ID A0A665UPQ3_ECHNA Unreviewed; 1089 AA.
AC A0A665UPQ3;
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:ENSENLP00000021698.1};
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:ENSENLP00000021698.1, ECO:0000313|Proteomes:UP000472264};
RN [1] {ECO:0000313|Ensembl:ENSENLP00000021698.1}
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; A0A665UPQ3; -.
DR Ensembl; ENSENLT00000022448.1; ENSENLP00000021698.1; ENSENLG00000008059.1.
DR InParanoid; A0A665UPQ3; -.
DR OMA; GANLHAF; -.
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; 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; 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 953..1084
FT /note="Ubiquitin-activating enzyme E1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00985"
FT REGION 36..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 664
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ SEQUENCE 1089 AA; 121795 MW; 3CD8B482A6EA795C CRC64;
QHYPCPHLPV TVFCLSYRSE LLMIQLFFRN NVSMSSSPLS KKRRLSGSET KTGSHCSSSN
SVRTDLSHTP ANGMAKNGND AEIDEGLYSR QLYVLGHDAM KRLQNSNVLI SGMKGLGVEI
AKNVILGGVR SVTVHDQGVA EWRDLSSQFY IREEDLGKNR AEVSQPRLAE LNNYVPVTAY
TGALTEDYLT KFQVVVLTNS TLDEQLHVGE FCHSRGIKLI VADTRGLFGQ LFCDFEEMMV
YDTNGEQPLS AMISMITKDN PGVVTCLDEA RHGLESGDYV TFTEVQGMTE LNGCQPVEIK
VLGPYTFSIC DTAGFTDYVR GGIVSQVKMA KKITFKSLSS SMAEPEFQMT DFAKLERPGQ
LHVGFQAIHA FQKKHNHLPA PWNQADADEL LTLAKEVNSA QTGSAKVEQL DEALIKKMAY
VSAGDLAPVN AFIGGLAAQE VMKACTGKFM PIMQWLYFDA LECLSEDEGE MLTEEECAPR
NSRYDGQIAV FGTKLQDMLA KQRYFLVGAG AIGCELLKNF AMIGLASGEG EVIVTDMDTI
EKSNLNRQFL FRPSDVTKMK SDTAAAAVKQ MNPSIRITGH QNRVGPDTER IYDDDFFESL
DGVANALDNV DARMYMDRRC VYYRKPLLES GTLGTKGNVQ VVIPFLTESY SSSQDPPEKS
IPICTLKNFP NAIEHTLQWA RDEFEGLFKQ PPENAMQYLT DPKFMERTLK LPGAQPVEVL
DAVFKSLVTD CPHSWADCVA WARNHWQCQY NNNIRQLLHN FPPDQLTSSG APFWSGPKRC
PHPLEFSTSN DLHMDYIVAA ANLFAQTYGL QGSTDRAGVV KILQEVKVPP FTPRSGVKIH
VSDQELQNSN SSVDDSRLEE LKAQLPSPES SQFKLTSIDF EKDDDTNFHM DFIVAASNLR
AENYDIPPTD RHKSKLIAGK IIPAIATTTA AVVGLVCLEL IKIVQSHKKL ESYKNGFMNL
ALPFFAFSEP IAAPKHKYYE IDWTLWDRFE VTGLQSNGEE MTLRQFLDYF KNEHKLEITM
LSQGVSMLYS FFMPAAKLKE RLDLPMTEIV TKVSKKKLGK HVKALVFELC CNDLSDEDVE
VPYVRYTIR
//
