ID A0A0V1C2E1_TRISP Unreviewed; 1146 AA.
AC A0A0V1C2E1;
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:KRY43398.1};
GN ORFNames=T01_11711 {ECO:0000313|EMBL:KRY43398.1};
OS Trichinella spiralis (Trichina worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6334 {ECO:0000313|EMBL:KRY43398.1, ECO:0000313|Proteomes:UP000054776};
RN [1] {ECO:0000313|EMBL:KRY43398.1, ECO:0000313|Proteomes:UP000054776}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS3 {ECO:0000313|EMBL:KRY43398.1};
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:KRY43398.1}.
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DR EMBL; JYDH01000001; KRY43398.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1C2E1; -.
DR STRING; 6334.A0A0V1C2E1; -.
DR eggNOG; KOG2012; Eukaryota.
DR InParanoid; A0A0V1C2E1; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000054776; 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:UP000054776};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU000519}.
FT DOMAIN 979..1104
FT /note="Ubiquitin-activating enzyme E1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00985"
FT REGION 47..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..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 1146 AA; 129761 MW; 4077CE7E3AA18411 CRC64;
MENPVQLSSY DCVLQFHLEI LRIQCDFVFR 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 FVLEDMKHNL EDGDYVTFRE
VKGMVELNDC PPRKVKVINT MEFNIGDIST YSEHTEGGKA KTVKVPVKME FVSLNEALLD
PEILVSDHSK LDRPQQMHVI WQGLHMFFEK EGRLPRPQNL ADAEQMLQYC EEINTQLPAK
IKLEKVDARL AKMLSFQAVG NLVAMNGFIG GIAAQEAMKA VTGIFTPIHQ WLYFDSLECL
PETDSAYGLR DEGACRLQGS RYDGQAAVFG WNFQEALAKQ KWLIVGAGAI GCELLKNFAM
MGVACGKDGC LIITDMDNIE LSNLNRQFLF RRSDVGAKKA EVAGKVAKNF 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 GATSDDDSRF QDLQLMLAKL KPEKTSRLVP
IDFEKDDDTN HHMEFITAAS NLRAENYKIE KADFMKTKQI AGRIIPAIAT TTAAVAGLVG
LEFYKIVSSS SKKANLERFK NSFMNLALPF FGFAEPIRTP VKKFYDKEWT LWDCLELKGE
MTLKEFLSYM KEKFNVEVTM LSQGVSMLFS FFLPLAKQQQ RMNMKVTDLV ESITGQKIPS
YVNAIVLETM CTDEHGEDIE LPYIKYVFRS CSKSKAFRFR GSIWKSVYHQ HIYLFIDVVS
KDAPMK
//
