ID A0A0V0VV91_9BILA Unreviewed; 1087 AA.
AC A0A0V0VV91;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=E1 ubiquitin-activating enzyme {ECO:0000256|ARBA:ARBA00012990};
DE EC=6.2.1.45 {ECO:0000256|ARBA:ARBA00012990};
GN ORFNames=T09_11648 {ECO:0000313|EMBL:KRX66947.1};
OS Trichinella sp. T9.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX66947.1, ECO:0000313|Proteomes:UP000054681};
RN [1] {ECO:0000313|EMBL:KRX66947.1, ECO:0000313|Proteomes:UP000054681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS409 {ECO:0000313|EMBL:KRX66947.1};
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:KRX66947.1}.
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DR EMBL; JYDN01000008; KRX66947.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0VV91; -.
DR STRING; 181606.A0A0V0VV91; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000054681; 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:SF162; SUMO-ACTIVATING ENZYME SUBUNIT 1; 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|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU000519};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU000519};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU000519};
KW Reference proteome {ECO:0000313|Proteomes:UP000054681};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU000519}.
FT DOMAIN 950..1075
FT /note="Ubiquitin-activating enzyme E1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00985"
FT REGION 1..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..52
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 654
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ SEQUENCE 1087 AA; 122573 MW; 87F691C17D9D9D2F CRC64;
MSLCEESTKN LNSNQVDPNN PSPPSKRSKI DSIDCSTGDK IQKSRTDMVE GSDSRNSENS
FNTDMANGRS KLGSFDPQLY SRQLYALGEV AMRRLRISTV LISGIGGVGV EIAKNLILGG
IRHVTIHDTK TATWLDLSAQ YYLNEQCLGK NRAVESWPHL EELNDSVTVG CITEELNENL
LVIITEATLA EQKQINLWTR KYGKKFIAAD CRGLFGVLFN DFGSNHIIDD SNGEPCTEVI
INHIDRETGN VFVLEDTKHN LEDGDYVTFR EVKGMVELND CPPRKVKVIN TMEFNIGDIS
AYSEHTEGGK AKTVKVPVKM EFVSLNEALL DPEILVSDHS KLDRPPQMHV IWQGLHMFFE
KEGRLPRPQN LADAEQMLQY CEEINTQLPE KIKLEKVDAR LAKMLSFQAV GNLVAMNGFI
GGIAAQEAMK AVTGIFTPIH QWLYFDSLEC LPETDSAYGL RDEGACRLQG SRYDGQAAVF
GWNFQEALAK QKWLIVGAGA IGCELLKNFA MMGVACGKEG CLIITDMDNI ELSNLNRQFL
FRRSDVGAKK AEVAGKVAKT FNSQLNVVAM CERVGTGTEN IFDDAFFEKL DGVANALDNI
EARTYVDRRC VYYRLPLLDS GTQGPKGSTQ VVYPFLTESY SSSHDPPEKS IPICTLRNFP
NTIEHTIQWA RDLFEGAFSI PAELANQFLD DPRGFFDRID KMHDSQKLEL LENVYHYLSD
DRPATVEACV RWARLQFEQH FNFQIQQLLY SFPEDQLTAF GTKFWSGSKR CPHAIYFDSS
NPEHRQFIFA SAFLRAQMYA MKPIDDMDKV VELASEVKPP PFKPKIGLKI PTTDEEAAEL
AGATSDDDSR FQDLQLMLAK LKPDKTSRLV PIDFEKDDDT NHHMEFITAA SNLRAENYKI
EKADFMKTKQ IAGRIIPAIA TTTAAVAGLV GLEFYKIVSS SSKRANLERF KNSFMNLALP
FFGFAEPIRT PVKKFYDKEW TLWDCLELKG EMTLKEFLSY MKEKFNVEVT MLSQGVSMLF
SFFLPLAKQQ QRMNMKVTDL VESITGQKIP SYVNAIVLET MCTDEHGEDI ELPYIKYVFR
SSIKSSD
//