ID   A0A665UML6_ECHNA        Unreviewed;      1045 AA.
AC   A0A665UML6;
DT   17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Ubiquitin-like modifier activating enzyme 1 {ECO:0000313|Ensembl:ENSENLP00000020948.1};
OS   Echeneis naucrates (Live sharksucker).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Carangiformes; Echeneidae; Echeneis.
OX   NCBI_TaxID=173247 {ECO:0000313|Ensembl:ENSENLP00000020948.1, ECO:0000313|Proteomes:UP000472264};
RN   [1] {ECO:0000313|Ensembl:ENSENLP00000020948.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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; A0A665UML6; -.
DR   Ensembl; ENSENLT00000021683.1; ENSENLP00000020948.1; ENSENLG00000008059.1.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000472264; Unplaced.
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; 1.10.10.2660; Ubiquitin-activating enzyme E1, SCCH domain; 2.
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; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR   PANTHER; PTHR10953:SF195; UBIQUITIN-LIKE MODIFIER-ACTIVATING ENZYME 1; 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:UP000472264};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|RuleBase:RU000519}.
FT   DOMAIN          909..1040
FT                   /note="Ubiquitin-activating enzyme E1 C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00985"
FT   ACT_SITE        591
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ   SEQUENCE   1045 AA;  116839 MW;  2C6E8EFE71CAF916 CRC64;
     MAKNGNDAEI DEGLYSRQLY VLGHDAMKRL QNSNVLISGM KGLGVEIAKN VILGGVRSVT
     VHDQGVAEWR DLSSQFYIRE EDLGKNRAEV SQPRLAELNN YVPVTAYTGA LTEDYLTKFQ
     VVVLTNSTLD EQLHVGEFCH SRGIKLIVAD TRGLFGQLFC DFEEMMVYDT NGEQPLSAMI
     SMITKDNPGV VTCLDEARHG LESGDYVTFT EVQGMTELNG CQPVEIKVLG PYTFSICDTA
     GFTDYVRGGI VSQVKMAKKI TFKSLSSSMA EPEFQMTDFA KLERPGQLHV GFQAIHAFQK
     KHNHLPAPWN QADADELLTL AKEVNSAQTG SAKVEQLDEA LIKKMAYVSA GDLAPVNAFI
     GGLAAQEVMK ACTGKFMPIM QWLYFDALEC LSEDEGEMLT EEECAPRNSR YDGQIAVFGT
     KLQDMLAKQR YFLVGAGAIG CELLKNFAMI GLASGEGEVI VTDMDTIEKS NLNRQFLFRP
     SDVTKMKSDT AAAAVKQMNP SIRITGHQNR VGPDTERIYD DDFFESLDGV ANALDNVDAR
     MYMDRRCVYY RKPLLESGTL GTKGNVQVVI PFLTESYSSS QDPPEKSIPI CTLKNFPNAI
     EHTLQGWATD EQFCIDPKFM ERTLKLPGAQ PVEVLDAVFK SLVTDCPHSW ADCVAWARNH
     WQCQYNNNIR QLLHNFPPDQ LTSSGAPFWS GPKRCPHPLE FSTSNDLHMD YIVAAANLFA
     QTYGLQGSTD RAGVVKILQE VKVPPFTPRS GVKIHVSDQE LQNSNSSVGK GQISAWQQAA
     VFVTHIFSQR LVHVNYSLLM VASTFIFYVD DSRLEELKAQ LPSPESSQFK LTSIDFEKDD
     DTNFHMDFIV AASNLRAENY DIPPTDRHKS KLIAGKIIPA IATTTAAVVG LVCLELIKIV
     QSHKKLESYK NGFMNLALPF FAFSEPIAAP KHKYYEIDWT LWDRFEVTGL QSNGEEMTLR
     QFLDYFKNEH KLEITMLSQG VSMLYSFFMP AAKLKERLDL PMTEIVTKVS KKKLGKHVKA
     LVFELCCNDL SDEDVEVPYV RYTIR
//