ID A0A067P7J3_9AGAM Unreviewed; 1566 AA.
AC A0A067P7J3;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=JAAARDRAFT_81797 {ECO:0000313|EMBL:KDQ50759.1};
OS Jaapia argillacea MUCL 33604.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Jaapiales; Jaapiaceae; Jaapia.
OX NCBI_TaxID=933084 {ECO:0000313|EMBL:KDQ50759.1, ECO:0000313|Proteomes:UP000027265};
RN [1] {ECO:0000313|Proteomes:UP000027265}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUCL 33604 {ECO:0000313|Proteomes:UP000027265};
RX PubMed=24958869; DOI=10.1073/pnas.1400592111;
RA Riley R., Salamov A.A., Brown D.W., Nagy L.G., Floudas D., Held B.W.,
RA Levasseur A., Lombard V., Morin E., Otillar R., Lindquist E.A., Sun H.,
RA LaButti K.M., Schmutz J., Jabbour D., Luo H., Baker S.E., Pisabarro A.G.,
RA Walton J.D., Blanchette R.A., Henrissat B., Martin F., Cullen D.,
RA Hibbett D.S., Grigoriev I.V.;
RT "Extensive sampling of basidiomycete genomes demonstrates inadequacy of the
RT white-rot/brown-rot paradigm for wood decay fungi.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:9923-9928(2014).
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; KL197756; KDQ50759.1; -; Genomic_DNA.
DR STRING; 933084.A0A067P7J3; -.
DR HOGENOM; CLU_001266_1_0_1; -.
DR InParanoid; A0A067P7J3; -.
DR OrthoDB; 1342875at2759; -.
DR Proteomes; UP000027265; 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:UP000027265};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 86..110
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 180..200
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 748..767
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 937..963
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 984..1011
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1031..1051
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1089..1114
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1134..1150
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1281..1302
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1322..1342
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1375..1394
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1467..1489
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1501..1520
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..62
FT /note="RING-CH-type"
FT /evidence="ECO:0000259|PROSITE:PS51292"
FT REGION 217..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 278..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 463..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 679..722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..245
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..313
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..361
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..379
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..510
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..583
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 608..625
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..640
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..695
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1566 AA; 175697 MW; 8A6C441AFA8A83DD CRC64;
MQQEEQDTCR ICSAPAEPDQ PLFHPCKCSG TIRYIHQDCL TTWLAHSKKK TCDVCKHPYS
FTKVYAQDMP ARLPPVLLIR RLAQQLFFAL LFCVRAVVVG TIWLALLPYV TLWTWRMYFA
MGDSTAWWIS DRPRPPSSYP RPMFHHLKAP LRANTSMNTN GSYVNQLLDH PTWRALSSDI
FAGQIIACLI VLAFVAMFLL REWILQNAGP EMLEVRGEEV RGQEAEPQPA PPQDPAPPVL
VPLPDVEPDP EQAAAVEEVG DDAGFAHESL DDSHLWVDSE SEVEPHEHEE DSSDRERRGK
GKRVDYGEPS AKRKRQSRRP HFRNQDSLIG PSITFSDREE GRRPVGRFRH PNPDRFLLKR
PEGEGTSSAS SSTSSLAVPE KAEFTFRSPL QMPTSTSLVQ RRSFSEPRMV IQPPTPGSSD
ALPGVRGYAV GRDGRLDLRM AFMDQPKYRD ILPSIDAEEV RKRQREWSER QQDALVAGSS
TERPSTGTQT SPSLFSFAPS DPSVHERTFS SKPPTPLPFP LSPSLPDNIA SAGPSTPRRP
PLPSVTLPAT SAGSSPLALH LSPSGSVAPS SSKAVSPLAS PNLATYQAPE ELEAGPSNLN
SVDYFGEDIR QPDMEEEHRH YFRDPEEEEE EEEDAEDDGN VLGEYPYPTS PASGLESDDE
DELDVEAMRM EMMEVEILEN DDDHEGREID GNRLAPIRDE VAPVVPPQDQ PGGPEANEEA
DADVQDDMDG AMEAIGMRGP IYGIIQNAAL MIFILDTTIG LGVWLPFTIG KSTALLSLDP
PRFLQLLHMP IRAMRILTDP VVDLTMYLLD RFLFSPVLFA TRMVGSRLME PILLLVRAAF
GHQLTDRLLE GLTRFTTPSE VHQAVDSNSF SLVPSDGLSI NTTLTSLLHR VLDSDSKYIR
LAEPHFAALG RWVRFSSSRF SSTWTRLALG SDIPDRVFAI GLGYVVVGFG LAVYLNVLTV
GSVQNAGRAV RNVVREQLLV AKMAAFITIE LVIFPLGCGI ILDLYTIWLF PDTTLDTRIA
FFRYAPLTAT FYHWVAGTMF MYQFAVFLTG CRGIMRPGAM WFIKDPQDHN YHPIRDILER
PSFSQLRKLV VSATVYAMVI ACGVATVSAT MRLISGTIFP LRWKLRQPLS EVPIDLLFLH
LVLPYTLHYF RPSKTIRKVT VHVWKVVAAE LRLTSCMFGG RYLAEEATPT HWRVPFFTSR
GDLLETDVTK DGSFKRVPAD DNVALTREMQ ATADVDEHGE PLNEVAARMI AAQNAETERA
KRNVKEDFTV VYMPPKFSYR VATFILVIWL AVCTVLASLV TFPIEFGRLF FKLFTSKEVH
DGYSFLAGFY LLWACYLVGY ATDRLDKRRQ RRGVRPRAEW PVYLVKRTLL WTAKISYMVT
FLGLVIPVLI SLLVETYLIL PFRYTVNPSL VPRIRIVDMW ALGLVYAKIA LRAQRGPAHN
NTVFRGLNNI TRNGWTHPDP VKATREVIIP VVCALLAALL LPAGSVWLVR NTLNLPLDDK
VLFLHVYPGI FALVGIFRLL KSSFGMLSIW SQSVRDTEFL VEMRLQNLES RKREDGDSGT
PVEVVV
//
