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Database: UniProt
Entry: I7M407_TETTS
LinkDB: I7M407_TETTS
Original site: I7M407_TETTS 
ID   I7M407_TETTS            Unreviewed;      1047 AA.
AC   I7M407;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 2.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=E1 ubiquitin-activating enzyme {ECO:0000256|ARBA:ARBA00012990};
DE            EC=6.2.1.45 {ECO:0000256|ARBA:ARBA00012990};
GN   ORFNames=TTHERM_00241900 {ECO:0000313|EMBL:EAS04669.2};
OS   Tetrahymena thermophila (strain SB210).
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae;
OC   Tetrahymena.
OX   NCBI_TaxID=312017 {ECO:0000313|EMBL:EAS04669.2, ECO:0000313|Proteomes:UP000009168};
RN   [1] {ECO:0000313|Proteomes:UP000009168}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SB210 {ECO:0000313|Proteomes:UP000009168};
RX   PubMed=16933976; DOI=10.1371/journal.pbio.0040286;
RA   Eisen J.A., Coyne R.S., Wu M., Wu D., Thiagarajan M., Wortman J.R.,
RA   Badger J.H., Ren Q., Amedeo P., Jones K.M., Tallon L.J., Delcher A.L.,
RA   Salzberg S.L., Silva J.C., Haas B.J., Majoros W.H., Farzad M.,
RA   Carlton J.M., Smith R.K. Jr., Garg J., Pearlman R.E., Karrer K.M., Sun L.,
RA   Manning G., Elde N.C., Turkewitz A.P., Asai D.J., Wilkes D.E., Wang Y.,
RA   Cai H., Collins K., Stewart B.A., Lee S.R., Wilamowska K., Weinberg Z.,
RA   Ruzzo W.L., Wloga D., Gaertig J., Frankel J., Tsao C.-C., Gorovsky M.A.,
RA   Keeling P.J., Waller R.F., Patron N.J., Cherry J.M., Stover N.A.,
RA   Krieger C.J., del Toro C., Ryder H.F., Williamson S.C., Barbeau R.A.,
RA   Hamilton E.P., Orias E.;
RT   "Macronuclear genome sequence of the ciliate Tetrahymena thermophila, a
RT   model eukaryote.";
RL   PLoS Biol. 4:1620-1642(2006).
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}.
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DR   EMBL; GG662443; EAS04669.2; -; Genomic_DNA.
DR   RefSeq; XP_001024914.2; XM_001024914.2.
DR   AlphaFoldDB; I7M407; -.
DR   STRING; 312017.I7M407; -.
DR   GeneID; 7825316; -.
DR   KEGG; tet:TTHERM_00241900; -.
DR   eggNOG; KOG2012; Eukaryota.
DR   InParanoid; I7M407; -.
DR   OrthoDB; 20494at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000009168; 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   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:UP000009168};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|RuleBase:RU000519}.
FT   DOMAIN          907..1042
FT                   /note="Ubiquitin-activating enzyme E1 C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00985"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..26
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        614
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ   SEQUENCE   1047 AA;  118636 MW;  36EC1BB920CDAED2 CRC64;
     MGCGLSNETK KTKEPTETKK KDNPDENLYS RQMAVYGAET QGKLMKMKVF IYGLQGVGIE
     VAKNLVLAGP SQVVIYDDNI CKSVDQGVNF YIQEKHVKNN STRAEASAEQ LQQLNPYCQV
     TILKGEIDTQ VLSSYNVVVF TDYFNKEKLI EFNNFCREKG IGFIYTANLG LYGCAFVDFG
     QKHKVFDNNG EDPKHSIVVS ITQDKEGLVT THEDKRHGLV DGDHVTFKEV QGMTEVNDQV
     YKVTVKSPFT FTIAQDTSKF KAYQREGIVQ QVKVCEEIQF NSLQQSLNNP IAPGKDCLEM
     CDFEKIGRPE QLHIILNGIF EFCKHNNGQL PQLLNQDHSK QLKEIVHKLL ESNKADASNK
     FKVEEIPDEL IQNVSLYARA HISPVASFWG GVVAQEIVKF TGKFTPLRQW LHHEVFECLP
     DSQVTREVVD SQNGHYVAIF GKEFQESLSK IKLFLVGAGA LGCEYLKMFA LMGMSTGQSG
     LVSVTDDDNI ETSNLNRQFL FRKENVGKSK SETACQVAKN MNNRLNVKSY KLRVAPENEQ
     FFNDDFWVSL DFVVNAVDNV KARLFVDAQC VWFEKPLFES GTLGTKCNSQ IVIPKLTQSY
     GDSADPPEES IPLCTLKNFP HQIEHTIQWA RDYFEGIMVE GPNELSQFIK NPQEYLSKMQ
     RENEGKSGIL RAKLEILQKL AIAFNGGTYQ NCVTLSRELF QEMFTNQIAQ LLHSFPLDHK
     TEEGQPFWSG PKRPPQIIYF DENDEEHINF IQSSANIFAY LFGLKYNTNR EEIKKMAKSV
     HVREFKPGNV KISTNQNDNT QNVAEDDEQI CTKIADELLK LKISSSKKIN TTEFEKDDPT
     NYHIDYVSAI ANLRARNYKI TEVDKFKVKL IAGKIIPALA TTTAMVVGAV GLEIIKYILK
     KPITQIKNSF MNLALPMWLF SEPLPPMKHK DKDYDEILLG PVKAIPPGFT NWDKIDVVGP
     LTVQGLLDYF SQQYQVKLSI ISVAKICIYN SYAGDSERLT QDIAALYEKL NKAPISQFKK
     FLEITASGET LNDGVDVNMP IVKYKYK
//
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