ID A0A0V0SP32_9BILA Unreviewed; 1112 AA.
AC A0A0V0SP32;
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:KRX28231.1};
GN ORFNames=T07_8111 {ECO:0000313|EMBL:KRX28231.1};
OS Trichinella nelsoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6336 {ECO:0000313|EMBL:KRX28231.1, ECO:0000313|Proteomes:UP000054630};
RN [1] {ECO:0000313|EMBL:KRX28231.1, ECO:0000313|Proteomes:UP000054630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS37 {ECO:0000313|EMBL:KRX28231.1};
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:KRX28231.1}.
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DR EMBL; JYDL01000001; KRX28231.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0SP32; -.
DR STRING; 6336.A0A0V0SP32; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000054630; 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:UP000054630};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU000519}.
FT DOMAIN 975..1100
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 1112 AA; 125467 MW; B52214D38506247F CRC64;
MSLCEESTKN LNSNQVDPNN PSPPSKRSKI DSIDCSTGDK IQKSRTDMVE GSDSRNSENS
FNTDMANGRS KLGSFDPQLY SRQLYALGEV AMRRLRISTV LISGIGGVGV EIAKNLILGG
IRHVTIHDTK TTTWLDLSAQ YYLNEQCLGK NRAVESWPHL EELNDSVTVG CITEELNEDL
LVIITEATLA EQKQINLWTR KYGKKFIAAD CRGLFGVLFN DFGPNHIIDD SNGEPCTEVI
INHIDRETGN VFVLEDMKHN LEDGDYVTFR EVKGMVELND CPPRKVKVIN TMEFNIGDIS
TYSEHTEGGK AKTVKVPVKM EFVSLNEALL DPEILVSDHS KMDRPPQMHV IWQGLHMFFE
KEGRLPRPQN LADAEQMLQY CEEINTQLPE KIKLEKVDAR LAKMLSFQAV GNLVAMNGFI
GGIAAQEAMK AVTGIFTPIH QWLYFDSLEC LPETDSAYGL RDEGACRLQG SRYDGQAAVF
GWNFQEALAK QKWLIVGAGA IGCELLKNFA MMGVACGKEG CLIITDMDNI ELSNLNRQFL
FRRSDVGAKK AEVAGKAAKT FNSHLNVVAM 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
AGATSGEYLC FLNTTTAPCK DYPCFFCIVS DDDSRFQDLQ LMLAKLKPEK TSRLVPIDFE
KDDDTNHHME FITAASNLRA ENYKIEKADF MKTKQIAGRI IPAIATTTAA VAGLVGLEFY
KIVSSSSKKA NLERFKNSFM NLALPFFGFA EPIRTPVKKY YDKEWTLWDC LELKGEMTLK
EFLSYMKEKF NVEVTMLSQG VSMLFSFFLP LAKQQQRMNM KVTDLVESIT GQKIPSYVNA
IVLETMCTDE HGEDIELPYI KYVFRSSSKS SD
//
