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Database: UniProt
Entry: A0A2Y9JLN3_ENHLU
LinkDB: A0A2Y9JLN3_ENHLU
Original site: A0A2Y9JLN3_ENHLU 
ID   A0A2Y9JLN3_ENHLU        Unreviewed;       997 AA.
AC   A0A2Y9JLN3;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Ubiquitin-like modifier-activating enzyme 6 isoform X2 {ECO:0000313|RefSeq:XP_022361486.1};
GN   Name=LOC111148946 {ECO:0000313|RefSeq:XP_022361486.1};
OS   Enhydra lutris kenyoni (northern sea otter).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC   Lutrinae; Enhydra.
OX   NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022361486.1};
RN   [1] {ECO:0000313|RefSeq:XP_022361486.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_022361486.1};
RG   RefSeq;
RL   Submitted (NOV-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}.
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DR   RefSeq; XP_022361486.1; XM_022505778.1.
DR   AlphaFoldDB; A0A2Y9JLN3; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000248482; 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; 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; IPR000011; UBQ/SUMO-activ_enz_E1-like.
DR   NCBIfam; TIGR01408; Ube1; 1.
DR   PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR   PANTHER; PTHR10953:SF186; UBIQUITIN-LIKE MODIFIER-ACTIVATING ENZYME 6; 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.
PE   3: Inferred from homology;
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248482}.
FT   DOMAIN          866..988
FT                   /note="Ubiquitin-activating enzyme E1 C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00985"
SQ   SEQUENCE   997 AA;  112135 MW;  0320E779086F75F7 CRC64;
     MQKMAKSRVF LSGMGGLGLE IAKNLVLAGI KALTIHDTEK CQMWDLGTNF FLCEDDVVNR
     RNRAEAVLQH IAELNPYVHV TSSSVPLDET TDLSFLDKYQ CVVLTEIKLP VQKKINNFCH
     SHCPPIKFIS ADMHGVWSRL FCDFGDEFEV SDTTGEEPKE IFISNITQAN PGIVTCLENH
     PHKLETGQFV TFREVNGMMS LNGSTQQITV VSPFSFSIGD TTELEPYLHG GIAVQIKTPK
     TFCFEPLETQ IKHPKCLIAD FSNPEAPLEI HTAMLALDQF QENYNRKPNI GCQKDSEELL
     KLATSISETL EEKPEVNADI VHWLSWTAQG FLPPLAAAVG GVASQEVLKA VTGKFSPLCQ
     WLYIEAADIV ESLGKPEREQ FLPRGDRYDA LRACIGDTLC QKLQKLNIFL VGCGAIGCEM
     LKNFALLGVG TGKEKGMVTV TDPDLIEKSN LNRQFLFRPH HIQKPKSYTA ADATLKINPQ
     LKIDAHLNKV CPATEAIYND EFYTKQDIII TALDNVEARR YVDSRCLANL RPLLDSGTMG
     TKGHTEVIVP HLTESYNSHR DPPEEEIPFC TLKSFPAAIE HTIQWARDKF ESSFSHKPSL
     FNKFWQTYSS AEEVLQKIQT GHSLEGCFQV IKLLSRRPRN WSQCVELARL KFEKYFNHKA
     LQLLHCFPLD TRLKDGSLFW QSPKRPPSPI KFDLNEPLHF SFLLNAAKLY AAVYCIPLTE
     EDLSADALLN ILSEVKIQEF KPSNKVVQTD ETARKPEHVP ISSEDERNAV FQLEKAISSN
     KATSSDLQMA VLSFEKDDDR NGHVDFITAA SNLRAKMYSI EPADRFKTKR IAGKIIPAIA
     TSTAAVSGLV ALEMIKVAGD YPFEAYKNCF LNLAIPIIVF TETSEVKRTE IRNGISFTIW
     DRWTIHGKED FTLLDFINVV KEKYGIEPTM VVQGVKMLYV PVMPGHAKRL KLTMHKLVKP
     STEKKYVDLT VSFAPDTDGD EDLPGPPVRY YFSHDTD
//
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