ID A0A1B6QD96_SORBI Unreviewed; 877 AA.
AC A0A1B6QD96;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN ORFNames=SORBI_3002G245000 {ECO:0000313|EMBL:KXG35895.1};
OS Sorghum bicolor (Sorghum) (Sorghum vulgare).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum.
OX NCBI_TaxID=4558 {ECO:0000313|EMBL:KXG35895.1, ECO:0000313|Proteomes:UP000000768};
RN [1] {ECO:0000313|EMBL:KXG35895.1, ECO:0000313|Proteomes:UP000000768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX PubMed=19189423; DOI=10.1038/nature07723;
RA Paterson A.H., Bowers J.E., Bruggmann R., Dubchak I., Grimwood J.,
RA Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A., Schmutz J.,
RA Spannagl M., Tang H., Wang X., Wicker T., Bharti A.K., Chapman J.,
RA Feltus F.A., Gowik U., Grigoriev I.V., Lyons E., Maher C.A., Martis M.,
RA Narechania A., Otillar R.P., Penning B.W., Salamov A.A., Wang Y., Zhang L.,
RA Carpita N.C., Freeling M., Gingle A.R., Hash C.T., Keller B., Klein P.,
RA Kresovich S., McCann M.C., Ming R., Peterson D.G., Mehboob-ur-Rahman,
RA Ware D., Westhoff P., Mayer K.F., Messing J., Rokhsar D.S.;
RT "The Sorghum bicolor genome and the diversification of grasses.";
RL Nature 457:551-556(2009).
RN [2] {ECO:0000313|Proteomes:UP000000768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX PubMed=29161754; DOI=10.1111/tpj.13781;
RA McCormick R.F., Truong S.K., Sreedasyam A., Jenkins J., Shu S., Sims D.,
RA Kennedy M., Amirebrahimi M., Weers B.D., McKinley B., Mattison A.,
RA Morishige D.T., Grimwood J., Schmutz J., Mullet J.E.;
RT "The Sorghum bicolor reference genome: improved assembly, gene annotations,
RT a transcriptome atlas, and signatures of genome organization.";
RL Plant J. 93:338-354(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};
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DR EMBL; CM000761; KXG35895.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B6QD96; -.
DR STRING; 4558.A0A1B6QD96; -.
DR EnsemblPlants; KXG35895; KXG35895; SORBI_3002G245000.
DR Gramene; KXG35895; KXG35895; SORBI_3002G245000.
DR eggNOG; KOG0940; Eukaryota.
DR InParanoid; A0A1B6QD96; -.
DR OMA; CAHRANM; -.
DR OrthoDB; 5480520at2759; -.
DR Proteomes; UP000000768; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR CDD; cd00078; HECTc; 1.
DR CDD; cd17039; Ubl_ubiquitin_like; 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 InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR11254:SF424; E3 UBIQUITIN-PROTEIN LIGASE UPL5; 1.
DR PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR Pfam; PF00632; HECT; 1.
DR SMART; SM00119; HECTc; 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000000768};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 77..150
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT DOMAIN 539..877
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 843
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 877 AA; 98088 MW; F575C0F9DC1A79EE CRC64;
MSAALACLRR TSKRRRDAPD HALPPSSKQP LMAHAGAGAD AAESSSSASA SASGGDGASA
AAAAASASSP PASPRELHFF VRATDSRTIA MHAAWDDTVG AVLDHLGACG YGRDLRLVYA
GRQLAPEATL AELCLLPDST LHLLARLRST QHPHAWQLAS HIASTAAAAE SEPSRIPAAA
FSLDELVKEF ILRAHRANLG LSRHDRASTG EDRAPADHAA EYLDIFLQAG AALALVRLYL
SKSPFRSYAE TAIKCFVATD PSSLPMDVLV VTAPVLLEFC RLLSLAAGKK ELLYRSCRRT
LASVLSTRPR LPPSMNSPTR LIEQVLPFAR ETVDLVLDGL ASMPMIIPPS DLDEFSNFLK
VMCQQARHWI SGEGPMPSNL YSRESEHGDT WIWRFHNMSM DMLKRLDECL KTLEMDLSLS
SESTGVMDSQ TTWAARSHIL VILTELDFIS AIYEDVGHNL QLVLLAHRAP LNALVRCSKR
NERLHWLVKH KNLLCFEARR NLVFMMLPEG KDDFGELHEM LIDRSHLLDE SFNYIAQAKQ
TELRGGLFME FKNEEATGPG VLREWFCLVC QALFSPKQVL FSPCPEDKRR FYLNETSAVD
PLHLKYFTFA GRIIGLALMH KVQVGVVLDR TLFLHLAGRS ITLEDISVAD PVKYASCKKI
LEMDAAEIDS LYLTFSRGAH ELGTEKVIDL FPGGQDISVN IRNRELYINL LIKNIFVDSI
SSQLTHFTEG FADILVNPKR REEFFECLDL EDLDRLLGGN NNAINLQDWK SHTQYNGYKE
KDRQITLFWK AVERMSLERQ RQLLFFWTSV KYLPSDGFCG LSSKLYIYKT SDSPDRLPSS
QTCFYRLCLP PYTSLKMMEN QLQKITQEHV SCSFGTW
//
