ID   A0A3Q4BJM1_MOLML        Unreviewed;       970 AA.
AC   A0A3Q4BJM1;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=E1 ubiquitin-activating enzyme {ECO:0000256|ARBA:ARBA00012990};
DE            EC=6.2.1.45 {ECO:0000256|ARBA:ARBA00012990};
DE   AltName: Full=Ubiquitin-activating enzyme E1 {ECO:0000256|ARBA:ARBA00030371};
OS   Mola mola (Ocean sunfish) (Tetraodon mola).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Molidae; Mola.
OX   NCBI_TaxID=94237 {ECO:0000313|Ensembl:ENSMMOP00000020172.1, ECO:0000313|Proteomes:UP000261620};
RN   [1] {ECO:0000313|Ensembl:ENSMMOP00000020172.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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   AlphaFoldDB; A0A3Q4BJM1; -.
DR   Ensembl; ENSMMOT00000020506.1; ENSMMOP00000020172.1; ENSMMOG00000015317.1.
DR   OMA; CIREKCN; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000261620; Unplaced.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004839; F:ubiquitin activating enzyme activity; IEA:UniProtKB-EC.
DR   CDD; cd01491; Ube1_repeat1; 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   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; 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; IPR018075; UBQ-activ_enz_E1.
DR   InterPro; IPR018074; UBQ-activ_enz_E1_CS.
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:SF198; E1 UBIQUITIN-ACTIVATING ENZYME; 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   SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 2.
DR   PROSITE; PS00536; UBIQUITIN_ACTIVAT_1; 1.
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:UP000261620};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|RuleBase:RU000519}.
FT   DOMAIN          49..419
FT                   /note="THIF-type NAD/FAD binding fold"
FT                   /evidence="ECO:0000259|Pfam:PF00899"
FT   DOMAIN          222..291
FT                   /note="Ubiquitin-activating enzyme E1 FCCH"
FT                   /evidence="ECO:0000259|Pfam:PF16190"
FT   DOMAIN          292..362
FT                   /note="Ubiquitin-activating enzyme E1 four-helix bundle"
FT                   /evidence="ECO:0000259|Pfam:PF16191"
FT   DOMAIN          442..938
FT                   /note="THIF-type NAD/FAD binding fold"
FT                   /evidence="ECO:0000259|Pfam:PF00899"
FT   DOMAIN          629..882
FT                   /note="Ubiquitin-activating enzyme SCCH"
FT                   /evidence="ECO:0000259|Pfam:PF10585"
FT   ACT_SITE        623
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ   SEQUENCE   970 AA;  108334 MW;  EC7DEE038995B17E CRC64;
     ERKGCFRSDL LGSGVRRGAG TVCSAAPAMR KLSARRNMSG EGDIDEGFYS RQLYVLGHDA
     MRRMAAANVL VAGMRGLGVE IAKNVILAGV KSVTVQDEGR TAWTDLSSQF FLKESHLGQN
     RATCSQQQLC DLNPRVRVSA HTGPLNDDDG LVLFQVVVLT DSSLDDQKRF GDFCHLRGIQ
     FIVADTKGLC GQLFCDFGEE FEVWDRDGET PETAIVQSIS KDNPGVVICL NEGSLRFSEG
     SKVSFSEVQG MTELNSLGPV EMKVHGPYSF SIGDTSAFSQ YERGGIVTEV KQPLKMNFKP
     LSKALPDHQL LKMSDFGKIP RHNTLHLAFQ ALHGFVKTER RLPLPRSQAD ADALLSAVRE
     LNTVAQLEQL DEAAVRNLAF TARGDLAPMN AFIGGLAAQE VIKACSGKFT PLQQWLYFDA
     LECLPEEEDQ LAEHCFSRET RYDGQIAVFG SAFQEKLERQ RYFLVGAGAI GCELLKNFAL
     IGLGAGDEGH VTVTDMDFIE KSNLNRQFLF RTQDIRKPKS VIAAKAVLEM NPRMNITAHQ
     NRVDPDSEGA YDYDFYMSLH GVAAALDNVP ARVYLDGRCV QHQKPMLEGG TQGSRGHTLV
     VVPHLTESYG RDTSHSNDAI PLCTLKNFPH RIEHTLQWAR DHFEGEFKQT PENLNLFLRD
     EGFVERTLRR GDAEALEVLE EIWGNLVDIT AEGKRPTSWK DCVTWARCKW ETVYNSDIRQ
     LLHCFPPDQM TTSGLHFWSG SKKCPHPLTF DPNSTTHMDY VVAAANLYGQ IFGISGTRDP
     VSIRQILEEV HVPSFTPKSS VKIHVTDLEM EEEKEKDCDD ARLAELKEKL ASLSLKGSAK
     QMYPINFEKD EDSNFHMDYI VAASNLRAEN YDIPAADRHQ SKRIAGKIIP AIATTTAAVA
     GLMCLELYKL VQGHQKISSY RVSYFLLSVD HFVWSQPRNA QQKDRSLYSK ARVVLRPNPA
     ERLRLFLPDL
//