ID A0A0L0DMQ1_THETB Unreviewed; 1150 AA.
AC A0A0L0DMQ1;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=E1 ubiquitin-activating enzyme {ECO:0000256|ARBA:ARBA00012990};
DE EC=6.2.1.45 {ECO:0000256|ARBA:ARBA00012990};
GN ORFNames=AMSG_01266 {ECO:0000313|EMBL:KNC53555.1};
OS Thecamonas trahens ATCC 50062.
OC Eukaryota; Apusozoa; Apusomonadida; Apusomonadidae; Thecamonas.
OX NCBI_TaxID=461836 {ECO:0000313|EMBL:KNC53555.1, ECO:0000313|Proteomes:UP000054408};
RN [1] {ECO:0000313|EMBL:KNC53555.1, ECO:0000313|Proteomes:UP000054408}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50062 {ECO:0000313|EMBL:KNC53555.1,
RC ECO:0000313|Proteomes:UP000054408};
RG The Broad Institute Genome Sequencing Platform;
RA Russ C., Cuomo C., Shea T., Young S.K., Zeng Q., Koehrsen M., Haas B.,
RA Borodovsky M., Guigo R., Alvarado L., Berlin A., Bochicchio J.,
RA Borenstein D., Chapman S., Chen Z., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D.,
RA Larson L., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J., Yandava C.,
RA Burger G., Gray M.W., Holland P.W.H., King N., Lang F.B.F., Roger A.J.,
RA Ruiz-Trillo I., Lander E., Nusbaum C.;
RT "The Genome Sequence of Thecamonas trahens ATCC 50062.";
RL Submitted (MAY-2010) 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}.
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DR EMBL; GL349437; KNC53555.1; -; Genomic_DNA.
DR RefSeq; XP_013761874.1; XM_013906420.1.
DR AlphaFoldDB; A0A0L0DMQ1; -.
DR STRING; 461836.A0A0L0DMQ1; -.
DR EnsemblProtists; KNC53555; KNC53555; AMSG_01266.
DR GeneID; 25561022; -.
DR eggNOG; KOG2012; Eukaryota.
DR OMA; RACIGDP; -.
DR OrthoDB; 20494at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000054408; Unassembled WGS sequence.
DR GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
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 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; IPR019572; UBA_E1_SCCH.
DR InterPro; IPR042063; Ubi_acti_E1_SCCH.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR InterPro; IPR000011; UBQ/SUMO-activ_enz_E1-like.
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; 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.
PE 3: Inferred from homology;
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Reference proteome {ECO:0000313|Proteomes:UP000054408}.
FT DOMAIN 981..1125
FT /note="Ubiquitin-activating enzyme E1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00985"
SQ SEQUENCE 1150 AA; 123218 MW; FC495FF7F38EB3AE CRC64;
MSAAAASASN AGASNAGGNV EIDEDLQSRQ LAVYGREAMM RLAKSKVLIT GMDGLGAEIA
KNVILANVGS VTLHDTAEVA IADLGAHFYL KEEDVGKNRA EACLGELQEL NPSVMTVASQ
RDLEPKFLAE FQIVVCVSTP LAEACRINEY CRSARPPIAF VYTSAYGLAG AAFSDFGPDF
PVFDWSGEAK KSAIVAKISQ ANPAVVTCVF DKNDPHSRHD LAEGEVVEFA EVKGMTELNG
NAYTVKEVIN PWMFSIEVDT TGFGEYFDGG LVTEKRMPRF IPFRSLRETL HSPGEFLVSD
WGKWGRPALL HLALQALDAY RTEHGGAYPA PGDAAAGDAV VAAATELNAA KLADLDAEAA
RLEAQSKALG AALDAMDAAA LGLDVEGSPE AAAGLSAART EVEAQLKAVR DRQGAMGWER
IDEVDEATLR SVASGSSAVL NAMAAFLGGL VGQEVVKAGT SKYMPLNQWY HFDALESLPA
EAVDPASLAP RGSRYDAMTA VYGAELVEKI RNLKYFLVGS GALGCEYLKN FALTGVGTGP
DGEVIVTDDD VIERSNLSRQ FLFRNWHVKK SKSLSASEAA MAMNPEFKVK ALQERVSPDT
ENIFNDAFWS SLSGVCNALD NIKARLYVDE RCVFYGKSLL ESGTLGPKCN TQVVVPHLTE
NYGASRDPPE REAPQCTIHN FPHTIEHCLV WAKSEFTGLF ETSPAEAQKV LDLGSVDAYV
ETMQASGAGI GDILNNLRGD ETWGGGVTDM LNDVPASYDD CVKWARHKWQ IYASNMIRLL
IHVFPEDMLT SEGGRFWTAP KRFPTPLEFD LADDMTFQFL RAASLLRAST FGINKPASVT
RETIAAALAS YSEPAFDPAA LGDVKIESDP NAEAGAAEGT DDDISTVVAA IAPIPEVKAK
TTTLYPEVFE KDDDTNHHIA FIQALGCLRA RAYAIAEVDM LKAKLLAGNI IPAIATATAM
AAGCCMFELV KLAQGLPVDA YRNSFFNLGV MAFSAADPMP PAKITSRQET IKPDPENYPD
YEEERDIIAF PDPHTAWDAV VIDIGAAGTV ADVLAYFDSH NLSVMSIAVN GGLIYRAGAS
GDAVKGNVFV DHVAEKVGAD ASRGFVVIEP LCEGADMQEI EFPPLVLVKV SDGYALSRTA
TTSMGKPVDA
//
