ID A0A194YKH3_SORBI Unreviewed; 1086 AA.
AC A0A194YKH3;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=SORBI_3010G202600 {ECO:0000313|EMBL:KXG20452.1};
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:KXG20452.1, ECO:0000313|Proteomes:UP000000768};
RN [1] {ECO:0000313|EMBL:KXG20452.1, 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=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CM000769; KXG20452.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A194YKH3; -.
DR STRING; 4558.A0A194YKH3; -.
DR EnsemblPlants; KXG20452; KXG20452; SORBI_3010G202600.
DR Gramene; KXG20452; KXG20452; SORBI_3010G202600.
DR eggNOG; KOG1609; Eukaryota.
DR InParanoid; A0A194YKH3; -.
DR OMA; WLHYSLV; -.
DR OrthoDB; 1342875at2759; -.
DR Proteomes; UP000000768; Chromosome 10.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0042335; P:cuticle development; IEA:EnsemblPlants.
DR GO; GO:0010143; P:cutin biosynthetic process; IEA:EnsemblPlants.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:EnsemblPlants.
DR GO; GO:1900486; P:positive regulation of isopentenyl diphosphate biosynthetic process, mevalonate pathway; IEA:EnsemblPlants.
DR GO; GO:0009414; P:response to water deprivation; IEA:EnsemblPlants.
DR GO; GO:0010345; P:suberin biosynthetic process; IEA:EnsemblPlants.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
DR GO; GO:0010025; P:wax biosynthetic process; IEA:EnsemblPlants.
DR CDD; cd16702; RING_CH-C4HC3_MARCH6; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR011016; Znf_RING-CH.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR13145:SF0; E3 UBIQUITIN-PROTEIN LIGASE MARCHF6; 1.
DR PANTHER; PTHR13145; SSM4 PROTEIN; 1.
DR Pfam; PF12906; RINGv; 1.
DR SMART; SM00744; RINGv; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS51292; ZF_RING_CH; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Reference proteome {ECO:0000313|Proteomes:UP000000768};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT TRANSMEM 119..141
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 161..185
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 312..333
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 430..453
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 493..512
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 541..564
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 598..617
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 760..785
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 859..882
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 894..911
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 951..974
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 986..1004
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 28..89
FT /note="RING-CH-type"
FT /evidence="ECO:0000259|PROSITE:PS51292"
FT DOMAIN 36..83
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 693..712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 731..753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 248..282
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 698..712
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1086 AA; 122160 MW; DE6E2FA7D4A02D3F CRC64;
MAEIAERAVA GELPEEPRPP HGEEEDEEEE EEGDVCRICR NRGDEDHPLR YPCACSGSIK
FVHQDCLLQW LDHSNSRQCE VCKHAFSFSP VYAENAPTRL PFQELIVGVG MKACHVFQFI
LRLAFVLSVW LMIIPFITYW IWRLTFVRSL GEAQRLFLSH ISAQLILSDC LHGFLLSAII
VLIFLGATSL RDYIRHLREL GGHDAERDDG GRERHGARAV RRLAGPNNRV PGDANIDELA
EAQGIGPGEL LRRNAENVAA RLERLEAQVE QMLDGLDDAD GAEDVPFDEL VGMQGPVFHL
VENAITVLAS NAIFLIVVIF VPFSLGRIVL YYLSWFFSSA STPMLAKMMP FTETAISIAN
DTLKSALNVV KNFSSDSNNE GVIGHVIEVV TQSLKINATG LSVIQGTGKS SLMKGTTIGS
SYLSDLTTLA VGYMFIFCLV FLYIGSLALL RYARGERFTI GRLYGIATIL EAIPSLCRQF
FAGMKHLMTM VKVAFLLVIE LGVFPLMCGW WLDVCTLKML GTTIAQRVEF FTMSPLASSS
IHWLVGIVYM LQISIFVSLL RGVLRNGVLY FLRDPADPNY NPFRDLIDDP VHKHARRVLL
SVAVYGSLIV MLVFLPVKLA MRVAPSIFPL DITIFDPFTE IPVDVLLFQI CIPFAIEHFK
PRATIKSLLH HWFAAVGWAL GLTDFLLPKP EENGGQENWN GRAERRDRGH GGREMVAPQV
EQRMIQHVAA EDNGRGNANE ANDATEESDV DDQGDSEYGF VLRIVLLLVL AWVTLLIFNA
GMIVIPISLG RLVFEAVPRL PITHGIKCND LFSFSIGCYI LWSAAAGTRY AIDYIRSRQL
GFLVQQICKW CSIVLKSSFL LSIWIFVIPV LIGLLFELLV IVPMRVPIDE SPVFLLYQDW
ALGLIFLKIW TRLVMLDQMA PLVDESWRSK FERVRDDGFS RLRGLWVLHE IIMPIVTKLL
TALCVPYVLA RGIFPVLGYP LIVNSAVYRF AWLGCLIFSA LFFCGKRFHV WFTNLHNSIR
DDRYLIGRRL HNFGEDSHSP EPSESGATIG SDDQDRALVL RDQEEDVGLR MRRNNMRANQ
QPRLAL
//
