ID A0A0V1LT66_9BILA Unreviewed; 1185 AA.
AC A0A0V1LT66;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=E1 ubiquitin-activating enzyme {ECO:0000256|ARBA:ARBA00012990};
DE EC=6.2.1.45 {ECO:0000256|ARBA:ARBA00012990};
GN Name=UBA1 {ECO:0000313|EMBL:KRZ62728.1};
GN ORFNames=T02_9848 {ECO:0000313|EMBL:KRZ62728.1};
OS Trichinella nativa.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6335 {ECO:0000313|EMBL:KRZ62728.1, ECO:0000313|Proteomes:UP000054721};
RN [1] {ECO:0000313|EMBL:KRZ62728.1, ECO:0000313|Proteomes:UP000054721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS10 {ECO:0000313|EMBL:KRZ62728.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRZ62728.1}.
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DR EMBL; JYDW01000006; KRZ62728.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1LT66; -.
DR STRING; 6335.A0A0V1LT66; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000054721; Unassembled WGS sequence.
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; 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: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; 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:UP000054721};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU000519}.
FT DOMAIN 1004..1129
FT /note="Ubiquitin-activating enzyme E1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00985"
FT REGION 46..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..89
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 683
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ SEQUENCE 1185 AA; 134324 MW; A4312CB6E8921615 CRC64;
MENPVKLSSY DCVLQFHLEI LRIQCDFVCR FPRYESSMSL CEESTKNLNS NQVDPNNPSP
PSKRSKIDSI DCSTGDKIQK SRTDMVEGSD SRNSENSFNT DMANGRSKLG SFDPQLYSRQ
LYALGEVAMR RLRISTVLIS GIGGVGVEIA KNLILGGIRH VTIHDTKTAT WLDLSAQYYL
NEQCLGKNRA VESWPHLEEL NDSVTVGCIT EELNENLLVI ITEATLAEQK QINLWTRKYG
KKFIAADCRG LFGVLFNDFG SNHIIDDSNG EPCTEETGNV FVLEDTKHNL EDGDYVTFRE
VKGMVELNDC PPRKVKVINT MEFNIGDISA YSEHTEGGKA KTVKVPVKME FVSLNEALLD
PEILVSDHSK LDRPPQMHVI WQGLHMFFEK EGRLPRPQNL ADAEQMLQYC EEINTQLPDK
IRLEKVDARL AKMLSFQAVG NLVAMNGFIG GIAAQEAMKA VTGIFTPIHQ WLYFDSLECL
PETDSAYGLR DEGACRLQGS RYDGQAAVFG WNFQEALAKQ KWLIVGAGAI GCELLKNFAM
MGVACGKEGC LIITDMDNIE LSNLNRQFLF RRSDVGAKKA EVAGKVAKTF NSQLNVVAMC
ERVGTGTENI FDDAFFEKLD GVANALDNIE ARTYVDRRCV YYRLPLLDSG TQGPKGSTQV
VYPFLTESYS SSHDPPEKSI PICTLRNFPN TIEHTIQWAR DLFEGAFSIP AELANQFLDD
PRGFFDRIDK MHDSQKLELL ENVYHYLSDD RPATVEACVR WARLQFEQHF NFQIQQLLYS
FPEDQLTAFG TKFWSGSKRC PHAIYFDSSN PEHRQFIFAS AFLRAQMYAM KPIDDMDKVV
ELASEVKPPP FKPKIGLKIP TTDEEAAELA GATSGEYLCF LNTTTAPCKD YPCFFCIVSD
DDSRFQDLQL MLAKLKPDKT SRLVPIDFEK DDDTNHHMEF ITAASNLRAE NYKIEKADFM
KTKQIAGRII PAIATTTAAV AGLVGLEFYK IVSSSSKKAN LERFKNSFMN LALPFFGFAE
PIRTPVKKFY DKEWTLWDCL ELKGEMTLKE FLSYMKEKFN VEVTMLSQGV SMLFSFFLPL
AKQQQRMNMK VTDLVESITG QKIPSYVNAI VLETMCTDEH GEDIELPYIK YRHFQLFRFR
GSIWKSVYHQ HIYLFIDVVS NDAPMVWKWL VRIASIINNN YLCGM
//
