ID A0A2T4BAA5_9HYPO Unreviewed; 1668 AA.
AC A0A2T4BAA5;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-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=BBK36DRAFT_1119504 {ECO:0000313|EMBL:PTB66139.1};
OS Trichoderma citrinoviride.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=58853 {ECO:0000313|EMBL:PTB66139.1, ECO:0000313|Proteomes:UP000241546};
RN [1] {ECO:0000313|Proteomes:UP000241546}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TUCIM 6016 {ECO:0000313|Proteomes:UP000241546};
RG DOE Joint Genome Institute;
RA Atanasova L., Chenthamara K., Zhang J., Grujic M., Henrissat B., Kuo A.,
RA Aerts A., Salamov A., Lipzen A., Labutti K., Barry K., Miao Y.,
RA Rahimi M.J., 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; KZ680213; PTB66139.1; -; Genomic_DNA.
DR OrthoDB; 1342875at2759; -.
DR Proteomes; UP000241546; 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:UP000241546};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 115..136
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 281..300
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 765..788
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 974..992
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1024..1051
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1071..1089
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1130..1153
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1173..1191
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1358..1382
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1402..1424
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1460..1483
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1515..1534
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1555..1576
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 26..87
FT /note="RING-CH-type"
FT /evidence="ECO:0000259|PROSITE:PS51292"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 370..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 472..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 564..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..336
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..502
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..646
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1668 AA; 185970 MW; 7C0941CCEF3B744F CRC64;
MEAAPDAGPA AQHRDSTRHD DGLGAANEPG ISICRICRGE GSQAEPLFYP CKCSGSIKYV
HQDCLMEWLS HSQKKYCELC KTPFRFTKLY SPDMPQSLPV HIFVQHMAKY LLRNLLVWLR
AAVAISVWAF WLPYFMRAFW SFMFRISDEG LATGSIMSRI SEANNTLSTI PSSILAIGTC
PASPLLNATT TSVAEVEAVV GHLQGKDVSD YLVRFFLGSF TSPLLASDGD PEQVANASAV
SSYASQSTIT STLLGNVAFI GNLTRSANLN RAIVSVLEGQ VITVLVIISF ILIILVRDYV
VQQQPEINMR AAFAAPENEF PLPPPPPPPD AAQPQPLPPN LDAAGSDDET LEENELVDEQ
AWRAIPTVMV GPEDSLTPGS SNQSMLDQDH EHDPFPTSST TSMQNDQLNS HAQEGADDGE
VAEERATVED YLRIYRRANG DFSEILRIIE EEGLQEKLKY WVEVTRRSTM DSAERAAADE
ATSEPAADGE SHHEHDADSD HETLQSPANG KGKEPAWSPT PADAFVSGSS SADHYDDAFA
AVGSRPRSMS DGFQEHQSVN PLANNSWSFD FLPPDAQHES QGSLDQEQPE HDLTYEEGSN
QPEDHDDDHD EDSHLNRENY RRLPERDTYR RFPEPQRLPE PEAFPRHPPD FDVYHRHPAA
DAELDGRPPH IDDAAEEAAI NDHDAPAAGL INRVADFMWG NLNEQDDAAV DDGWVDVPDE
ANGEDVDGIA ADGNAAAFDA EAIDDLEDFE GVMELIGMRG PIAGLFQNAI FCAIIVAVTI
FACIFLPYNI GRVSVWLLAS PTRVVRMLFE FSKLLQDVTF LVGGLSSWCG LNVVDMFVSV
IGGSAKAHVV SARKISWALW TGAGSRLSRS LFLEFFPMTT MEIHNFSAVS HEALNTVKGN
ILSVFSNIGD SFTAARAMGF ANIVYTTFTA LNEMVRKCAL LATKPNLWVI DLSMPEKWPA
ADPQLTHWSS LDRFWAILAG YATVFLIGAL YLKKGSPFSR SATIHAWEAG VIDFLQQASG
IIKVILIISI EMLVFPLYCG LLLDVALLPL FEDATLTSRI MFTCKYPLTS VFVHWFVGTG
YMFHFALFVS MCRKIMRPGV LYFIRDPDDP EFHPVRDVLE RNLTTQLRKI LFSAFVYGAL
VIVCLGGVVW GLSFAMPGVL PIHYSSNEPV LEFPIDLLFY NFLMPLVVKF FRPSDALHTM
YTWWFRKCAR GLRLTYFLFG ERKIDEEGTL RLRPGAEDTR LLKSSYLLEL GEGDVVVPKT
WRDTFEGGHL KPNTVMNSEQ RRELRRRKAR LVESQQLIKD GQFVRAPASD RIKIPKGQRV
FLTVSERNHR RDGRQDDDVY STNQYLMVYV PPYFRARVLL FIFFIWLFAS VTGVGFTIIP
LILGRRIFKL LIPSYVRTND IYAFSIGVYL LGSAAYFAFH YPMIKKTVRR WVRQARRDVA
DGRAWRRGTA MGVRVAKISY AYFILVIVFP LLTSTLMELY VTIPLHTYMY PPKAISTALE
GEAVERHTVR VIQSWVLGLL YLKLGSQMIT SLFPDSRAAR AVRSIMRRGW MRPDVRLLTR
AFVIPGLLAF CVAVFGPPMV AGFVIRHGGL AGGSPADDAA EAVRMAVIYR QSYPVAAFAA
MLAKHAIGLV KVTNRWAAGV RDEAYLIGER LHNFGSRASG TKRVRAQG
//
