ID S9RAN8_SCHOY Unreviewed; 1013 AA.
AC S9RAN8;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Ubiquitin-like 1-activating enzyme E1A {ECO:0000256|ARBA:ARBA00044354};
GN ORFNames=SOCG_01402 {ECO:0000313|EMBL:EPX71184.1};
OS Schizosaccharomyces octosporus (strain yFS286) (Fission yeast)
OS (Octosporomyces octosporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=483514 {ECO:0000313|EMBL:EPX71184.1};
RN [1] {ECO:0000313|EMBL:EPX71184.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YFS286 {ECO:0000313|EMBL:EPX71184.1};
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
RN [2] {ECO:0000313|EMBL:EPX71184.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=YFS286 {ECO:0000313|EMBL:EPX71184.1};
RG The Broad Institute Genome Sequencing Platform;
RA Nusbaum C., Russ C., Rhind N., Niki H., Allshire R., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Birren B.;
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC {ECO:0000256|ARBA:ARBA00004718}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family.
CC {ECO:0000256|ARBA:ARBA00005673, ECO:0000256|RuleBase:RU000519}.
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DR EMBL; KE503208; EPX71184.1; -; Genomic_DNA.
DR RefSeq; XP_013019811.1; XM_013164357.1.
DR AlphaFoldDB; S9RAN8; -.
DR EnsemblFungi; EPX71184; EPX71184; SOCG_01402.
DR GeneID; 25030384; -.
DR VEuPathDB; FungiDB:SOCG_01402; -.
DR eggNOG; KOG2012; Eukaryota.
DR HOGENOM; CLU_002556_0_0_1; -.
DR OMA; GANLHAF; -.
DR OrthoDB; 20494at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000016088; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:EnsemblFungi.
DR GO; GO:0005634; C:nucleus; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProt.
DR GO; GO:0000287; F:magnesium ion binding; IEA:EnsemblFungi.
DR GO; GO:0004839; F:ubiquitin activating enzyme activity; IEA:EnsemblFungi.
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:SF162; SUMO-ACTIVATING ENZYME SUBUNIT 1; 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 Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU000519}.
FT DOMAIN 884..1009
FT /note="Ubiquitin-activating enzyme E1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00985"
FT REGION 773..801
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 594
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ SEQUENCE 1013 AA; 112373 MW; 46356E566DB41B33 CRC64;
MSSKMNIDQT GSGTIDEGLY SRQLYVLGHE AMKQMSQSDV LIIGCKGLGV EIAKNVCLAG
VKSVTLYDPQ PTHIEDLSSQ YFLTEDDLGV ARAEVSVPKL AELNQYVPVS STPQLSIQDL
KKYKCVVVTE TSLSKQLEIN DFTHENGIAF ISADSRGLFG SVFCDFGPEF ICTDVDGNEP
LTGMIANITD DGTVTMLEET RHGLEDGDYV KFAEVKGVPA LNNGQPHKVE VKGPYTFSIG
SIDVLGGSAA TGGIFTQVKM PQKLAFKSLR ESLKEPDYVF PDFGKMLRPP QYHVAFQALS
AFADTHNGAL PRPRNDADAG EFLQLAKKIG TSFDSQLELD EKLLKEVSYQ AKGDLVSMCA
FLGGIVAQEV LKSTTSKFFP FKQFFYFDSL ESLPTSVELS EESCKPRGTR YDGQIAVFGA
EFQQRLSSLN QFLVGAGAIG CEMLKNWSMM GVATGEHGHI HVTDMDSIEK SNLNRQFLFR
PRDVGKLKAE SAANAVAIMN PSLTGKITSY QERVGPESEG IFGDEFFGNL SMVTNALDNV
EARLYVDRRC VFFEKPLLES GTLGTKGNTQ VVVPHLTESY GSSQDPPEKS FPICTLKNFP
NRIEHTIAWA RDLFEGLFKQ PVDNVNLYLS SPNFLETTLK TSSNPREVLE NIRDYLVTDK
PLSFEECIIW ARNQFEKFFN HNIQQLLFNF PKDSVTSNGQ PFWSGPKRAP SPLTFDINNR
AHFDFIVAAA SIYAFNYGLK EETDPALYER VLSSFKPAEY TPKSGVKIQV NDSDEAPEAA
ANSDKQELKS IADSLPPPSS LAGFRLTPAD FEKDDDTNHH IDFITAASNL RALNYEITTA
DRFKTKFVAG KIVPAMCTST AVVSGLVCLE LVKLVDGKKK LEDYKNGFFN LAIGLFTFSD
PIGSPKMKFN EKEVDKIWDR FTLPNFTLQN LIDHFSEKEG LEVTMLSSGV SLLYANFQPP
KKLAERLPLK ISDLVEQISK KKLEPFRKHL ILEVCCDDKD GEDVEVPFIT VKV
//
