ID A0A0V1PFI8_9BILA Unreviewed; 1105 AA.
AC A0A0V1PFI8;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
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:KRZ95012.1};
GN ORFNames=T08_14753 {ECO:0000313|EMBL:KRZ95012.1};
OS Trichinella sp. T8.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ95012.1, ECO:0000313|Proteomes:UP000054924};
RN [1] {ECO:0000313|EMBL:KRZ95012.1, ECO:0000313|Proteomes:UP000054924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS272 {ECO:0000313|EMBL:KRZ95012.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-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:KRZ95012.1}.
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DR EMBL; JYDM01000015; KRZ95012.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1PFI8; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000054924; 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; 2.
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:UP000054924};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU000519}.
FT DOMAIN 953..1078
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 1105 AA; 124981 MW; A1478060E96A895E CRC64;
MENPVQLSSY 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 EEINTQLPEK
IKLEKVDARL AKMLSFQAVG NLVAMNGFIG GIAAQEAMKA VTGIFTPIHQ WMYFDSLECL
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 FKPKIDLQLM LAKLKPDKTS RLVPIDFEKD DDTNHHMEFI TAASNLRAEN
YKIEKADFMK TKQIAGRIIP AIATTTAAVA GLVGLEFYKI VSSSSKKANL ERFKNSFMNL
ALPFFGFAEP IRTPVKKFYD KEWTLWDCLE LKGEMTLKEF LSYMKEKFNV EVTMLSQGVS
MLFSFFLPLA KQQQRMNMKV TDLVESITGQ KIPSYVNAIV LETMCTDEHG EDIELPYIKG
IFSCFGFEVQ FGKAYITNTS TYLLM
//
