ID A0A3N2PPY7_9PEZI Unreviewed; 1942 AA.
AC A0A3N2PPY7;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN ORFNames=SODALDRAFT_325839 {ECO:0000313|EMBL:ROT36514.1};
OS Sodiomyces alkalinus F11.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Sodiomyces.
OX NCBI_TaxID=1314773 {ECO:0000313|EMBL:ROT36514.1, ECO:0000313|Proteomes:UP000272025};
RN [1] {ECO:0000313|EMBL:ROT36514.1, ECO:0000313|Proteomes:UP000272025}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F11 {ECO:0000313|EMBL:ROT36514.1,
RC ECO:0000313|Proteomes:UP000272025};
RX PubMed=30368956; DOI=10.1111/mec.14912;
RA Grum-Grzhimaylo A.A., Falkoski D.L., van den Heuvel J.,
RA Valero-Jimenez C.A., Min B., Choi I.G., Lipzen A., Daum C.G., Aanen D.K.,
RA Tsang A., Henrissat B., Bilanenko E.N., de Vries R.P., van Kan J.A.L.,
RA Grigoriev I.V., Debets A.J.M.;
RT "The obligate alkalophilic soda-lake fungus Sodiomyces alkalinus has
RT shifted to a protein diet.";
RL Mol. Ecol. 27:4808-4819(2018).
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=2.3.2.26; Evidence={ECO:0000256|ARBA:ARBA00000885};
CC -!- SIMILARITY: Belongs to the UPL family. K-HECT subfamily.
CC {ECO:0000256|ARBA:ARBA00006331}.
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DR EMBL; ML119059; ROT36514.1; -; Genomic_DNA.
DR STRING; 1314773.A0A3N2PPY7; -.
DR OrthoDB; 1093891at2759; -.
DR Proteomes; UP000272025; Unassembled WGS sequence.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd00078; HECTc; 1.
DR Gene3D; 3.30.2160.10; Hect, E3 ligase catalytic domain; 1.
DR Gene3D; 3.30.2410.10; Hect, E3 ligase catalytic domain; 1.
DR Gene3D; 3.90.1750.10; Hect, E3 ligase catalytic domains; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR045322; HECTD1/TRIP12-like.
DR PANTHER; PTHR45670; E3 UBIQUITIN-PROTEIN LIGASE TRIP12; 1.
DR PANTHER; PTHR45670:SF1; E3 UBIQUITIN-PROTEIN LIGASE TRIP12; 1.
DR Pfam; PF00632; HECT; 1.
DR SMART; SM00119; HECTc; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR PROSITE; PS50237; HECT; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000272025};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 1584..1942
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 1..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 749..858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1118..1293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1378..1410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..244
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 763..790
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 791..824
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1133..1147
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1167..1182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1203..1250
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1275..1293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1909
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1942 AA; 211746 MW; 286950E87360079E CRC64;
MASSRNTKIT DSLLMPTRVT RSSARQAASR TASSTTSALG ADPPPTASSA LDNHPPAENQ
QTPSSRKRKA APQGPSPNQA ALPTAPSSAR RSKRQKTTDT AAPPPSQPAD QASTVAKNRR
KGKAPANMSS PGNSGAVGAS ENVPSSGSSS RRSSRGKRSG QRDSQESLPS SSTLYRQRKR
TARTNNPAEQ DTTMTGTDDA AEKEAVPPPP PPPPGHRSDH DDSDEHDEDE SGRYDEDEDD
DDPFGGFGGA GGPGSGLSST LRALTGMMSS GISSRLRGLL SNLRQKDDPT MQLVALQELS
EILLVSNEDN LSGHFSPDSF VKELVTLMQP NELTGEENPE IMLLACRCLA NLMEALPASV
ANVVYGGAVP VLCQKLLEIS FIDLAEQALS TLEKISAEYP STIVREGGLT ACLSYLDFFA
TSTQRTAVTT AANCCRNIPE DSFPVIKDVM PTLLNVLGSN DQRVVEQASI CVSGIVESFK
YQPSKLEELV SVDLLKAVLR LLVPGTTNLI GPNIHTQFLR VLAFTARSSP RLSAELFKLN
IVETLYQILT GVSPPSGTDD LASRLDSVVI MQALIHRPRD QVIETLNVIC ELLPNLPHDA
DPACGDFIAL GAGEPITPTS TTPGRARKSP NDKRIELLAE CQDEVRRFAL ILFPTLTDAF
SSTVNLNVRQ KVLTAQLKML SNLDAEILGE ALRTVPYASF LASILSQQDH PSLVMLALQA
TELLLSRLDD VYQYQFYREG VIAQITKLAS QEFPQPPPEK VKTSSDETPE ASDQRELEGS
DSRHDGEKEH SDDGEDEEER DESERDEDEE DDADRDDEED EDDHQQHDQE RAGSPHSSGG
STVSVDEPVP RHLSNDQSMR IRIRDVAKRF LETHDVEKHD KTMKKKATDF LTDLTNLADQ
IGDFYLNPTD AKAKVDPEQG AELFQKLVTY FDAEVLESVT SAELLASRLV YVLLNIFSNP
DEELAHAAQA TFLKIFMGHT VKAKPKTATA DSPATPFSVL IHKLQDLLSR SEHFEVVTVH
HNSLDHRSSA ASMLAKQIRL RLVADDDSEI PRPYRNIMVS IHAIATFKSL DDYLRPRISL
SERTRGSRRA DGLSRALAAM ASHGGLPPLS QAAAARLAER AGLADATSPA SGSSSAPPPP
PPGDSSSAPA SRPSSRKTKS KSTPRDGDPS TPDASSSSRN KAVLRRSARR QAATSTDTPA
SAGPPDEDDD LQDALECADE RQLTDDDDIG DDDDLDAIVG DLDEDMDESP GPDPGAVNLE
VAAGGKVTAR AEDGTRVPTP SQGSSNQGQG LGLPSRTSAL LAAAVSQRTP SPATSSRPMS
YAAAIQSVPQ DWHIEFTLDG KAIPSETTIY RAVHMSASNS DEHVSRSIWS AVHPIRFRRA
PGPPPPSPEG GSSFGTVADT SADNADGIPP SLDKHRITAS ILRLLNILHD LNANVDDVFM
ENKDTARLNV EPLAQFVNTK LTAKLNRQLE EPLVVASNCL PSWSEDLARL YPFLFPFETR
HLFLQSTSFG YARSMTRWQN AQSNDDSRRN HYNDRPFLGR LQRQKVRISR SKILESALKV
MELYGASQSI LEVEYFEEVG TGLGPTLEFY STVSKEFSKK KLKLWREVDS NESDEYISGA
TGLFPRPMSD EEAAGPNWER YLTLFKMLGK FVARSMIDSR IIDLNFNPIF FRIGDASSKS
GVKPSLGAVK VVDPGLAQSL KTIKKFSLAK KKIDEDPSRT PAQKVADTEA VVVDDVRIED
LCLDFTVPGY PEIELVPNGS RVKLTMDNVD LYLDRVIDMT LGSGVRRQVD AFRSGFSQVF
PYSALSAFTP DELVSLFGRV EEDWSLETLM DSIKADHGFN MDSKSVRNLL QIMSEMTPRE
RRDFLQFTTG SPKLPIGGFK SLTPMFTVVC KPSEAPYTSD DYLPSVMTCV NYLKLPDYSS
IETMRKQLAT AIKEGQGAFH LS
//
