ID A0A6Q2Y6G8_ESOLU Unreviewed; 926 AA.
AC A0A6Q2Y6G8;
DT 02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Ubiquitin like modifier activating enzyme 6 {ECO:0000313|Ensembl:ENSELUP00000061544.1};
GN Name=UBA6 {ECO:0000313|Ensembl:ENSELUP00000061544.1};
OS Esox lucius (Northern pike).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC Esocidae; Esox.
OX NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000061544.1, ECO:0000313|Proteomes:UP000265140};
RN [1] {ECO:0000313|Ensembl:ENSELUP00000061544.1, ECO:0000313|Proteomes:UP000265140}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25069045;
RA Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT "The genome and linkage map of the northern pike (Esox lucius): conserved
RT synteny revealed between the salmonid sister group and the Neoteleostei.";
RL PLoS ONE 9:e102089-e102089(2014).
RN [2] {ECO:0000313|Ensembl:ENSELUP00000061544.1}
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}.
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DR AlphaFoldDB; A0A6Q2Y6G8; -.
DR Ensembl; ENSELUT00000073212.1; ENSELUP00000061544.1; ENSELUG00000007992.2.
DR GeneTree; ENSGT00940000158826; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000265140; LG25.
DR Bgee; ENSELUG00000007992; Expressed in liver and 15 other cell types or tissues.
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 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; 2.
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; IPR000011; UBQ/SUMO-activ_enz_E1-like.
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; 1.
DR Pfam; PF10585; UBA_E1_SCCH; 2.
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:UP000265140}.
FT DOMAIN 787..909
FT /note="Ubiquitin-activating enzyme E1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00985"
FT REGION 897..926
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 926 AA; 104142 MW; EF6D11828EE28336 CRC64;
MAADSMEIDD SLYSRQRYVL GDSAMQQMAQ SSVFLSGMAG LGVEIVTLHD TKQCETKDLG
CNFFIRQDDV LNHRKRVEAV HPRVAELNPY VHVDSSSFPL DLSTDLNFLR RYQLKQTEIY
VGLKPLNRRI ICTLQFIGCD TYGICARVFC DFGEHFEVSD PTGEEAKEIF IQNITLDDPG
VVTCMDGRTH GLQTGQSILF REVNGMDQLN GTARQVTVLS PYSFAIGDTS GLQPYAHGGF
FLLVKTPRTY SFETMEHQLC EPKVLTPDFS KPEAPVQIHA AMLALDDFQE EHNRFSYSLT
HCQTAQGSLP PLAAAVGGMA SQEVLKALTG KFAPLQQWFY LDAIEVVKPL QSLSAEEFIP
RGDRYDGLRA CIGESMCLEL HKLRVFMVGC GAIGCEMLKN LALLGVGLAQ NSGQVCMSDP
DLIEKSNLNR QFLFRPHHIQ HNPQPSFLYI IDAHLNKVCP ATESIYNDLF YSRLHLVVTA
LDNVEARRYV DSRSVSNQKA LLDSGTMGTK GHTEVIVPNL TESYNSHRDP PEEEIPFCTL
KSFPAIIEHT IQWARDKFES AFAHKPSIYN MFWETHSSAE SVLQRMQRRE SLEGAFQVVK
LLSRRPSQWE HCITMARLKF DKYFKRKALQ LLHSFPLDTR LKDGSLFWQS PKRPPSPIEF
DLTDRIETDE NVKKPDQMKL SVSSEEEREA IAQLEEAIAA DHVTPERLRM SPLIFEKDDD
ANGHMDFVAA ASSLRARMYA IEVADRLKTK RIAGKIIPAI ATATAAVAGL VSLELVKVAG
GYGFESFNNC FFNLAIPVVV LTEAAPVRKT QIREDISFSI WDRWVVCGHQ DFTLSNFINA
VREQYGIEPT MVVHGVKMLY VPVMPGHNKR LKLTMQKLIK PAVDRRYVDL TVSFAPESDG
DEDLPGPPVR YYFTRDGDAP PDSLGL
//
