ID A0A3B3UV51_9TELE Unreviewed; 1012 AA.
AC A0A3B3UV51;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Ubiquitin-like modifier-activating enzyme 1 {ECO:0000313|Ensembl:ENSPLAP00000016551.1};
OS Poecilia latipinna (sailfin molly).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48699 {ECO:0000313|Ensembl:ENSPLAP00000016551.1, ECO:0000313|Proteomes:UP000261500};
RN [1] {ECO:0000313|Ensembl:ENSPLAP00000016551.1}
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 RefSeq; XP_014891188.1; XM_015035702.1.
DR RefSeq; XP_014891189.1; XM_015035703.1.
DR AlphaFoldDB; A0A3B3UV51; -.
DR STRING; 48699.ENSPLAP00000016551; -.
DR Ensembl; ENSPLAT00000025542.1; ENSPLAP00000016551.1; ENSPLAG00000020720.1.
DR GeneID; 106949458; -.
DR KEGG; plai:106949458; -.
DR CTD; 7318; -.
DR GeneTree; ENSGT00940000166002; -.
DR OrthoDB; 20494at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000261500; 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: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 Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU000519};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU000519};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU000519}.
FT DOMAIN 883..1007
FT /note="Ubiquitin-activating enzyme E1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00985"
FT ACT_SITE 586
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ SEQUENCE 1012 AA; 112957 MW; 349CE342EBB4747F CRC64;
MAETGAIDEG FYSRQLYVLG HEAMRRMATA EVLIAGMKGL GVEIAKNVIL SGVKSVTVQD
EGQADWSDLS SQFFLHESDL GQNRATSSIP QLTALNPHVF VSAHTGPLNE DLLLNYQVVV
LTDSSLDDQK RFGEFCHKHG IKFIVVDTKG LCGQLFCDFG DQFEVLDRDG EMPASLMIDR
ITKDNPGVVI CADDQKHGLF DGTKVTFSEV QGMTELNSMA PVEIKVCGPY SFSICDTSSF
SSHERGGVVT EVKQPLMLNF KPLSKALKDH QPLILNDYGK ISRHNTLHLA FQALHRFVKK
EQRLPHPWSQ SDADLLLGIV NELNSVAELD ELDEAAVRIF SYTARGDLAP MNAFFGGLAA
QEVIKASSGK FTPLQQWFYF DALECLPEDG GCLQESSFLS KGTRYDAQIV VFGSEFQQKL
LNQKYFMVGA GAIGCELLKN FALIGIGAGE KGRITVTDMD YIERSNLNRQ FLFRSKDIGK
PKSEVAAKAV AEMNPQIKIT AHQNRLDPDS EGVYDYSFFM GLDGVAAALD NVEARVYLDK
RCVQHQKPML EGGTLGSKGH TLVVVPHLTE SYGPGKSSSG NAIPLCTLKN FPHRIEHTLQ
WARDQFEGLF KQTPENVNLF LRDPNFIERT LTHGDAEALE ILGGVCISLQ EMEAGGHRPK
SWEDCVGWAR RKWETQYNNE IRQLLHCFPP GELTSNGLPF WSGSKRCPHP LTFDPNNTTH
MEYVVAAANL YGQIYGIEGT RDCAAIKNTL ERVSVPPFSP KSSVKIHLTD KEMEEDRKKE
GDDTDKAQLE ELKGKLSSLK SAAQMYPIDF EKDDDSNFHM DYIVAASNLR AENYDIPAAD
RHQSKRIAGR IIPAIATTTA AVAGLMCLEL FKLIQGHKKI ESYRTAYLNL AVQYFVLSQP
CRPQSFTVAG KKYTLWDDFL VEGRRCNQQE MTLADLIQHV KETNGLTICS LFYGTAILYN
GHKDRLKMSV SDLVKMVTKK EIPPHKKMLE LIPSFDEDED CETVPTIRYM LL
//
