ID A0A2V1CQ46_9HELO Unreviewed; 1854 AA.
AC A0A2V1CQ46;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN ORFNames=DL98DRAFT_509944 {ECO:0000313|EMBL:PVH87748.1};
OS Cadophora sp. DSE1049.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Helotiales incertae sedis; Cadophora.
OX NCBI_TaxID=1485229 {ECO:0000313|EMBL:PVH87748.1, ECO:0000313|Proteomes:UP000244409};
RN [1] {ECO:0000313|EMBL:PVH87748.1, ECO:0000313|Proteomes:UP000244409}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSE1049 {ECO:0000313|EMBL:PVH87748.1,
RC ECO:0000313|Proteomes:UP000244409};
RX PubMed=29679020; DOI=10.1038/s41598-018-24686-4;
RA Knapp D.G., Nemeth J.B., Barry K., Hainaut M., Henrissat B., Johnson J.,
RA Kuo A., Lim J.H.P., Lipzen A., Nolan M., Ohm R.A., Tamas L.,
RA Grigoriev I.V., Spatafora J.W., Nagy L.G., Kovacs G.M.;
RT "Comparative genomics provides insights into the lifestyle and reveals
RT functional heterogeneity of dark septate endophytic fungi.";
RL Sci. Rep. 8:6321-6321(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; KZ804112; PVH87748.1; -; Genomic_DNA.
DR STRING; 1485229.A0A2V1CQ46; -.
DR Proteomes; UP000244409; Unassembled WGS sequence.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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 Ligase {ECO:0000313|EMBL:PVH87748.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000244409};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 1499..1854
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 1..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 726..801
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1061..1130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1185..1215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..179
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 735..750
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 751..775
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 776..794
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1069..1107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1201..1215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1821
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1854 AA; 201502 MW; B8A8EBA70ECCA397 CRC64;
MPPNSRITRA AARQATSSSE SPAASVGASS AASSSRQPPP PPSTRKRKAP ARETSPAPEA
EPAKPSSARR TKRQKVVDTD TAPPAPPAPQ AVAPSRRKKG KTPAVMSSPG DSAGPSNDPP
AAATTSSKRK SARNKKGGQA DTTVTPSGRR SKKTTSSAKD GDNTLDNSVD EKVPPPGEDD
ASDDNEDEEM ARHYEGRDDD DDDDDPFGGF GGPGGPPHGL SSTLRALSGM MSGVSTRLRD
ILNNLKQKDD PSLQLIALQD LSEILLVSTE DNLSGHFSPD AFVKELVVLM QPSDFGEENP
EMMLLACRCL ANLMEALPAS TANVVYGGAV PVLCAKLLEI HFIDLAEQAL STLEKISVEY
PASIVREGGL TACLTYLDFF ATSTQRTAVT TAANCCRNIP EDSFPVIKDV MPILLNVLSS
NDQKVVEQGS LCVSRVVESF RYHPSKLEEL VSSDLLKAIL RLLLPGTTNL IGPNIHTQFL
RVLAFTAKAS ARLSAELFKM NVVETLYQIL TGVSPPDATE DAASKLDSVV VMQALIHRPR
EQVIETLNVI CELLPGLPRE IEVSPEDLLD ADAASAAATT SSSGSRKKSS NEKRIELLEG
CKNEVKRFAI IIFPTLTDAF SSTVNLSVRQ KVLTAQIKML SNLDKEILME ALRSVPYASF
LAAILSQQDH PSLVNYALQA AELLLARLDD IYRYQFYREG VIAEIAKLAT ATESAKAISE
DTPVIEVAEP IEANGTRKVS EKPSRSAPGD DDDSSDEDND DENENDEDNE NDDIQDDISP
SPSSRGSTMS LDGPQHRLPT DAGGMQQLIV QRAKKFLDVH ENEKNSKSMK KKATKILTSL
QGLASDIEAH YLQGKPGEGM KLFSTLASYF DGDVLESVTS AELLNSEVVR VLLEVFSNPD
ENLSNDARSA FLEVFMGRTV TKKPKTTSAD SPATPFSILI HKLQDLLSRS EHFEVVTVHQ
NTFDGNRSSA ASMLAKQIRL KLVADDDSEI PRPYRNIMVS IHAIATFKAL DDYLRPRISL
SERPRGSRRE GLSSALAALA AAGMPNPYAQ TGQSRLVERG LASATAATPT APPPATARSS
RKPKSKTSST GAAAPGGPST VATPQDKTAR RSSRRQAQAE TPVPPLMQEE DSLAGALECA
DERQLTDDEE MEDSAALDAI VGDLEDDMEE GSPADPTAVN LEVAAGGKVT ARKEDGTRVA
TPSQMPGSNP RTASALQAAA AHAALTTPSA SSRPMSYAAA IQAIPQDWHI EFSLDDKVIA
NETTIYRAVH STSTTIDDQN SRSVWSAIHP IKFKRVPGPP PPEPSSLTQA PEVVTETTAS
GIPASLDKHP ATSSILRLLN ILHALNANLD DVLAENKDTL KLNAEPLSQF VNTKLTAKLN
RQLEEPLIVA SNCLPSWSED LARLYPFLFP FETRHLFLQS TSFGYARSMT RWQNAQSADE
SRRDRHRDER PFLGRLQRQK VRISRSKILE SALKVMELYG ASQSILEVEY FEEVGTGLGP
TLEFYSTVSK EFSKKKLKLW RETEANDTDE YAFGVRGLFP APMSEEQASN ENGKRILHLF
KMLGKFVARS MIDSRIIDVS FNPTFFRIGD ESTTVSPSLG AVKTVDPQLA KSLKLIKKYA
VAKKAIDENP NLTPAQKVAN AQALEIDGMK IDDLGLDFTL PGYPVELIPN GGRTTVDIDN
VQLYLDKVID FTLGTGVQRQ VDAFRAGFTQ VFPYSALSAF TPDELVMLFG RIEEDWTLET
LMDSIKADHG FNMDSKSVKN LLQTMSELTL PERRDFLQFT TGSPKLPIGG FKSLTPMFTV
VCKPSEPPYS SDDYLPSVMT CVNYLKLPDY TDLDVMRRRM GTAIKEGQGA FHLS
//
