548
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1445 AA; 160837 MW; F6585D198C44E02D CRC64;
MADPDISVDV LRDEAAEEGD VCRVCRVEGD DDDPLIYPCK CSGSVRYVHP SCFKSWLAHS
QKQRCEICGH PYTFSKIYQS YIPSTIPFLV YLRQAGLFLQ RIAYNVVRVE LAILAWLVVL
PSCNMFTLQG VVWMADQLPW SFTSVPSSGN SSHSEGALQA LTNSSLVNST SPASLQEQIS
QSRVVPRLMT GITILVERLF RLVTFAWVTY SEEEELSAVI RFLFRGQLLT IVLAAAVFGV
MVLRTVLEEN AFGRDFGPAH PESDEPVDPD EWIVRKGVAY KKDEAGMEEL RKAEAPLQLD
NKQREEVKKL VGVLKETRAT TRTRKADVGK KRARKEKGKQ GEGESPKQMP DILGQPDDSE
DIVLPDDMSI LAAVDSNPET PHYPTSTASI DISSAEDSDN IDIPRTVLRP LFQRPAWSIE
VTASTSSSER NPSASAGDQA PPLPDSPLAL LDDEIDQRPL LGSLPMTPPR PSPALQSPMG
VEYRAPELIG EKDGEDEESL AASPFKGKGK ERAPDSSDRG SNNGLSTNPY NDISSEAQEP
STESDPVEAE VTHTIPRPIG EIPEQLRAEV EEAIMLLADE GLEVQMEEGA RPFPQLDIQV
AEVDDHVDVE FAEEGDWMWD DAGGEGFWGP VMEIVGIVGP WANLIQNLMI CIVIGSAATT
LLVGIPLMIG KTLLAADFVR SFLYTGRLVI KGTRVVTDPL IDISTEILRD VVVRPALSSF
HALEAIVADK LGLQGVLSSR ISHLDASIFS LFAAPFQSGD NHGGSKSIDI LALIGNRTYR
AYQRYRSFGM TAAFSTNLAS RLWCLAVGYV GFITTFGSIT LLGELDGAEG ELGRSIAFIK
VAIFTILDAI ILPFLLGCSI DFYTIPLFSG ASIWTRIDWF RTAPGSAYFV HLFIGSTFTY
YFVTMLLWIR GDIRRGALYW MLDPRDPKFS ITKQLLEKST WWSVQRRFSI VKQHLIVQFW
LFGVWCWGLK LLGSSSVPEL RLSVGPISSI PFDLLFIHLA IPPSIKALRL QRRLRFLWRY
LFRRAVALFG LTDLVYGKRK VGQLPDITPP AWLETLWKPA DFIYRTFVEI YDPIQGGSVR
APSSNVTFEN LHGRKPDKRG AFIALDESGS PKSQEDKIRL LRQDRLTRSK ARDPKKDFTV
LEIPPYWLAR VWALIYLTLI SLGIGIGVVT LLPVVLGRAA FDILGVKQLH DGYSFFAGCY
ILYFIAKISR AVGKYVVKSR RAGVLYHSSA STWLKRSVMS WINKVYTFSI LFGVLPVLTG
LCIELHLGIL VRYGLALSVK PVIHLWDAWA NGLVSLSVMI GVVEMYSPRI VRNRNANATY
ARIWSLHNIY RRPSRQTAKE VTTAVLPLAL WGMLYILVPA SIAVSMALLN IVRPSSAIAY
LGMSTEEYNS FMCKLLAVTP RHSFHRLYIS YSPHRIPNFD YPNHASPCTV LAQETLDSST
TIHDR
//
