ID A0A364N956_9PLEO Unreviewed; 1677 AA.
AC A0A364N956;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, 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=DDE83_002767 {ECO:0000313|EMBL:RAR13878.1};
OS Stemphylium lycopersici.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Stemphylium.
OX NCBI_TaxID=183478 {ECO:0000313|EMBL:RAR13878.1, ECO:0000313|Proteomes:UP000249619};
RN [1] {ECO:0000313|Proteomes:UP000249619}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIDEFI 213 {ECO:0000313|Proteomes:UP000249619};
RA Medina R., Franco M.E.E., Lucentini C.G., Saparrat M.C.N., Balatti P.A.;
RT "Draft genome sequence of Stemphylium lycopersici strain CIDEFI 213.";
RL Submitted (MAY-2018) 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:RAR13878.1}.
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DR EMBL; QGDH01000029; RAR13878.1; -; Genomic_DNA.
DR STRING; 183478.A0A364N956; -.
DR OrthoDB; 1342875at2759; -.
DR Proteomes; UP000249619; 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:UP000249619};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 118..143
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 304..323
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 810..832
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1041..1059
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1091..1118
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1138..1159
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1197..1220
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1240..1258
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1355..1380
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1400..1418
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1455..1478
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1490..1509
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1544..1565
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1585..1608
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 37..98
FT /note="RING-CH-type"
FT /evidence="ECO:0000259|PROSITE:PS51292"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 378..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 475..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..393
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..506
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..543
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..587
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..604
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 612..630
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..681
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1677 AA; 185086 MW; 2FD443F5066ADF08 CRC64;
MATDAAPLNA GPFDEAPAMA TPAQDDDVTD TSETRAVDKD EADTCRICRG EGTVDEPLFF
PCKCSGSIKY VHQECLMEWL SHTQKKHCEL CKTSFRFTKL YHPGMPSRIP TTVFIRRAAL
HVFNMFVTWC RGVLVGAVWL FLLPWCMRLV WRSLFWVGDG GWSRDMLMET AETPEMRTFS
TGELNMIRTA VDGAKSRNGT ADVSLPNPPI SISYNPNNNA TGESMFWTFA KRFFFGVPYP
SLQLAQIDKP SHFSISESNV TASNFTSGPL ALRSPSLLSD VPFFNWFHSQ SANRFIVDVI
EGQIITLLVV VAFILVFLIR EWVVQQQPVI NMVALGDNAA AQQAADLEQE AEVEVENIAV
DEDELDDALG ALGAEVAQEA QEAQNTNDEG PAPPNDDNVQ VNGLEASEPI IRRVRRSSSL
RRERDEVVRR LVRDGLSDDV SAIIQSEAAD ENADIFNQDN EDARNLHESL RRAMNAREEA
SEHQDDSQAS GSSYPTRTSS LPLPSGSVSD AGDFDPSWQR PEMPARDRSF IATEIRRSLE
EGKSWSFENV PQASGPVADN AEEESRSWKD NTANEQRREE PGSMLDQEQH SEHSSGSWQQ
VPDVVGDDSD QALEGENTHD KGKGKAVDNN EDASNESASS TGSAADSDNG ITVDTTIEVD
NSVSQPEHNT STQGQEQTGA GEAREHQNEP PAAANDVQPV EPQAPGNPMN RVLDWMFGDV
APATQVADEG GNDEHVVRDL ADEAPFVPFM GNDVRDHGNA PAQDAEVAAA AAQAGIDVND
QEAIEDAEDL EGILELIGMQ GPLVGLFQNA LFSAVLISAT LACAVWLPYL WGKVVILFMG
SPIALFIKLP LQVVAAITDF VVDVTLLIVA GTTYWSSYTI SGLVKFCSWG TLSQTIEGPL
RKISAPAYSL AESAMVRIGK MFIESPLSPG PDYFRLSVNA HASLRSLQNT TSFALNETSN
FANAVFEEIS ADSPPKLVLR ILTQFPSVIA NTYTVAYSQS SALLSWLWSS KSYRITLDVD
LGRNTTVAYT AMERWTAGDR LIAVLAGYGF FALAGAVYLK RGTPFSSSQQ GQKIERILSD
ILQQAGGVLK VILIISIEML AFPLYCGLLL DLAMLPLFKN ATLYTRWQFA RESPWTSGFV
HWFIGTCYMF HFALFVAMCR KIMRKGVLYF IRDPDDPTFH PVRDVLERSV TTQLRKIAFS
ALVYGALVIV CLGGVVWTLS RATSNVLPIH WTTEAPSLEF PLDLLFYNFL TPVIIKFYKP
SEGLHAMYKW CFQKCAAFLR LSNFLFGDKV PEQEGEDGRY VRAPASDQAR IPKGHPVFVE
VDRDNVRKDG QNDVGIHNSE LVSMVFIPPW FRMRIFCFVV AIWIFMGLSG VSVTILPLLF
GRYLFSLFLP PTVEMNDIHA FSLGIYTLAS IGYSVYHATK FIMTLHRPVP DAMSTLHTIA
TTTWRVGGRV LRFSYVWASL IFVIPFLFAV LLELYFLMPL HAYLGPKEPH VVHLIQDWTL
GFLYSRLAAR LVFANRNSRP ARAFAAVVRD GYLYPNAQIA TKCFLIPVLA AFSVAIAVPA
SLAWMTSRTM YYGASEATKN QVWRFSFPAV GLSLVLMWAS SAVVRLLVRW RLVVRDEVYL
IGERLHNFGE RKAPVAQVAA STLTSSSSSS SSPSSSPGLL VAGEVMGEGE AGLQAAA
//
