ID A0A1B6QBC8_SORBI Unreviewed; 3830 AA.
AC A0A1B6QBC8;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
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_3002G147600 {ECO:0000313|EMBL:KXG35227.1};
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:KXG35227.1, ECO:0000313|Proteomes:UP000000768};
RN [1] {ECO:0000313|EMBL:KXG35227.1, 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 -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SIMILARITY: Belongs to the UPL family. TOM1/PTR1 subfamily.
CC {ECO:0000256|ARBA:ARBA00034494}.
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DR EMBL; CM000761; KXG35227.1; -; Genomic_DNA.
DR EnsemblPlants; KXG35227; KXG35227; SORBI_3002G147600.
DR Gramene; KXG35227; KXG35227; SORBI_3002G147600.
DR OMA; ADEMKYG; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000000768; Chromosome 2.
DR ExpressionAtlas; A0A1B6QBC8; baseline and differential.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd00078; HECTc; 1.
DR CDD; cd14327; UBA_atUPL1_2_like; 1.
DR Gene3D; 6.10.250.1630; -; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 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; IPR016024; ARM-type_fold.
DR InterPro; IPR010309; E3_Ub_ligase_DUF908.
DR InterPro; IPR010314; E3_Ub_ligase_DUF913.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR025527; HUWE1/Rev1_UBM.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR PANTHER; PTHR11254:SF442; HECT-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR Pfam; PF06012; DUF908; 2.
DR Pfam; PF06025; DUF913; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF00627; UBA; 1.
DR Pfam; PF14377; UBM; 3.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00165; UBA; 1.
DR SUPFAM; SSF48371; ARM repeat; 3.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR SUPFAM; SSF46934; UBA-like; 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS50030; UBA; 1.
PE 3: Inferred from homology;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000000768};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 1387..1428
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 3489..3830
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 1014..1044
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2246..2303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2703..2742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3134..3159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1014..1037
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2249..2277
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 3797
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 3830 AA; 421201 MW; 4885683DAC4B374C CRC64;
MYIYYFDSLR NLPSALHRPV GGNQSRLTSP RLAPRRHAHP IRFLAFSPRR SRQRPRKTLT
TRSLCSDCLR RRRSDPRRRQ TAQRVAPCGG GRRGGGLCLP GDANCGMKLR RRRAIEVPPN
IKSFINSVTT VPLENVELPL KNFAWEFDKG DFHHWVDLFN HFDSFFESYI KSRKDLHLED
NFLDVDPPFP REAVLQILRV SKLILENCTN RHFYIFFEHL SALLASTDAD IIEASLQTLM
AFVDKSVGKS SIRNASLASK LFAFSQGWGG KEGGLGLIAC SLPSVSDPVS TEVGSTLHFE
FYRAADKSEK SQCLENENRL EVIHLLNVNA CKETDLEILD KLIKDYSVPQ ALRFPLLTRL
RFARAFDSLT CRHQYICIRL YAFIVLVQAG HDSEGLSTFL SNEPEFIDEL LSLLSYEDEI
PEKIRILGIL SLVALCQDRS HQPTLLSSVT SGGHRGILPS LMQKAVDSII NGSMKWSIIF
AEALLSLVSM LVSSTPGSLA LQDAGFIPTI LPLLKDTKTQ HLHLVGTAVH VIESFLDYHN
PSSALFRDLG GLDDTIARLK IEVSQIEVVS KKIEESHSNN NGKKVESCPP VQDVQPSCSE
SLILYHRKNL MKVLLRTISL ATYVPGSSAR VDGSEENVLP PCLCKIFKRS KDFGGGVFSL
AANVMSDLIH KDPTCYTVLD AAGLPQAFLD AIMGGVLYNS DAVSCIPQCL DALCLNSNGL
