ID C5X6C6_SORBI Unreviewed; 1053 AA.
AC C5X6C6;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 2.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=E1 ubiquitin-activating enzyme {ECO:0000256|ARBA:ARBA00012990};
DE EC=6.2.1.45 {ECO:0000256|ARBA:ARBA00012990};
GN ORFNames=SORBI_3002G428800 {ECO:0000313|EMBL:EER99949.2};
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:EER99949.2, ECO:0000313|Proteomes:UP000000768};
RN [1] {ECO:0000313|EMBL:EER99949.2, 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 -!- FUNCTION: Activates ubiquitin by first adenylating its C-terminal
CC glycine residue with ATP, and thereafter linking this residue to the
CC side chain of a cysteine residue in E1, yielding a ubiquitin-E1
CC thioester and free AMP. {ECO:0000256|ARBA:ARBA00002457}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine
CC = AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-
CC L-cysteine.; EC=6.2.1.45; Evidence={ECO:0000256|ARBA:ARBA00000488};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family.
CC {ECO:0000256|ARBA:ARBA00005673, ECO:0000256|RuleBase:RU000519}.
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DR EMBL; CM000761; EER99949.2; -; Genomic_DNA.
DR AlphaFoldDB; C5X6C6; -.
DR STRING; 4558.C5X6C6; -.
DR EnsemblPlants; EER99949; EER99949; SORBI_3002G428800.
DR Gramene; EER99949; EER99949; SORBI_3002G428800.
DR eggNOG; KOG2012; Eukaryota.
DR HOGENOM; CLU_832635_0_0_1; -.
DR InParanoid; C5X6C6; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000000768; Chromosome 2.
DR ExpressionAtlas; C5X6C6; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004839; F:ubiquitin activating enzyme activity; IBA:GO_Central.
DR GO; GO:0006974; P:DNA damage response; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR CDD; cd01491; Ube1_repeat1; 1.
DR CDD; cd01490; Ube1_repeat2; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 2.40.30.180; Ubiquitin-activating enzyme E1, FCCH domain; 1.
DR Gene3D; 3.50.50.80; Ubiquitin-activating enzyme E1, inactive adenylation domain, subdomain 1; 1.
DR Gene3D; 3.40.50.12550; Ubiquitin-activating enzyme E1, inactive adenylation domain, subdomain 2; 1.
DR Gene3D; 1.10.10.2660; Ubiquitin-activating enzyme E1, SCCH domain; 1.
DR Gene3D; 3.10.290.60; Ubiquitin-activating enzyme E1, UFD domain; 1.
DR InterPro; IPR032420; E1_4HB.
DR InterPro; IPR032418; E1_FCCH.
DR InterPro; IPR042302; E1_FCCH_sf.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR018965; Ub-activating_enz_E1_C.
DR InterPro; IPR042449; Ub-E1_IAD_1.
DR InterPro; IPR038252; UBA_E1_C_sf.
DR InterPro; IPR019572; UBA_E1_SCCH.
DR InterPro; IPR042063; Ubi_acti_E1_SCCH.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR InterPro; IPR018075; UBQ-activ_enz_E1.
DR InterPro; IPR018074; UBQ-activ_enz_E1_CS.
DR InterPro; IPR033127; UBQ-activ_enz_E1_Cys_AS.
DR InterPro; IPR000011; UBQ/SUMO-activ_enz_E1-like.
DR NCBIfam; TIGR01408; Ube1; 1.
DR PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR PANTHER; PTHR10953:SF226; UBIQUITIN-ACTIVATING ENZYME E1 3; 1.
DR Pfam; PF16191; E1_4HB; 1.
DR Pfam; PF16190; E1_FCCH; 1.
DR Pfam; PF09358; E1_UFD; 1.
DR Pfam; PF00899; ThiF; 2.
DR Pfam; PF10585; UBA_E1_SCCH; 1.
DR PRINTS; PR01849; UBIQUITINACT.
DR SMART; SM00985; UBA_e1_C; 1.
DR SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 2.
DR PROSITE; PS00536; UBIQUITIN_ACTIVAT_1; 1.
DR PROSITE; PS00865; UBIQUITIN_ACTIVAT_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU000519};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU000519};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU000519};
KW Reference proteome {ECO:0000313|Proteomes:UP000000768};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU000519}.
FT DOMAIN 926..1048
FT /note="Ubiquitin-activating enzyme E1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00985"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 629
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ SEQUENCE 1053 AA; 116300 MW; D22BFC45C5EC4120 CRC64;
MLPSKRSAGA DGGESKRAKL GESPSSAAAA VGTASNGTRN GAAPEIDEDL HSRQLAVYGR
ETMRRLFAAD VLVSGLNGLG AEIAKNLALA GVKSVTIHDV KMVEMWDLSG NFFLSEQDVG
KNRAVACVSK LQELNNAVLV SALTEELTSE HFSKFQAVVF TDISLEKAYE FDDYCHSHQP
PISFIKAEVC GLFGSVFCDF GPEFTVLDVD GEDPHTGIIA SISNDSPAMV SCVDDERLEF
QDGDLVVFSE VQGMAELNDG KPRKVKNARP FSFSIEEDTS SYGVYTKGGI VAQVKEPKVL
RFKALRDAMR DPGDFLLSDF SKFERSPVLH LAFQALDKFK KEHGRYPTAG CEQDAQTFLK
FAADINEASV GPKLENIDEK LLCHFASGSR AVLNPMAAMF GGIVGQEVVK ACSGKFHPLY
QFFYFDSVES LPTYQLDPQD LKPSNSRYDA QVSVFGSKLQ KKMLDANIFI VGSGALGCEF
LKNLALMGVS CSSKGKLTIT DDDVIEKSNL SRQFLFRDWN IGQAKSTVAA AAAIAINPSL
QIDALQNRAS PDTENVFHDT FWDGLDVVIN ALDNVNARMY MDMRCLYFQK PLLESGTLGA
KCNTQMVIPH LTENYGASRD PPEKQAPMCT VHSFPHNIDH CLTWARSEFE GLLEKTPNEV
NSFLSNPAQY AAAMRKAGDA QARELLERVS ECLDKERCNT FEDCITWARL RFEDYFSNRV
KQLTFTFPED AATSTGTPFW SAPKRFPRPL QFSATDSSHI NFIMAASILR AESFGIAIPD
WAKNASKLAD AVDKVAVPKF EPKKGVNIVT DEKATNLSSA SVDDVAVIND LLTKLEEYAK
GLPPGFQMKP IQFEKDDDTN FHMDLIAGFA NMRARNYSIP EVDKLKAKFI AGRIIPAIAT
STAMATGLVC LELYKVIAGE HPIEDYRNTF ANLALPLFSM AEPVPAKVMK HQDLSWTVWD
RWTIKGNLTV AELLQWFSDK GLSAYSMSCG TSLLYNSMFA RHKDRLQKKV VDVAREVAKV
EVPEYRKHID VVVACEDDDG NDIDIPLVSV YFR
//
