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Database: UniProt
Entry: S2JGX9_MUCC1
LinkDB: S2JGX9_MUCC1
Original site: S2JGX9_MUCC1 
ID   S2JGX9_MUCC1            Unreviewed;      1007 AA.
AC   S2JGX9;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=E1 ubiquitin-activating enzyme {ECO:0000256|ARBA:ARBA00012990};
DE            EC=6.2.1.45 {ECO:0000256|ARBA:ARBA00012990};
GN   ORFNames=HMPREF1544_05422 {ECO:0000313|EMBL:EPB87762.1};
OS   Mucor circinelloides f. circinelloides (strain 1006PhL) (Mucormycosis
OS   agent) (Calyptromyces circinelloides).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX   NCBI_TaxID=1220926 {ECO:0000313|EMBL:EPB87762.1, ECO:0000313|Proteomes:UP000014254};
RN   [1] {ECO:0000313|Proteomes:UP000014254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1006PhL {ECO:0000313|Proteomes:UP000014254};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., Earl A., Findley K., Lee S.C., Walker B., Young S., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome sequence of Mucor circinelloides f. circinelloides 1006PhL.";
RL   Submitted (MAY-2013) 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}.
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DR   EMBL; KE123962; EPB87762.1; -; Genomic_DNA.
DR   AlphaFoldDB; S2JGX9; -.
DR   STRING; 1220926.S2JGX9; -.
DR   VEuPathDB; FungiDB:HMPREF1544_05422; -.
DR   eggNOG; KOG2012; Eukaryota.
DR   InParanoid; S2JGX9; -.
DR   OMA; GANLHAF; -.
DR   OrthoDB; 20494at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000014254; 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:UP000014254};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|RuleBase:RU000519}.
FT   DOMAIN          876..1001
FT                   /note="Ubiquitin-activating enzyme E1 C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00985"
FT   ACT_SITE        589
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ   SEQUENCE   1007 AA;  112666 MW;  7649AEC70B6AA1EE CRC64;
     MNVDSEQTID EGLYSRQLYV LGHEAMKKMS VAHVLVVGLK GLGVEIAKNV VLAGVKSVTL
     WDPTPAEITD LSAQFYLTEQ DVGQPRAKVT QPKLAELNQY VPVHLLEGEL TEEVLKKYKV
     VVITEMPLSK QLAISEICHA NNIHFISTEV RGLFGRIFND FGSKFEIIDT TGEEPLHGMI
     ANISKEEEGI VTCLDEVRHG LEDGDYVTFK EIQGMTELND ITPRKVKVFG PYSFSIGDTS
     SFGDYTNGGL FTQVKMPKYV DFKSFNESLT KPEFLVSDFA KFDRPMQLHL AFQALSGFVE
     KHGRYPKPRN EQDATEVFEQ TKALVATVDE KPELDEKLIK EVAYQSLGEL SPMVAVFGGL
     AAQEVLKSVS GKFSPIHQYM YFDALEALPT SVALTEELCA PTGSRYDGQI AVFGKTFQEK
     IANTNEFLVG AGAIGCEMLK NWAMMGLGSG PKGHITITDM DTIEKSNLNR QFLFRAGDVG
     KLKSECASAA VSKMNPDLNG KITIHQDRVG PETENIYDDD FFEALDGVTN ALDNVEARKY
     MDRRCVYYRK PLLESGTLGT KGNTQVIIPF LTESYSSSQD PPEKSIPICT LKNFPNAIEH
     TIQWARDLFE GYFKQPADNV NLYLTQPNFI EATLKQGGTS KDTIETVYNC LTTDKPTSFA
     DCVAWARLKF EDLFSNNIRQ LLFNFPPDAV TSTGQRFWSG PKRAPTPLTF DINNRAHLDF
     IIDAANLHAF NYGLKEETSD DYFRKELANV IVPEFKPKEG VKIQVQENET VDNDSGNDSL
     DEVIANLPSP SSVGNFRLHP AEFEKDDDSN HHIDFITAAS NLRAMNYGIT PADRYKTKFI
     AGKIIPAIAT TTAMVTGLVC LELYKIIDGK KDLEQYKNGF VNLALPFFGF SEPIAAPQIE
     YNGIKFTLWD RFDIDKDITL QEFIDYFQNE HKLEVTMVSS GVSMLYSFFM NKKKAAERLN
     MKLSQVVESV SKKPIPAHVK SLIFEICVND ADDEDVDVPY VKVKIRP
//
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