ID A0A194YN33_SORBI Unreviewed; 1832 AA.
AC A0A194YN33;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
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_3004G001500 {ECO:0000313|EMBL:KXG29245.1};
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:KXG29245.1, ECO:0000313|Proteomes:UP000000768};
RN [1] {ECO:0000313|EMBL:KXG29245.1, 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};
CC -!- SIMILARITY: Belongs to the UPL family. K-HECT subfamily.
CC {ECO:0000256|ARBA:ARBA00006331}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM000763; KXG29245.1; -; Genomic_DNA.
DR STRING; 4558.A0A194YN33; -.
DR EnsemblPlants; KXG29245; KXG29245; SORBI_3004G001500.
DR Gramene; KXG29245; KXG29245; SORBI_3004G001500.
DR eggNOG; KOG0168; Eukaryota.
DR eggNOG; KOG0170; Eukaryota.
DR InParanoid; A0A194YN33; -.
DR OMA; THFDISH; -.
DR OrthoDB; 1093891at2759; -.
DR Proteomes; UP000000768; Chromosome 4.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR CDD; cd00078; HECTc; 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; IPR000225; Armadillo.
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:SF4; HECT-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR Pfam; PF00632; HECT; 1.
DR SMART; SM00185; ARM; 3.
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:UP000000768};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 1441..1832
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 1..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 593..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 902..1060
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1076..1108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1480..1499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..607
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 907..951
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 990..1013
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1014..1047
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1799
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1832 AA; 198361 MW; BBA3B60915B70F74 CRC64;
METRSSSRKR AAAAASSSAS KRPRRNSSSS SSSAPPPMEP SPSSRRRSRA AAAADKGKDP
DPSSSDHPSP PVPDEDADVP FPQSFTSAST ALQGLLRRLG AGLDDLLPSS SSAPSSATSG
HLKRILAGLQ AHGDESRQLQ SLMQLCEMLS IGTEDSLAAF PVDAFVPILV GMLGREDEPA
TAGASPDVML LAARALANLV DVLPSSCSAV VHYGAIQCFC ARLLTIEYMD LAEQSLQALK
KISLEHPTAC LRAGALMAVL SYLDFFSTGV QRVALSTAAN ICRKLPSDAS EFVMEAVPLL
TNLLNHHDSK VLEHASVCLT RIAEAFAHYP DKLDELCNHG LVAQAASLIA VGNSSGQASL
STSTYTGLIR LLSICASGSL LAVKTLLLLG ISGTLKDILS GSALISGASV SPAVTRPADQ
MFEIVSLADD LLPHMPARII KLPTYYHAYK GSSTKKSASI KQEGAGSTGN ERSGRERLLR
EQPELLQQFG MDLLPTMTQV YGSSVNAPIR HKCLSIIGKL MYYSSAETIQ SLLGTTNISS
FLAGILAWKD PQVLIPALQI AEIMMEKLPE AFSKLFVREG VVHAVESLIC SESSNTMPSQ
VPPQDKDNDS AMPSRPRRQR RRGGAVAAEN SSLDESNSSN LGVTCSTTIT SEAPNTSLRL
AVSDHAKSFK DKYFPADTDS SDIGVTDDLL KLRALCAKLN TVSENVKTKA KGKSKAISAN
FLDISIDVEE QLDKIISEIL SELSKVNGVS TFEFIRSGVV TALLDYLSCG TFGKEKVSEG
NLPQLRQQVL RRYKSFISVA LSIDHERDET PMALLVQKLQ SALSSLERFP VVLSQSSRIG
IGGSRLTSGL SALAQPFKLR LSRAQGEKSL RDYSSNIVLI DPFASLAAVE EFLWPRVQRG
EVPSKPIIPS GNNSESGVPG TTAGASLTAA MAQSGRRPTT RSKSSAAGVG TSKKDSHDES
TSTAKGKGKA IVKPNSDESK GPNTRNAARQ KSASEKDSEM KRAQGHSSSE DEELDTSPVE
IDDALMIDDD DISDDDDDDD DDDDHEVLQE GSLPICSQDG VHDVKLSDAD ECNIGSASFS
QAQPSSGSGA RNTSSRVPDS TEFRSTSTFG SRGAMSFVAA TMAGLASVGG RSVRGGRDRR
GLSLGGSMND HNKLIFTAGG KQLSKHLTVY QAIQRQLMLD EDDEERFNGS DIPNDGNRFW
GDVFTITYQK ADNQVEKGCQ GTSTSLNIKS DSYRSISEAQ GVSLLDSILQ GELPCDLERT
NSTYNILALL RVLEGLNQLS SRLRLQGASD DFAEGKITTL DELYRTGAKV PSEVFVNSKL
TPKLARQMQD VLALCSGSLP SWCYQMTKAC PFLFPFETRR QYFYSTAFGL SRALNRLQQQ
QSDNHSSGGE REVRFGRLQR QKVRVSRNRI LDSAAKVMEM FSSQRAVLEV EYFGEVGTGL
GPTLEFYTLL SHELQSAQLG LWRSSSYDSG LHIDRKDVIS LDPEDDSSGK GPNTDLPGDG
RHLIQAPLGL FPRPWPPKVD ASEGSRLFKV LEHFRLIGQV MAKVLQDGRL LDLPLSTAFY
KLILGQELDL FDIVSFDSEF GKTLQELRVL VERKQFLEST CGKNQLQVAD LRFHGASIED
LCLDFTLPGY PDYVLKEGEG STIVNIYNLE EYITLVVDAT VKSGIKRQVE AFRSGFNQVF
DMSSLHIFSP QELDYLICGR QEIWELESLV DNIKFDHGYT AKSPAIVNLL EILSEFTPEQ
QHAFCQFVTG APRLPPGGLA ALNPKLTIVR KHPSSAVNTS NSTGATESAD DDLPSVMTCA
NYLKLPPYST KEIMRKKLLY AILEGRGSFD LS
//
