ID A0A2T3ZMG3_9HYPO Unreviewed; 1703 AA.
AC A0A2T3ZMG3;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=M441DRAFT_127875 {ECO:0000313|EMBL:PTB45999.1};
OS Trichoderma asperellum CBS 433.97.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=1042311 {ECO:0000313|EMBL:PTB45999.1, ECO:0000313|Proteomes:UP000240493};
RN [1] {ECO:0000313|EMBL:PTB45999.1, ECO:0000313|Proteomes:UP000240493}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 433.97 {ECO:0000313|EMBL:PTB45999.1,
RC ECO:0000313|Proteomes:UP000240493};
RG DOE Joint Genome Institute;
RA Aerts A., Atanasova L., Chenthamara K., Zhang J., Grujic M., Henrissat B.,
RA Kuo A., Salamov A., Lipzen A., Labutti K., Barry K., Miao Y., Rahimi M.J.,
RA Shen Q., Grigoriev I.V., Kubicek C.P., Druzhinina I.S.;
RT "Multiple horizontal gene transfer events from other fungi enriched the
RT ability of initially mycotrophic Trichoderma (Ascomycota) to feed on dead
RT plant biomass.";
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}.
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DR EMBL; KZ679256; PTB45999.1; -; Genomic_DNA.
DR STRING; 1042311.A0A2T3ZMG3; -.
DR OrthoDB; 1342875at2759; -.
DR Proteomes; UP000240493; 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:UP000240493};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 114..135
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 279..298
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 791..814
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 844..869
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1003..1021
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1053..1080
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1100..1118
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1159..1182
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1202..1220
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1388..1411
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1431..1449
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1489..1513
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1587..1606
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 25..86
FT /note="RING-CH-type"
FT /evidence="ECO:0000259|PROSITE:PS51292"
FT REGION 318..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 370..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..400
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 480..498
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..560
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..594
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 597..631
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1703 AA; 189226 MW; 41A26C23BAC2D02A CRC64;
MEDAASDTGP AAQQHRYDDR LNTAAIDTAP AICRICRGEG TPVEPLFYPC KCSGSIKYVH
QDCLMEWLSH SQKKYCELCK TPFRFTKLYA PDMPQSLPIH IFVEHMAKYM FRNLLVWLRA
AVAISVWVFW LPYFMRAVWS FMFWISDEGL GGSIISRINE TNSTMSAIPS SILAIGTCPA
SPLLAATTTS AAEVEAVVGQ LEGKDVSDYF VRFLLNSFTS PLLASDGELG YAANSSAALN
NASQFAAATT LLSNVGVLGN LTRNASLNRA IVSVLEGQII TVLVIISFIL IILVRDYVVQ
QQPEINMRAA FAAPENDIQD VPEPGEIIQQ DNLPPANLHP TDSDDETLED SDQVGDQDWQ
RMPAGRLAPA GEQALTPDSS NHSMPDHDSF PTSSTNTSLQ NDQLNSHARE GADEGDAAEE
PTTLDEYLRI YRRANGDLQD TLRIIEEEGL QEKLKYWVEF TRRSTSTIEN TSRIVTNEPA
MEEVDQEHPE HEIDSDHDTL QSPSNWKGKE PWSPTQADLD ISGPSDAPED DFFGATSRPR
SMSDGLQGQF SANPLANNSW SFDALPVDDK PDEPSQALPA IQEQFTQDLS DGEPSEEFSG
QPRDFDDEDD SHLSREAYRR LPDRDTYQRY PPREIEQPLP NLNEREQRLD AEIEAQPPHA
NGAAEEAAVN GADAPAAGFA EKIADFMWGN MDDLDPPVVP RALIVAAHRA ALDDIAAEEA
VERAAGQGAA AGNNDRDDPW VDVPAEPNGD DGEGIAADDN AAPLDPEAIE DMEDFEGVME
LIGMRGPIAG LFQNAIFCAV LVSVTIFACI FIPYNIGRVS VWLLASPMRV VRLLFELSKL
LQDATFLVGG LGSWCALNFV DIFAAVMGGS VKAHIVSARK MSWGLWTGAA SRICTFLFKD
FFPMSATEIH NFSAVSHDAL NIVKGNVVSV FSNISSSLTT ANTVGFDKVM ATTMTLLSST
SETAIRVASL LTKPSSWVID LSLAEEWPSL DPQLTYWSSL DRFWAILAGY TTMFLVGALY
LKKGSPFSRN AIVHAWETGV IESLQQASGI MKVILIISIE MLVFPLYCGL LLDAALLPLF
EDTTFTSRII FTCKYPMTSV FVHWFVGTGY MFHFALFVSM CRKIMRPGVL YFIRDPDDPE
FHPVRDVLER NLTTQLRKIL FSAFVYGALV IVCLGGIVWG LSFAMPSALP IHYSSNEPVL
EFPVDLLFYN FLMPLAVKFF KPSDALHTMY TWWFRRCARA LRLSYFLFGE RRVDEEGVLH
LPAETPAGRI PHMGYLLELA EDGNAIVPKT WRDTFEGGDL KPTTHMSSSE RKAYRHKKAR
LVESHQLVKD GKFIRAPASD RIKIPKGQQV FLTVSERNRR KDGRADDDIY SSDQYLQVYI
PPNFRTRIFT FILLIWLFAS VTGVGFTIIP LVLGRKIFKE LIPDYIRTND IYAFSIGVFL
LGSVAYAIAR QHTIRKKIGK WVREAERDML EGEIAGRIAR IAIHTAKLFY AYTVLLVVFP
LLTSALMELY VAIPLHTYMH PPTAVSTLKD EGANRHTVRV IQSWVLGLLY LKLGSRMITS
LFPDSRASAA VRNIIRRRWW LRPNVRLLTR GFVIPGLLIS CVAIYGPPTV ARFIIKHTSL
AGGSGSEDAA AAVTATVIYR QSYPIAACAA ILAKHAVGFI KVMNRWTASV RDEAYLIGER
LHNFGSRTSS TKKTKVRARR ANA
//
