ID A0A087YF91_POEFO Unreviewed; 1012 AA.
AC A0A087YF91;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 2.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Ubiquitin-like modifier-activating enzyme 1 {ECO:0000313|Ensembl:ENSPFOP00000016694.2};
OS Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000016694.2, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000016694.2}
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 EMBL; AYCK01000412; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_007550981.1; XM_007550919.2.
DR RefSeq; XP_016526565.1; XM_016671079.1.
DR AlphaFoldDB; A0A087YF91; -.
DR STRING; 48698.ENSPFOP00000016694; -.
DR Ensembl; ENSPFOT00000016716.2; ENSPFOP00000016694.2; ENSPFOG00000016531.2.
DR GeneID; 103137255; -.
DR KEGG; pfor:103137255; -.
DR CTD; 7318; -.
DR eggNOG; KOG2012; Eukaryota.
DR GeneTree; ENSGT00940000166002; -.
DR OMA; CIREKCN; -.
DR OrthoDB; 20494at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000028760; Unassembled WGS sequence.
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 Reference proteome {ECO:0000313|Proteomes:UP000028760};
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; 112909 MW; 850646828693D331 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 EVKQPLTLNF 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
IEYVVAAANL YGQIYGIEGT RDCAAIKNTL ERVSVPPFSP KSSVKIHLTD KEMEEDRKKE
GDDTDKAQLE ELKGKLSSLK SAAQMYPIDF EKDDDSNFHM DYIVAASNLR AENYDIPAAD
RHQSKRIAGR IIPAIATTTA AVAGLMCLEL FKLIQGHKKI ESYRTAYLNL AVQYFVLSQP
CRPQSFTVAG KKYTLWDDFL VEGRRCNQQE MTLADLIQHV KETNGLTICS IFYGTAILYN
GHKDRLKMSV SDLVKMVTKK EIPPHKKMLE LIPSFDEDED CETVPTIRYM LL
//
