ID A0A059AEP6_EUCGR Unreviewed; 1689 AA.
AC A0A059AEP6;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=E1 ubiquitin-activating enzyme {ECO:0000256|ARBA:ARBA00012990};
DE EC=6.2.1.45 {ECO:0000256|ARBA:ARBA00012990};
GN ORFNames=EUGRSUZ_J01907 {ECO:0000313|EMBL:KCW52517.1};
OS Eucalyptus grandis (Flooded gum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW52517.1};
RN [1] {ECO:0000313|EMBL:KCW52517.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW52517.1};
RA Schmutz J., Hayes R., Myburg A., Tuskan G., Grattapaglia D., Rokhsar D.S.;
RT "The genome of Eucalyptus grandis.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
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; KK198762; KCW52517.1; -; Genomic_DNA.
DR STRING; 71139.A0A059AEP6; -.
DR EnsemblPlants; KCW52517; KCW52517; EUGRSUZ_J01907.
DR Gramene; KCW52517; KCW52517; EUGRSUZ_J01907.
DR eggNOG; KOG2012; Eukaryota.
DR InParanoid; A0A059AEP6; -.
DR OMA; SINCKKV; -.
DR UniPathway; UPA00143; -.
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:0004672; F:protein kinase activity; IEA:InterPro.
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; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 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; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
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:SF215; UBIQUITIN-ACTIVATING ENZYME E1 1; 1.
DR Pfam; PF16191; E1_4HB; 1.
DR Pfam; PF16190; E1_FCCH; 1.
DR Pfam; PF09358; E1_UFD; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00899; ThiF; 2.
DR Pfam; PF10585; UBA_E1_SCCH; 1.
DR PRINTS; PR00109; TYRKINASE.
DR PRINTS; PR01849; UBIQUITINACT.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00985; UBA_e1_C; 1.
DR SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
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 Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU000519}.
FT DOMAIN 339..593
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 597..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..667
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1265
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ SEQUENCE 1689 AA; 186331 MW; D1FC4B0CC9733BC4 CRC64;
MAAALECWSS RASTDEDMVE QVLMRTHDRS EGSPAGAAGA ASSGGAREPS SSSSSSSSSS
VMQKKLQRLS RNVSEAIASL KNSLNLDSSR DGAPQASKID GCRRMVWGSV VRSLTQLYPG
SQLPEKLVSN IRKHYDSLPL SYAQAGFDMK DVFLHIKLME QASGDDRPAI LIQEVSQDEV
HGSVFKLTFA CNSSISWSVM SGALDNASIC CKKIQIFEKK GFTLGIVLLL VQAEQERMFK
TRIENALKLA MKKHRPATVK LAFGLCGCQE ETANSREVGQ AEDDVGELNY RNGSENLYPK
VQLQMPLPTS SFVISVDEWQ TIQSGGDEIA KWLLNSDNLE FIDQIGPSSF KGVYKGRRVG
IEKLKGCDKG NSYEFELRKD FLELMTCGHK NVLQFIGVCI EESHGLCVVT KLMEGGSLHD
LMLKSKKLQI REIVRIAIDV VEGIKFMNEH GITYRDLNTQ RILLDRHGNA CLGDMGIVAA
CKSVGEAMEY ETDGYRWLAP EIIAGDPESV SETCMSNVYS FGMVLWEMVT GEAAYAAYSP
VQAAVGIAAC GLRPDIPKDC PQFLRNLMTK CWNNSPSKRP QFSEIVSLLL HYINSGNDNR
KRAGEEGEVV EGGESGGEGV GSSSGAASSA GVSRLKKNRV GCFGPPELTA TGNGKSNADS
GNGSSGSGAP IMALGGSMPT DIDEDLHSRQ LAVYGRETMR RLFASNVLVS GMQGLGVEIA
KNLVLAGVKS VTLHDEGVVQ LWDLSGNFLF SERDVGKNRA LASVEKLQEL NNAVVVTTLT
TKLTKERLSD FQAVVFTDID LQKAIEFDDY CHTHQPPISF IKTEVRGLFG SVFCDFGPEF
TVFDVDGEEP HTGIIASIGN DNPALVSCVD DERLEFQDGD LVVFSEVHGM TELNDGKPRK
IKSARPYSFI LEEDTTNYGA YEKGGIVTQV KLPKVLKFNP LKEAIKDPGD FLLSDFSKFD
RPPLLHLAFQ ALDKFVSEFG RYPVAGSEVD AQRLISVANS INESLGDGKL EDINPKLLQH
FAFGSRAVLN PMAAMFGGIV GQEVVKACSG KFHPLFQFFY FDSVESLPTE PLDLDDLKPR
NSRYDAQVSV FGSKLQKKME DAKVFLVGSG ALGCEFLKNI ALMGVSCGKH GKLTVTDDDV
IEKSNLSRQF LFRDWNIGQA KSTVAASAAT SINPRLNVEA LQNRVGPETE NVFDDTFWEN
LSVVINALDN VNARLYVDQK CLYFQKPLLE SGTLGAKCNT QMVIPHLTEN YGASRDPPEK
QAPMCTVHSF PHNIDHCLTW ARSEFEGLLE KTPAEVNAYL SNPVEYTKAM INSGDAQAKD
TLEHVLECLD KERCETFEDC ISWARLKFED YFTNRVKQLT YTFPEDALTS TGAPFWSAPK
RFPCALQFSV SDPGHLHFVM AASILRAETF GIPVPDWAKN PKKMAQAVDK VIVPGFQPKE
NANIVTDEKA TSLSTASLDD AAVINDLITR LEHCRLKLPP GFRMKPIQFE KDDDTNYHMD
LIAALANMRA RNYSIPEVDK LKAKFIAGRI IPAIATSTAM ATGLVCLELY KVLDGGHKVE
DYRNTFANLA LPLFSMAEPV PPQAVKHRDL TWTVWDRWII KNNPTLRELM QWLQDKGLNA
YSISCGSCLL YNSMFPRHQE RMDRKVVDLA KEVAKLEVPS YRRHLDVVVA CEDDEGNDID
IPQISIYFR
//
