ID A0A4W4ETV9_ELEEL Unreviewed; 967 AA.
AC A0A4W4ETV9;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Ubiquitin-like modifier activating enzyme 1 {ECO:0000313|Ensembl:ENSEEEP00000015661.1};
GN Name=uba1 {ECO:0000313|Ensembl:ENSEEEP00000015661.1};
OS Electrophorus electricus (Electric eel) (Gymnotus electricus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Gymnotiformes;
OC Gymnotoidei; Gymnotidae; Electrophorus.
OX NCBI_TaxID=8005 {ECO:0000313|Ensembl:ENSEEEP00000015661.1, ECO:0000313|Proteomes:UP000314983};
RN [1] {ECO:0000313|Proteomes:UP000314983}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24970089;
RA Gallant J.R., Traeger L.L., Volkening J.D., Moffett H., Chen P.H.,
RA Novina C.D., Phillips G.N.Jr., Anand R., Wells G.B., Pinch M., Guth R.,
RA Unguez G.A., Albert J.S., Zakon H.H., Samanta M.P., Sussman M.R.;
RT "Nonhuman genetics. Genomic basis for the convergent evolution of electric
RT organs.";
RL Science 344:1522-1525(2014).
RN [2] {ECO:0000313|Proteomes:UP000314983}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28695212;
RA Traeger L.L., Sabat G., Barrett-Wilt G.A., Wells G.B., Sussman M.R.;
RT "A tail of two voltages: Proteomic comparison of the three electric organs
RT of the electric eel.";
RL Sci. Adv. 3:e1700523-e1700523(2017).
RN [3] {ECO:0000313|Ensembl:ENSEEEP00000015661.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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; A0A4W4ETV9; -.
DR Ensembl; ENSEEET00000015841.1; ENSEEEP00000015661.1; ENSEEEG00000007735.1.
DR GeneTree; ENSGT00940000165405; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000314983; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
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; 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:SF195; UBIQUITIN-LIKE MODIFIER-ACTIVATING ENZYME 1; 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; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU000519};
KW Reference proteome {ECO:0000313|Proteomes:UP000314983};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU000519}.
FT TRANSMEM 802..822
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 843..865
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 904..925
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 834..962
FT /note="Ubiquitin-activating enzyme E1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00985"
FT ACT_SITE 559
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ SEQUENCE 967 AA; 107900 MW; 5CB0112F7E27294C CRC64;
MAKNGNVAEI DEGLYSRQLY VLGHDAMKRM QNSNVLISGL RGLGVEIAKN VILGGVKSVT
LHDQGVAEWR DLSSQFYLRE EDLGKNRAEV SQNRLAELNS YVPVTSYTGA LTNDYLTQFQ
VVVLTNSTLD EQMHIGDFCH SKGIKLIIAD TRGLFGQLFC DFGDEMMVYD TNGEQPLSAM
ISMITKDSAG VVTCLDEARH GFETGDHVTF MEVQGMTELN GCPPIEIKVL GPYTFSICDT
SSFSDYVRGG IVTQVKMPKK VAFKSFSSSM SEPEFLLTDF AKFDRPGQLH VGFQALHAFE
KKHSRSPKPW NQVMALANDV NAAQSGPAKQ DELDEGLLKK LSCMAAGDLA PVNAFIGGLA
AQEVMKVTNI FYTPLYCRYD GQIAVFGSKL QDLLGKQRYF LVGAGAIGCE LLKNFAMMGL
ATGEGEVIVT DMDTIEKSNL NRQFLFRPWD VTKMKSETAA AAVKQMNPSI RITGHQNRVG
PDTERIYDDD FFENLDGVAN ALDNVDARMY MDRRCVYYRK PLLESGTLGT KGNVQVVIPF
LTESYSSSQD PPEKSIPICT LKNFPNAIEH TLQWARDEFE GLFKQPVENF GVNSFSVNRA
GSLCLIVVEA VYKSLVSEYP RSWEQCVAWA RNHWQCQYSN NIRQLLHNFP PDQLTSSGAP
FWSGPKRCPH PLEFSTSNDL HMDYIVAAAN LVAQAYGLQG STDRADVAKV LQDVKVPEFT
PKSGVKIHVS DQELQSANAS VGKEQRVILH PSLDLMCFAL SPKDDDTNFH MDFIVAASNL
RAENYDIPPA DRHKSKLIAG KIIPAIATTT AAVVGLVCLE LLKIVQGHKK LESYKNGFMN
LSLPFFAFSE PIATLLIYGL LLQYYEIDWT LWDRFEVKGI QPSGEEMTLR QFLDYFKNEH
KLEITMLSQG VSMLYSFFMP AANMTEIVTK VSKKKLGKHV KALVFELCCN DITDEDVEVP
YVRYTIR
//
