ID A0A6Q2YL79_ESOLU Unreviewed; 1004 AA.
AC A0A6Q2YL79;
DT 02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=E1 ubiquitin-activating enzyme {ECO:0000256|ARBA:ARBA00012990};
DE EC=6.2.1.45 {ECO:0000256|ARBA:ARBA00012990};
DE AltName: Full=Ubiquitin-activating enzyme E1 {ECO:0000256|ARBA:ARBA00030371};
OS Esox lucius (Northern pike).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC Esocidae; Esox.
OX NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000066759.1, ECO:0000313|Proteomes:UP000265140};
RN [1] {ECO:0000313|Ensembl:ENSELUP00000066759.1, ECO:0000313|Proteomes:UP000265140}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25069045;
RA Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT "The genome and linkage map of the northern pike (Esox lucius): conserved
RT synteny revealed between the salmonid sister group and the Neoteleostei.";
RL PLoS ONE 9:e102089-e102089(2014).
RN [2] {ECO:0000313|Ensembl:ENSELUP00000066759.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 AlphaFoldDB; A0A6Q2YL79; -.
DR Ensembl; ENSELUT00000053108.1; ENSELUP00000066759.1; ENSELUG00000022770.2.
DR GeneTree; ENSGT00940000166002; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000265140; LG17.
DR Bgee; ENSELUG00000022770; Expressed in stomach and 14 other cell types or tissues.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004839; F:ubiquitin activating enzyme activity; IEA:UniProtKB-EC.
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:SF198; E1 UBIQUITIN-ACTIVATING ENZYME; 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.
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:UP000265140};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU000519}.
FT DOMAIN 872..999
FT /note="Ubiquitin-activating enzyme E1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00985"
FT ACT_SITE 578
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ SEQUENCE 1004 AA; 111134 MW; FF6E26A53EDC40DE CRC64;
MRRMGTAAVL IAGMRGLGVE IAKNVILSGV KSVTVQDEGL AQWMDLSSQQ RCVTITTDLK
LFFLQVSHLG QNRALISQPQ LSALNPHVCV SAHTGKLNEK LLLQFQVVVL TDSSLEDQQR
FGAFCHSNGI KFIVADTKGL CGQLFCDFGK EFEVLDPDGE TPPSVMIDNI TKTDPGVVKC
SEPVNGFVDG CSVSFSEVCG MKELNEYGPV EIKVLGPDSF SICDTSGFSA YEKCGVATEV
KNSKTLTFKP LNEALTDLEL LVYTDHGKIS NHQTLHLAFQ ALHGFVKQEG RLPEARSQSD
AELLVALVKE LNKVYKLEQL DEEVVRSLSL TARGDLAPIN AFIGGLAAQE VLKACSGKFS
PLQQCLYFDA LECLPEDNQE DGEQWRESTY LPSGSRYDGQ AVVFGSAFQE KLGKQRYFLV
GAGAIGCELL KNFALIGLGA GQGGHITVTD MDSIERSNLN RQFLFRSQDI GRQKSEVAAQ
AVRAMNPSMN ITAHQNCLDP DSEKVYGYHF FMGLDGVAAA LDNVEARVYL DSRCVHHQRP
LLDGGTLGTK GSTLVVVPHL TQSYGPAKTN SRDAIPLCTL KNFPHRIEHT LQWAKDQFEG
LFKQAAENVN QYLGEGAGFL ERTLGRGEAE ALEVLECVWG AVGMQRPRGW DDCVGWARRQ
WETVYNNDIA QLIHCFPPQQ LTSSGLPFWS GTKRCPHPLN FDPNDTTHMD YVVAASNLYG
QIYGIVGTRD ISAIKSILEK VHIPAFTPKS AVKIHLTDEE MEEDKNSGDF DTERLEELHK
KLSSPPMNSS DLQMHPMVFE KDDDNNFHMD YIVAASNLRA ENYDIPTADR HKSKLIAGRI
IPAIATTTTA VAGLMCLELY KLVQGHKRIS SYRSAFINLA VQYCVLSEPL GPRRFTFAGK
EYSLWDDFLV QGRRESGQEM TLGELLEHIK QEHHLQVTGL YYGNAVVYDG GSNHKERLAK
SVSEVVSLAT KTEVPEHLCV LEMFASIAED EDCETFPPIR YLFK
//
