ID M4APV8_XIPMA Unreviewed; 1012 AA.
AC M4APV8;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Ubiquitin-like modifier-activating enzyme 1 {ECO:0000313|Ensembl:ENSXMAP00000016503.1};
OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Xiphophorus.
OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000016503.1, ECO:0000313|Proteomes:UP000002852};
RN [1] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA Walter R., Schartl M., Warren W.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX PubMed=23542700; DOI=10.1038/ng.2604;
RA Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA Postlethwait J.H., Warren W.C.;
RT "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT evolutionary adaptation and several complex traits.";
RL Nat. Genet. 45:567-572(2013).
RN [3] {ECO:0000313|Ensembl:ENSXMAP00000016503.1}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000016503.1};
RG Ensembl;
RL Submitted (NOV-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_014331427.1; XM_014475941.1.
DR AlphaFoldDB; M4APV8; -.
DR STRING; 8083.ENSXMAP00000016503; -.
DR Ensembl; ENSXMAT00000016527.2; ENSXMAP00000016503.1; ENSXMAG00000016439.2.
DR GeneID; 102220506; -.
DR KEGG; xma:102220506; -.
DR CTD; 7318; -.
DR eggNOG; KOG2012; Eukaryota.
DR GeneTree; ENSGT00940000166002; -.
DR HOGENOM; CLU_002556_0_0_1; -.
DR InParanoid; M4APV8; -.
DR OMA; CIREKCN; -.
DR OrthoDB; 20494at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000002852; 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 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:UP000002852};
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; 113038 MW; 0034C3DCCC08EED0 CRC64;
MAETGEIDEG FYSRQLYVLG HEAMRRMGTA EVLIAGMKGL GVEIAKNVIL SGVKSVTVQD
EGQAEWSDLS SQFFLHESDL GQNRAASSIP QLTALNPHVL VSAHTGPLNE DLLQKYQVVV
LTDSSLDDQK RFGEFCHKHG IKLIVADTKG LCGQLFCDFG EQFEVLDRDG EMPASLMIDR
ITKDNPGVVI CADDQKHGLF DGTKVIFSEL QGMTELNSMA PVEIKVCGQY SFSICDTSSF
SNYERGGVVT EVKQPLTLNF KPLSEALNDH QLLILNDYGK ISRHNTLHLA FQALHSFVKK
EQQLPRPWSE SDADLLLKIV KELNSVAKLE ELDEAAVRIF SYTARGDLAP MNAFFGGLAA
QEVIKASSGK FTPLQQWFYF DALECLPEAE GCLQESSFSS KDTRYDSQIV VFGSEFQQKL
LKQKYFMVGA GAIGCELLKN FALIGLGAGE EGLITVTDMD YIERSNLNRQ FLFRSKDIGK
PKSEVAAKAV AEMNPQIKII AHQNRLDPDS EGVYDYNFFM GLDGVAAALD NVEARVYLDK
RCVQHQKPML EGGTLGSKGH TLVVVPHLTE SYGPGKSSSG NAIPLCTLKN FPHRIEHTLQ
WARDQFEGLF KQIPENVNLF LRDPNFIGRT LTHGDAEALE ILGGVCISLQ EMEAGGHRPK
SWEDCVGWAR CKWETLYNND IRQLLHCFPP GELTSNGLPF WSGSKRCPHP LTFDPNNTTH
MEYVVAAANL YGQIYGIKGT RDCAAIKNTL EKVSVPPFSP KSSVKIHLTD KEMEEDRKKV
GDDTDKAQLE ELKGKLSSLK STSQMYPIDF EKDDDNNFHM DYIVAASNLR AENYDIPAAD
RHQSKRIAGR IIPAIATTTA AVAGLMCLEL FKLIQGHKKI DSYRTAYLNL AVQYFVLSQP
CRPQSFTVAG RKYSLWDDFL VEGRRSNQQE MTLADLIQHV KKTNDLTICS LFYGTAILYN
GHEDRLEMSV SDLVKMVTKK EIPPHKKMLE LIPSFDEDED CETVPTIRYM LL
//