ID A0A162TRT0_MUCCL Unreviewed; 1010 AA.
AC A0A162TRT0;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=E1 ubiquitin-activating enzyme {ECO:0000256|ARBA:ARBA00012990};
DE EC=6.2.1.45 {ECO:0000256|ARBA:ARBA00012990};
GN ORFNames=MUCCIDRAFT_26195 {ECO:0000313|EMBL:OAD06612.1};
OS Mucor lusitanicus CBS 277.49.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX NCBI_TaxID=747725 {ECO:0000313|EMBL:OAD06612.1, ECO:0000313|Proteomes:UP000077051};
RN [1] {ECO:0000313|EMBL:OAD06612.1, ECO:0000313|Proteomes:UP000077051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 277.49 {ECO:0000313|EMBL:OAD06612.1,
RC ECO:0000313|Proteomes:UP000077051};
RG DOE Joint Genome Institute;
RA Corrochano L.M., Kuo A., Marcet-Houben M., Polaino S., Salamov A.,
RA Villalobos J.M., Alvarez M.I., Avalos J., Benito E.P., Benoit I.,
RA Burger G., Camino L.P., Canovas D., Cerda-Olmedo E., Cheng J.-F.,
RA Dominguez A., Elias M., Eslava A.P., Glaser F., Grimwood J., Gutierrez G.,
RA Heitman J., Henrissat B., Iturriaga E.A., Lang B.F., Lavin J.L., Lee S.,
RA Li W., Lindquist E., Lopez-Garcia S., Luque E.M., Marcos A.T., Martin J.,
RA Mccluskey K., Medina H.R., Miralles-Duran A., Miyazaki A., Munoz-Torres E.,
RA Oguiza J.A., Ohm R., Olmedo M., Orejas M., Ortiz-Castellanos L.,
RA Pisabarro A.G., Rodriguez-Romero J., Ruiz-Herrera J., Ruiz-Vazquez R.,
RA Sanz C., Schackwitz W., Schmutz J., Shahriari M., Shelest E.,
RA Silva-Franco F., Soanes D., Syed K., Tagua V.G., Talbot N.J., Thon M.,
RA De Vries R.P., Wiebenga A., Yadav J.S., Braun E.L., Baker S., Garre V.,
RA Horwitz B., Torres-Martinez S., Idnurm A., Herrera-Estrella A.,
RA Gabaldon T., Grigoriev I.V.;
RT "Expansion of signal transduction pathways in fungi by whole-genome
RT duplication.";
RL Submitted (JUN-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:OAD06612.1}.
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DR EMBL; AMYB01000002; OAD06612.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A162TRT0; -.
DR STRING; 747725.A0A162TRT0; -.
DR VEuPathDB; FungiDB:QYA_26195; -.
DR OrthoDB; 20494at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000077051; 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; cd01491; Ube1_repeat1; 1.
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:UP000077051};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU000519}.
FT DOMAIN 879..1004
FT /note="Ubiquitin-activating enzyme E1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00985"
FT ACT_SITE 592
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ SEQUENCE 1010 AA; 113039 MW; 7DF70803C0B06FDE CRC64;
MSNMNVDSEQ TIDEGLYSRQ LYVLGHEAMK KMSVAHVLVV GLKGLGVEIA KNVVLAGVKS
VTLWDPTPAE ISDLSAQFYL TEQDVGQPRA KVTQPKLAEL NQYVPVHLLE GELTEEVLKK
YKVVVITEMP LSKQLAISEI CHANNIHFIS TEVRGLFGRI FNDFGSKFEV IDTTGEEPLH
GMIANISKEE GIVTCLDEVR HGLEDGDYVT FKEIQGMTEL NDITPRKVKV FGPYSFSIGD
TSSFGDYTNG GLFTQVKMPK YIDFKSFNES LTQPEFLVSD FAKFDRPMQL HLAFQALSGF
VEKHGRYPKP RNEQDATEVF EQTKALVASV DDKPEELDEK LIKEVAYQSL GELSPMVAVF
GGLAAQEVLK SVSGKFSPIH QYMYFDALEA LPTSVPLTEE LCAPTGSRYD GQIAVFGKAF
QEKIANTNEF LVGAGAIGCE MLKNWAMMGL GSGPKGHLTI TDMDTIEKSN LNRQFLFRAG
DVGKLKSECA SAAVSKMNPD LNGKITIHQD RVGPETENIY DDDFFEALDG VTNALDNVEA
RKYMDRRCVY YRKPLLESGT LGTKGNTQVI IPFLTESYSS SQDPPEKSIP ICTLKNFPNA
IEHTIQWARD LFEGYFKQPA DNVNLYLTQP NFIEATLKQG GTSKDTIETV YNCLTTDKPA
SFADCVAWAR FKFEDLFSNN IRQLLFNFPP DAVTSTGQRF WSGPKRAPTP LTFDVDNRAH
LDFIIDAANL HAFNYGLKEE TSDEYFRKEL ANIIVPEFKP KEGVKIQVQE NETVDNDSGN
DSLDEVIANL PSPSSVGNFR LHPAEFEKDD DSNHHIDFIT AASNLRAMNY GITPADRYKT
KFIAGKIIPA IATTTAMVTG LVCLELYKII DGKKDLEQYK NGFVNLALPF FGFSEPIAAP
QIEYNGIKFT LWDRFDIDKD ITLQEFIDYF QNEHKLEVTM VSSGVSMLYS FFMNKKKAAE
RLNMKLSQVV ETVSKKPIPP HVKSLIFEIC VNDADDEDVD VPYVRVKIRP
//
