ID A0A066WRL4_TILAU Unreviewed; 1595 AA.
AC A0A066WRL4;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN ORFNames=K437DRAFT_219360 {ECO:0000313|EMBL:KDN53300.1};
OS Tilletiaria anomala (strain ATCC 24038 / CBS 436.72 / UBC 951).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Georgefischeriales; Tilletiariaceae; Tilletiaria.
OX NCBI_TaxID=1037660 {ECO:0000313|EMBL:KDN53300.1, ECO:0000313|Proteomes:UP000027361};
RN [1] {ECO:0000313|EMBL:KDN53300.1, ECO:0000313|Proteomes:UP000027361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UBC 951 {ECO:0000313|EMBL:KDN53300.1,
RC ECO:0000313|Proteomes:UP000027361};
RG DOE Joint Genome Institute;
RA Toome M., Kuo A., Henrissat B., Lipzen A., Tritt A., Yoshinaga Y., Zane M.,
RA Barry K., Grigoriev I.V., Spatafora J.W., Aimea M.C.;
RT "Draft genome sequence of a rare smut relative, Tilletiaria anomala UBC
RT 951.";
RL Submitted (MAY-2014) 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=2.3.2.26; Evidence={ECO:0000256|ARBA:ARBA00000885};
CC -!- SIMILARITY: Belongs to the UPL family. K-HECT subfamily.
CC {ECO:0000256|ARBA:ARBA00006331}.
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:KDN53300.1}.
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DR EMBL; JMSN01000003; KDN53300.1; -; Genomic_DNA.
DR RefSeq; XP_013246139.1; XM_013390685.1.
DR STRING; 1037660.A0A066WRL4; -.
DR GeneID; 25262234; -.
DR HOGENOM; CLU_000366_1_1_1; -.
DR InParanoid; A0A066WRL4; -.
DR OMA; AEPLSQF; -.
DR OrthoDB; 1093891at2759; -.
DR Proteomes; UP000027361; 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 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:UP000027361};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 1267..1595
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 407..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 605..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 652..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 860..920
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 964..1014
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..451
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..619
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..672
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 865..917
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 982..1014
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1562
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1595 AA; 173478 MW; 10B6DCEF386EC1DF CRC64;
MNLRAMAGFL SGLSRRFKTI LSSLRNRFDP AERLVALQEL SEVLSVSSED SLAGYFPTES
FVKELIALLG GNPSDASIES GVVAPDSDVA AALAAADAAD AGDNTEIMLL AARCLTNLME
AMPYATHSVV TNGAIPLLNS KLMFIEFIDL AEQVLQTLEK ISVDYPNAIV EEGGLMAMLQ
YIDFFNIHVQ RTAMNAVSNC CRKLNSDNFD KVKDAMSQIQ GMLASPDRRL KESAVRSVVR
IIDSYKAFPE ILETLITEDV CAATKFVLEP SAGSNGSSGA IISTSMYTDL VKALCNASKA
TPQITAHLLQ SGIGATLYCI LTGSKAADTG NLVSADPLSK PDETIGNVSI SGQSPVVKMT
LLQNLSTKPK EQIQEALTLV CELLPPLPWT DIFDQRNYSE KALKRKKHEL AKREGVAKGR
NSLEPPTANS QMESSEDTVE AAPTSQASQI KKEYRKGSKE AAAQVAHARR LEMLNEQKDR
LLKLSAMILP ALVDIHTASI TPSIRSKAMT AILKILAFAD ASQLEGLLRS VPMSTFVAGV
LSSKDSPTVI QGSLQVVELL LTKLGHIYCA LLEREGVMWE VKQLAKQPVS DTGMSNKAIG
LPADTLSTES QNTDDSPASE APKLGTVGNS GLRQVKDANV LRARMVHLVF GRHKQKTPNN
TESSTADSLE RASGLAQQIA SGSFESEGAA ASCLHSAFAL LQSNGEGLSG FEVVKSGLIN
ALLIFLNADS DASLASRRKG LLRDTMKFMP ESSRNLIQRL QESLSRLERV EMVSVAGSLD
DEHRRSPAAA LSKQIRLRLV ADDPDGIPKS CNNIIVSIHA VASFGSLHDF LRPKIALGNS
LIGPGTSRLS SVLAAFAAAA QGQESPREPT RNTNSLTSDG ASTATATESV EAHTRGVASG
QNSGSTTHPG QVTSDEQADK TLQREQGLLR GESASLADAL MQNLMHDDMD PLDEDLEELD
IIEREISPPE SGDPSARQLP GSRAEEQETN VSAPDTANTS TAEPNSQTKL ASYSEAVQKP
ATDWHLAFSV DGEDVGLPET IFSAIYRAEK RKNASFSFER TIWQNLVTVR FRKVPGTRAR
DHEEIYGIAA EKQPAVSSIF PEDSTELKIL RLLEVLYHAM SSLSRHSSQS GIRHLDTSLF
INNKLTAKLN RQLEEPLIVA STSLPDWAVG LPLEYPFLFP FETRFSFLQS TSFGYARLIA
RWQLLHRGSD NGRNEDSFGF LSRLQRQKVR ISRRRLLDSA VKIFDLYASN SSILEVEYFD
EVGTGLGPTL EFYSLVSQDF ALKENNIWLD EQTNPQSLHV SAAHGLYPIP ISSSASTTLE
GSKRLGLFRT LGTFVAKALL DSRIVQIDFS RLFISAILGR KVAYNLDTLA QVDGGLASSL
KAIQSVAPED VATLHLDFTL PGDSNYELVP GGSDKKVSGN NVNDYISAVI DAYLDSGIQP
VVESFRAGFE KVFMLSSLKP FTADELVLLF GNSQEDWSAE TLLSNIKPDH GFTPESEPYR
NLLSIMQDFT DQERRTFLQW LTGSPKLPIG GFKALHPQLT VVKRPHEAPL KPDDYLPSVM
TCVNYLKLPS YSGKEVMRQR LNTAMLEGGT AFHLS
//
