ID A0A1E1L900_9HELO Unreviewed; 1819 AA.
AC A0A1E1L900;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=RCO7_07199 {ECO:0000313|EMBL:CZT06844.1};
OS Rhynchosporium commune.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Ploettnerulaceae; Rhynchosporium.
OX NCBI_TaxID=914237 {ECO:0000313|EMBL:CZT06844.1, ECO:0000313|Proteomes:UP000178129};
RN [1] {ECO:0000313|EMBL:CZT06844.1, ECO:0000313|Proteomes:UP000178129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UK7 {ECO:0000313|EMBL:CZT06844.1,
RC ECO:0000313|Proteomes:UP000178129};
RA Ploux O.;
RL Submitted (MAR-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}.
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DR EMBL; FJUW01000040; CZT06844.1; -; Genomic_DNA.
DR STRING; 914237.A0A1E1L900; -.
DR InParanoid; A0A1E1L900; -.
DR OrthoDB; 1342875at2759; -.
DR Proteomes; UP000178129; 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; IPR001841; Znf_RING.
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; PS50089; ZF_RING_2; 1.
DR PROSITE; PS51292; ZF_RING_CH; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Reference proteome {ECO:0000313|Proteomes:UP000178129};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT TRANSMEM 121..139
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 294..318
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 946..967
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 988..1015
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1083..1104
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1116..1137
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1169..1187
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1219..1246
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1266..1284
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1325..1348
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1368..1386
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1527..1550
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1570..1588
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1629..1650
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1716..1735
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1756..1778
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 29..90
FT /note="RING-CH-type"
FT /evidence="ECO:0000259|PROSITE:PS51292"
FT DOMAIN 37..84
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 489..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 522..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 685..773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 798..819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..544
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..594
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 712..729
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 730..753
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1819 AA; 203840 MW; D3AC422B4FE9698C CRC64;
MADTQDGQVV FPDLMNDPQY TTNFDEENDG SADADTCRIC RAEGTDTEAL FHPCKCSGSI
KFVHQDCLME WLSHSQKKHC ELCKTPFRFT KLYSPNMPKS LPLPVLLRHV VVHSIKNVAT
WLRFCVVAVV WLGCLPFVIR QVWRLLFWFS DGGWPQDSIP TVSSNRTSSE QDLKMALEIQ
KLAKIVANGT SPVTPLQDSQ TTSAHVGSLV EKLMEFLAPV ARGKNISDSD PLIAGLLNTV
YYALGFQNAA DETNMTASLP QNIMGSTVGP HHSTLLGDVR FLRNLTRNSH INQLVITIAE
GYVITLLVVV CFILVFLIRE WVVQQQPGIN VGAGFNAEFA PPERARDLAN RDPAQEGRLR
VHDDNLIENG HGLGDIERRP IVQPRRRNNE IDEVVQLAQQ TDELLEDLRQ TGGDSAPIHR
PAPIRDALTP AAEIQRAITE QPRMTEEFLA IWRRADNDPL EVLRIIERED KSEQMRYWVN
AMKLLTKQDL QGSGPRNPSR SPNLASRSSA RGEVVLSLLE PDRLSDNVTN PATVSASGNR
SRASSESWED VESLHCQYQR RAPDDSVNDA DIEDQASDKG KGKAVQEPVE EDTLITSLQE
RVEKGTSPRL KGRGLPTQIF EQNIGSTEFS SLPWMHSGIN GASLSASRPR AISDGPQPRD
TISPLANNSW SFSNLDAQVT QIDDNVPASS WSKENRKPVA ERDLQTGPGT QIAEPREGQS
SSFDQANQGW KDAQDRRVQR AFEKAREARG IKEEPQVQSQ VQEPIEEHSS SEEPLHIVGQ
DGLTRGARNW DEVFDANPVE SSTNSEAGLD ANPNNLPEDA PLPAELAPVL ARPLAPQGFM
GRVADFLWGG VNDDRREEDL GGNDEHIVQD MAAEAPFVPV AHHDHFDDHT DDDDDFALPD
PDAVEAAIAA GLDPNDPDAM DEVEDFEGIM ELVGMRGPIF SLVQNALFSA FLLALTVAIG
VWIPYNIGRV SLLLTANPGP AFKLPLRFTF GIAAFLQDVC LSILGLLSYA TLWLLSTPLE
LLSSYSPIRS TSIASRRFAL GSTAIGLSHD AVDRILNGTQ SSLTNMFESE MFAFSAASHE
SLILMRSFIL NVLASIGHAI TYIFTGDYHV SVGAILQLIA GVAQHCWGLL AALPALLAKP
DSWVISLEVS KRAAPLNPEL SVWDGTDRFW AVFAGYTALF LLGALYVKKG SPFSTGQAGR
EWEATVIDLL NQAGGVIKVI LIISIEMLVF PLYCGLLLDG ALLPLFEQTT IMSRIHFTIK
SPLTSIFVHW FVGTCYMFHF ALFVSMCRKI MRKGVLYFIR DPDDPTFHPV RDVLERNVAT
QLRKILFSAL VYGGLVVICL GGVVWGLAYA FKDVLPIHWS SNEPVLEFPI DLLFYNFLMP
LAVKFFKPSD GLHAMYSWWF RRCARMLRLT WFMFDERKQD EEGYNVRRTW KDIFKGTTTD
SLKKIKTDDI EKPFVEDPEL VVYFRMDGHY VRAPASDQVR IPKNMSTFLE VNEANEPLGS
KGEDDDMFHS KKKFKQVYLP PRFRTRIFLF ILSIWLFAAL TGVSITILPL VLGRYIFAKM
IPTHVRKNDV YAFSIGIYIL GSLLYAALHV RQFVLYIPGA INVDADTPQN VRRRVTTIAS
RVGRITWTYT AFLFILPTLF SFLVEFYLIV PLHTYFAIDE RHVMHFVQSW TLGLLYVKLT
TRITLWYEDS RPAQSLRAII RNGYLDPDAR LATRSFILPV GLALCLALFT PWCFAKMMIL
TILKDRPEKH TVAYRYAYPM CLSLCFIFYA AYVLLGLLKD WRMTIRDEVY LIGERLHNFG
DRKAVSSAVG VPNVRRIDT
//