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Database: UniProt
Entry: A0A0V0VV91_9BILA
LinkDB: A0A0V0VV91_9BILA
Original site: A0A0V0VV91_9BILA 
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
//
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