ID A0A5A9NVH0_9TELE Unreviewed; 1014 AA.
AC A0A5A9NVH0;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Ubiquitin-like modifier-activating enzyme 1 {ECO:0000313|EMBL:KAA0712771.1};
GN ORFNames=E1301_Tti004928 {ECO:0000313|EMBL:KAA0712771.1};
OS Triplophysa tibetana.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Nemacheilidae; Triplophysa.
OX NCBI_TaxID=1572043 {ECO:0000313|EMBL:KAA0712771.1, ECO:0000313|Proteomes:UP000324632};
RN [1] {ECO:0000313|EMBL:KAA0712771.1, ECO:0000313|Proteomes:UP000324632}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TTIB1903HZAU {ECO:0000313|EMBL:KAA0712771.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:KAA0712771.1};
RX PubMed=30977968;
RA Yang X., Liu H., Ma Z., Zou Y., Zou M., Mao Y., Li X., Wang H., Chen T.,
RA Wang W., Yang R.;
RT "Chromosome-level genome assembly of Triplophysa tibetana, a fish adapted
RT to the harsh high-altitude environment of the Tibetan Plateau.";
RL Mol. Ecol. Resour. 19:1027-1036(2019).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAA0712771.1}.
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DR EMBL; SOYY01000013; KAA0712771.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5A9NVH0; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000324632; Chromosome 13.
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 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; 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; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU000519};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU000519};
KW Reference proteome {ECO:0000313|Proteomes:UP000324632};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU000519}.
FT DOMAIN 883..1009
FT /note="Ubiquitin-activating enzyme E1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00985"
FT COILED 772..799
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 589
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ SEQUENCE 1014 AA; 114254 MW; 67FE6AABF71CD620 CRC64;
MAQTDIDESL YSRQLYVIDH DSMRRMGKAD VLIAGMRGLG VEIAKNVILA GVRSVTIHDE
GVVEWRDLSS QFYLKESDLG QNRALCSEKQ LSSLNVYVRV TAHTEKLNED FLQQFQVVVL
TDSTLDEQLR LGKFCNSNNI KFIVADTRGL CGQLFCDFGD SFEVIDTDGD TPVSAMISQI
SKENPGIVTC TDEDGHEFTD GMFVTFSGIQ GMAELNACEP IEIKVIGKYS FSICDTSGFS
EYERSGVVTE VKQSKIFNFK PLDVAIDEVF RDSELLEMTD YGKTERHLSL HMAFLALHKF
SEEYSRTPIS RSQADAELLV NIAKELSLTK KFSDLDEDVV RKLSMVARGD LAPLNAFIGG
LAAQEVLKAC SVKFTPLRQW LYFDALECLP EDEGFLIEEA CAPRDCRYDG QIAVFGSAFQ
DKLKKQKYFL VGAGAIGCEL LKNFALIGLG AGEGGSITVT DMDSIERSNL NRQFLFGSQD
IGRLKSEAAA ECVRKMNPYM NITAHQNRVA PETEQVYTYS FYSHLDGVAA ALDNVDARVY
LDKCCVRNRK PLLEGGTLGS KGHTMVVVPH LTESYGPSTS GGQKAIPLCT LKNFPHRIEH
TLQWARDQFE GLFKHKAENV NQYLSDPVFV ERTVARGDVE AVEVLEGVYR SLTEEWPQNW
TDCVSWARRW WKTLYNNDIR QLLHCFPPDQ LTSSGLPFWM GAKRCPQPLT FDTSNAPHMD
FIVAAANLYG RIYGIKGSRN HADFQSVLQG VKVPEFIPKS SLKIAVTDEE LKEGHEARKD
EDMMKLEELQ EKLSKLQLSD PNFRMNPQEF EKDDDDNFHM DYIVAASNLR AENYDIPTAD
RHKSKLIAGR IIPAIATTTA AIAGLMCLEL YKLVQGHRQI SSYRNSYINL ATQYFVLSQP
CSAPRFKVAG KDYSIWEDFL LQGRHKGREE MTLEELLKHI KDKYNLTVTE LYYGPAVLYS
DSNHEARLKL SISDLISSVT KTEIPVHEEM LEIIPSFAED EDCLNVPPIR YLLR
//
