ID A0A1J1HZE5_9DIPT Unreviewed; 1082 AA.
AC A0A1J1HZE5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, 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};
GN ORFNames=CLUMA_CG005537 {ECO:0000313|EMBL:CRK91918.1};
OS Clunio marinus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Chironomoidea; Chironomidae;
OC Clunio.
OX NCBI_TaxID=568069 {ECO:0000313|EMBL:CRK91918.1, ECO:0000313|Proteomes:UP000183832};
RN [1] {ECO:0000313|EMBL:CRK91918.1, ECO:0000313|Proteomes:UP000183832}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Syromyatnikov M.Y., Popov V.N.;
RL Submitted (APR-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}.
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DR EMBL; CVRI01000021; CRK91918.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J1HZE5; -.
DR STRING; 568069.A0A1J1HZE5; -.
DR OrthoDB; 20494at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000183832; Unassembled WGS sequence.
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 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; 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: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; 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:UP000183832};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU000519}.
FT DOMAIN 949..1074
FT /note="Ubiquitin-activating enzyme E1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00985"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 657
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ SEQUENCE 1082 AA; 121991 MW; 5D40DC5C8565A031 CRC64;
MSAVTKNQDF SPAAKKRKLE SEISNNSVST AFGTTQHSNN STSGESQTNN TVNQTQQQQQ
QQQLTNRTMA NGSTKNGEID EGLYSRQLYV LGHEAMKRMA ASDVLISGIG GLGVEIAKNV
ILSGVKSVTL HDQQNSEMKD LSSQFYLSES TIGKNRAEAS CGQLSELNNY VPTLAYTGPL
TEDFLKKFRV VVLTDIDEVE QKRIAEITRK YNIALIIPLT RGLFGQIFCD FGPEFTVYDV
NGASPLSAMI AGITKDKDGV VTCLDEARHG FEDGDYVTFT EVEGMTELNQ CEPIKIKVLG
PYTFSIGNTL EFSDYVRGGI VMQVKMPKII SFKSLSDAER TPEFVMSDWS KFDHPQNINI
AFTALSRFIK KFGRNPRPWN IEDANEFLVI CKERASELNV DELNEKMLEI FAKIADGDLC
PINAVIGGIS AQEVMKACSG KFSPIMQFFS YDAIECLPED LSVLNEAECQ PIGCRYDSQI
AVFGKKFQDK LGSLRYFIVG AGAIGCELLK NFAMMGIGAG KDGELIVTDM DLIERSNLNR
QFLFRPHDVQ APKSRVAAAA VKRMNPYLNV KYHETRVGVD TENVYDDEFF ERLDGVANAL
DNVEARNYMD RRCVYYRLPL LESGTLGTMG NIQVVVPHLT ESYSSSQDPP ERSIPICTLK
NFPNAIEHTL QWARDMFEGV FTQNPQNASQ YINDSGFIER TLKLPGVQPL ETMESVKRAL
LDERPSSFMD CVSWARLHFE ENFSNQIKQL LFNFPRDQQT TSGQPFWSGP KRCPDPIEFN
ADESLHLDYI LTGANLKAEI YGISQIRDPN VVREMVQQVQ VPVFVPRSGI KIAENDAALQ
QQQSDNGSYD QDRVKNIVDE MKNMGRPTFT ITPLEFEKDD DNNLHMDYIV AASNLRALNY
KIQPADRYKS KLIAGKIIPA IATTTSLVSG CVALELYKLA QGFKQLDRFK NGFVNLALPL
CTFSEPSRAK EQQYYDTKWT LWDRFEVEGE MTLSEFLKYF QDKHKLEITM ISQGVCMLYS
FFQPKAKLLE RMSMSMTEVV RRVSKRQIAP HERALVFEIC CNDDEGEDVE VPYVRYTLPR
TN
//
