ID M7YXF4_TRIUA Unreviewed; 943 AA.
AC M7YXF4;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=E1 ubiquitin-activating enzyme {ECO:0000256|ARBA:ARBA00012990};
DE EC=6.2.1.45 {ECO:0000256|ARBA:ARBA00012990};
GN ORFNames=TRIUR3_11088 {ECO:0000313|EMBL:EMS51846.1};
OS Triticum urartu (Red wild einkorn) (Crithodium urartu).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4572 {ECO:0000313|EMBL:EMS51846.1};
RN [1] {ECO:0000313|EMBL:EMS51846.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23535596; DOI=10.1038/nature11997;
RA Ling H.Q., Zhao S., Liu D., Wang J., Sun H., Zhang C., Fan H., Li D.,
RA Dong L., Tao Y., Gao C., Wu H., Li Y., Cui Y., Guo X., Zheng S., Wang B.,
RA Yu K., Liang Q., Yang W., Lou X., Chen J., Feng M., Jian J., Zhang X.,
RA Luo G., Jiang Y., Liu J., Wang Z., Sha Y., Zhang B., Wu H., Tang D.,
RA Shen Q., Xue P., Zou S., Wang X., Liu X., Wang F., Yang Y., An X., Dong Z.,
RA Zhang K., Zhang X., Luo M.C., Dvorak J., Tong Y., Wang J., Yang H., Li Z.,
RA Wang D., Zhang A., Wang J.;
RT "Draft genome of the wheat A-genome progenitor Triticum urartu.";
RL Nature 496:87-90(2013).
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. {ECO:0000256|ARBA:ARBA00043952}.
CC -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family.
CC {ECO:0000256|ARBA:ARBA00005673}.
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DR EMBL; KD214669; EMS51846.1; -; Genomic_DNA.
DR AlphaFoldDB; M7YXF4; -.
DR STRING; 4572.M7YXF4; -.
DR eggNOG; KOG2012; Eukaryota.
DR OMA; LANMCAR; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004839; F:ubiquitin activating enzyme activity; IEA:UniProtKB-EC.
DR CDD; cd01491; Ube1_repeat1; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
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; 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; IPR035985; Ubiquitin-activating_enz.
DR InterPro; IPR018075; UBQ-activ_enz_E1.
DR InterPro; IPR018074; UBQ-activ_enz_E1_CS.
DR InterPro; IPR000011; UBQ/SUMO-activ_enz_E1-like.
DR NCBIfam; TIGR01408; Ube1; 1.
DR PANTHER; PTHR10953:SF4; UBA_E1_C DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 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.
PE 3: Inferred from homology;
KW Ligase {ECO:0000256|ARBA:ARBA00022598}.
FT DOMAIN 816..938
FT /note="Ubiquitin-activating enzyme E1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00985"
SQ SEQUENCE 943 AA; 104556 MW; E42502FE9993C982 CRC64;
MVAGEPVGGG SNGNGVAEID EDLHSRQLAV YGRETMRLLF ASNVLVSGLN GLGAETAKNL
ALAGVKSVTL HDVENVDMWD LSGNFFLSED DIGKNRAAAC VEKLQELNNA VLVSAVTEEL
TTEHLSKFQA VVFTNLSLDK AVEFNDYCRS HQPPIPFIKT EVCGLFGSVF CDFGPEFTVL
DVDGEDPHTG IIASISNDNP AMVSCVDDER LEFQDGDLVV FTEVSGMTEL NDGKPRKIVD
ARPFSFCIEE DTRNFGIYAK GGIVTQVKEP MILEFKSLRE CIKEPGNFLL SDFSKYQRPP
LLHFAFLALD NFRKKFGRFP VAGCDQDARK FVEFTASINE AAIDYKMDEL DEKLLQHFAS
GSRAVLNPMA AMFGGIVGQE VVKACSGKFH PQYQFFYFDS LESLPTYALD PKDLKPLNSR
YDAQISVFGS KLQKKMRDSN IFVVGSGALG CEFLKNFALM GVSCGRKGKL TITDDDVIEK
SNLSRQFLFR DWNIGQAKST VAATAASAIN SSLHIDALQN RACPETEHVF NDAFWEGLDA
VINALDNVNA RMYMDMRCLY FQKPLLESGT LGPKCNTQMV IPHLTENYGA SRDPPEKQAP
MFEDYFSNRV KQLTFTFPED AATSTGAPFW SAPKRFPHPV QFSAVDSSHI QFILAASILR
AVSFGIPIPD WAKNMGNLAD IVSKVAVPEF EPKSGVKIET DEKATNLSSA SVDDAAVIED
LLTKLEACAK KLPSGFQMKP IQFEKDDDTN FHMDLIAGLA NMRARNYGIQ EVDKLKAKFI
AGRIIPAIAT TTAMATGLVC LELYKVLAGD HPVEDYRNTF ANLALPMFSM AEPVPPKEMK
HQDLRWTVWD RWSIKGNITV AELLKWLSDK GLTAYSVSCG TSLLYNTMFP RHRDRLKRKM
VDVAQEVAKV DVPAYRKHFD VVVACEDDDG NDIDIPLISI YFR
//
