ID A0A1R2BTD5_9CILI Unreviewed; 1017 AA.
AC A0A1R2BTD5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=E1 ubiquitin-activating enzyme {ECO:0000256|ARBA:ARBA00012990};
DE EC=6.2.1.45 {ECO:0000256|ARBA:ARBA00012990};
GN ORFNames=SteCoe_19844 {ECO:0000313|EMBL:OMJ80020.1};
OS Stentor coeruleus.
OC Eukaryota; Sar; Alveolata; Ciliophora; Postciliodesmatophora;
OC Heterotrichea; Heterotrichida; Stentoridae; Stentor.
OX NCBI_TaxID=5963 {ECO:0000313|EMBL:OMJ80020.1, ECO:0000313|Proteomes:UP000187209};
RN [1] {ECO:0000313|EMBL:OMJ80020.1, ECO:0000313|Proteomes:UP000187209}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WM001 {ECO:0000313|EMBL:OMJ80020.1};
RA Slabodnick M., Ruby J.G., Reiff S.B., Swart E.C., Gosai S., Prabakaran S.,
RA Witkowska E., Larue G.E., Fisher S., Freeman R.M., Gunawardena J., Chu W.,
RA Stover N.A., Gregory B.D., Nowacki M., Derisi J., Roy S.W., Marshall W.F.,
RA Sood P.;
RT "The macronuclear genome of Stentor coeruleus: a giant cell with tiny
RT introns.";
RL Submitted (NOV-2016) 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:OMJ80020.1}.
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DR EMBL; MPUH01000443; OMJ80020.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R2BTD5; -.
DR OrthoDB; 20494at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000187209; 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:UP000187209};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU000519}.
FT DOMAIN 874..1013
FT /note="Ubiquitin-activating enzyme E1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00985"
FT ACT_SITE 585
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ SEQUENCE 1017 AA; 113977 MW; E3840618D631BCF1 CRC64;
MADIDTNLYS RQIGTFGMEM MGKLIKLDVL IHGLRGVGVE TAKNLILAGP HSVTIVDNSI
VEARDLGSNF YLTPENVGNT TRGKASLDKL QELNPHVRVS LHEGPLDEAF LSHFHVVFLS
ETDLDSLIRF NNFCRNHEPA IKFLSCEVFG AAGYGFVDFG NDFICFDKDG ENNRSFIISN
ITNGNPGIVM VHEEKRHTYQ DGDYVVFKEV QGMTEINGLE PMPVKFVSPF SFSIGDTSSF
GSYTREGIVE QVKVPTKFEF KSFAETLKNP AVKEPLMVSD LGKFGRPEQL HFAQWAVREF
QKIHHYLPEL LNQGHANEVV EIAKALNEAG KESFSVDAID EDVVRKVALY ARSQVSPIAS
FWGGIMAQEI VKATGKYTPL QQWLHIDFFE IVPDNADRTL HNNRYDDQIA LIGNEIHNKL
AASYSFLVGA GALGCEFLKL YALMGVSSNG GQVVVTDDDS IEVSNLNRQF LFRRTDVGHS
KSERATLAAK KMNPELNVLA RQDRVSPENE TIFDDTFWNS RNFVTNAVDN VNARLYVDGR
CVWYEKPLLE SGTLGTKANV QVCLPHKTQS YGDSQDPPEE SIPMCTLKNF PHAIEHCIEW
AKDEFQGTFS DGPQEVNKYF DDPIRYLASL GSSGNSTVQK DKLEKIKIFI ALMKHANFEE
CVHVAREMLQ DSFYNTISQL LHNFPADYAT KDGTPFWSGP KRAPTPCVFD ANDDTHLNYI
ISAANLMASV LGVPQNRNPE QVRNIVRNIQ VKPFVPRVVA IQTEENQTVQ GADDEQILSA
LLQEMKVVDR EVAHKRLTPA VFEKDDDTNF HIDFITHAAN LRARNYKINE ADRQKTKMIA
GKIIPAIATT TAMIAGAVAV ELYKLHIHAD IEKFRNIFVN LGVNIIVMSE PQPPMRTKSK
DYDPIVMGPI KAYPEGFSTW EKLHVTGPCT LGEFNQKILS EHKLKVNIVS CGKTCLYNGY
LPKNKHGDRL AKLLHVLYEE ISGTKIIPGR RYLAVEVSCE GNEDGSDYAV PVIKYTF
//