QLVKDRNALR CFVKIFTSRS YLKALSGDTT GALSSGLDEL MRHASSLRSS GVSMFIEILD
TISKVGHGGD SISCNKESDN SSAAVSMDTD VEVATTQSEG VPPEVGCSVK TVDAPLDALT
SSSIELFLPE CICNVARLLE TVLQNTDTCR LFIEKKGIEA VLQLFKLPSI PVSVSIGQSI
SVAFKNFSPQ HSVSLARVVC SFFRDHLKMT NELFGSISGT KLLDSEPTKQ SALLKSLSTL
EGLLSLANFL LKGTAIMVSE LAFADAEILK ELGKVYIEVT WQISLLSDSK VDKQEADQDD
LAGDASISER DSDDDTNTAP FSRYTNPVSA RASLSPWSME QDFVSTVRSA ANMHRHGRHS
LSRISGRPNG VFDATNTDVD GPCFPEETSR SHDALKKSPD VVVSELLTKS GYTMRSFLSS
LVKGLAARRR ADSILNPASR SLVTALAQFF LSALGFSGHS TAGFEMSLSV KCCYLGKVVE
DMAVLTFDSR RRLCNSALVN SFYVNGTFKE VLTTFEATSQ LLWTLPFSVL AAATDQGSSV
SEKVSHNSWL LDTLQSYFKF LEYCVNSTFL LSPSSSHNQL LVQPIVTELS INLFPVPSDP
ESFARMLKSQ VLDAVLPVWN HTMFPECSPA LVTSLVSIMN NICSVVGDMK QNRSSVGVAN
QRVTSPPLDE SAIATIVEMG FSRARAEESL RSIRTNSVEM ATDWLFSHPE EFVQEDVQLA
QALALSLGSS IETPKEDGSH KNDTAIAEEK SVFVLPLDDI LTVSTKLFRS NDSTMAFPLT
DLLMTICNRN KGEYCKRVVL YLFEQLRCFS SDTTGDMGAL YSVAHLLALL LSEDSGIREI
SAENGVISQV LNMLESLKSR TDQTDQTWNS ISALLLILDN MLQFNPKLYI ETMDGISKSI
SDASSADSKA NPLPTAENRT EIIDSADDAS ANVCRKVLGK STGYLNDQES QKALVFCCAF
IKLCVPATVM QAVLQLSARL TKTHALAAHF FESGGLASLL NLPGTCIFPG FEALASAIVR
HLIEDPQTLQ SAMELEIRQS LSNRGSRTPR SFLTIMAPLI SRDPVIFMKA VTSVCQLDYS
GGRMNVVLLK DKEKDREKQK VPVTESGVPC NEPVRLTAEV KSVDTPNRCS RNPKKVPACL
SQVIDQLLEI IMSYPSASKE HRFDGYSLLT PMDVDEPNTK GKSKVDDDQE LDGDALSERS
ALLSKFAFVL KLMSEILLMY VHAVGIILRR DTEISQARSC DQVAGHSGLL HHIFYLLLPL
PSIKMADASD DWIGKLSERA SWFLVALCCR SAEGRRRVVS EIVKAFNYFI GSASNTSKGS
LIPDRKVLAL SELVNSILSR NSQSNLPVLG CSPDIAKPMV DGGMVQSLSG LLKVIDLDHP
DAARVVNLIL KALDSLTRTA YASDQVLKTD RFTNNRLPGS HEQTREADDT VIHEQTTGGT
HHHTNDIIQS ASQQAQELSH IGGNNNENFD QPAEQEMGVD LADNNNTSNG NPPMRAVQFM
REEAIEGNVM ATSTDVSLAF SVQHQVDDEM GVEDEDLGEE GEDEDDEDED DEEIADEGAG
LMSIADTDIE DQENNAIDDE YNDDLMDEDD DFLENRVIEV RWRESLTGMD NHLRFSRGRA
DSSGFIDISS ESFHGVGTDD SFNLHRSFGL ERRRQSGSRS LLDRPRTEGN AFLHPLLVRP
AHSREGTSLE WPSGRTSSRD FHTLSFGNSD IPLYMLDAGF PQETSPAVFG ERVVSTAPPP
LIDFSLGLDS LRIRRGPGDN LWTDDGHPQA GNHAAAVAQA VEGHFVSQLT VASNSNNAPQ
VQPEQTGNGV NAQLALPDTG NAEPVATDPL CQPGSHQPVC TVNQGLAPAN DVRCPTDVHV
NQQLAGSIYD NRVEEEVRQT APDDPNAALP QSDEMMCIAD TQLDGHPERD SLSGNESYGH
IMQNEIEAPR QVHLSNDPRE APSDQSSCHA LVTSATAAPE LSDAHVDSAA VDADVDMNSV
DIAENEVENS APASDGNDLS SRRHEEAEPQ TEQPNANNEA SSANEIDPTF LEALPEDLRA
EVLASQQNRS APAASYTPPA AEEIDPEFLA ALPPDIQAEV LAQQRAQRIA HSQPVGQPVD
MDNASIIATF PPDLREEVLL TSSEAVLSAL PSALLAEAQM LRDRELSRYR ARGSLFGGSY
RLGGRRLPTD NQTIIDRAVG VTVGRRVIST TPGGSKGKDV EGTPLLDSEA LRALIRLLQL
APPLSKGLLQ RLMFNLCAHS VTRVTLVGHL LDMIKPESEG LSVSDCMATY RLHGCQWNIV
YAQPYSANGL PPLVTRRLLE LLTYLASNHP SVADLLIHFS PSASSNCLTL QHNKETSQES
PTPNRMQPSS EGYTPILLFL KLLNKPLFLR SRVYLEQVMC LLEVVVNNAA SQIDCPPHSA
QITNSSDIEL VDGTPSQTHV EPSTLEQGHI PDNNQSRDVE VPPTCAKQND NVHEILTQLP
DAELHNLCNI LALEGLPDKV YSLAAEVVKQ LASVAASHRK FFSIELAGVA QSLSSSAVEE
LLTLKNTQML GLSTCSMAGA AILRVLQVLS TLTSGVMDSR HEKDLLQEEQ SILWDLNVGL
EPLWQELSDC ISATEAKFVH NSSLASHAPL MDALEVGASS SGSSSLPPGT QRLLPFIESF
FVLCEKLQTN QPVTLSDYSV TAPEVKESAG SSSSPSLKTS GICNVTFIRV AEKHRRLLNV
FIRQNPSLLE KSLSMMLKVP RLIDFDNKRA YFRSRIRQQH DQHLSAPLRI SVRRAYVLED
SYNQLRLRRT QDLKGRLTVQ FQGEEGIDAG GLTREWYQLL SRVIFDKGAL LFTTVGNNAT
FQPNPNSVFQ TEHLSYFKFV GRVVAKALFD GQLLDVHFTR SFYKHILGAK VTYHDIEAID
PDYYKNLKWM LENDVSDLPD LTFSMDPDEE KHILYEKTEV TDYELKPGGR NIKVTEETKQ
EYVDLVAEHI LTTAIRPQIN GFLEGFTELV PRDLISLFND KELELLISGL PEIDLDDLKV
NTEYIGYSAA SPVIQWFWEV VKAFSKEDMA RLLQFVTGTS KVPLEGFKAL QGISGPQRFQ
IHKAYGAPDR LPSAHTCFNQ LDLPEYTSKE QLEERLLLAI HEASEGFGFG
//
