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Database: UniProt
Entry: B7FYG1_PHATC
LinkDB: B7FYG1_PHATC
Original site: B7FYG1_PHATC 
ID   B7FYG1_PHATC            Unreviewed;      1108 AA.
AC   B7FYG1;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   RecName: Full=E1 ubiquitin-activating enzyme {ECO:0000256|ARBA:ARBA00012990};
DE            EC=6.2.1.45 {ECO:0000256|ARBA:ARBA00012990};
DE   Flags: Fragment;
GN   Name=UBA1 {ECO:0000313|EMBL:EEC48718.1};
GN   ORFNames=PHATRDRAFT_54460 {ECO:0000313|EMBL:EEC48718.1};
OS   Phaeodactylum tricornutum (strain CCAP 1055/1).
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC   Bacillariophyceae; Bacillariophycidae; Naviculales; Phaeodactylaceae;
OC   Phaeodactylum.
OX   NCBI_TaxID=556484 {ECO:0000313|EMBL:EEC48718.1, ECO:0000313|Proteomes:UP000000759};
RN   [1] {ECO:0000313|EMBL:EEC48718.1, ECO:0000313|Proteomes:UP000000759}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCAP 1055/1 {ECO:0000313|EMBL:EEC48718.1,
RC   ECO:0000313|Proteomes:UP000000759};
RX   PubMed=18923393; DOI=10.1038/nature07410;
RA   Bowler C., Allen A.E., Badger J.H., Grimwood J., Jabbari K., Kuo A.,
RA   Maheswari U., Martens C., Maumus F., Otillar R.P., Rayko E., Salamov A.,
RA   Vandepoele K., Beszteri B., Gruber A., Heijde M., Katinka M., Mock T.,
RA   Valentin K., Verret F., Berges J.A., Brownlee C., Cadoret J.P.,
RA   Chiovitti A., Choi C.J., Coesel S., De Martino A., Detter J.C., Durkin C.,
RA   Falciatore A., Fournet J., Haruta M., Huysman M.J., Jenkins B.D.,
RA   Jiroutova K., Jorgensen R.E., Joubert Y., Kaplan A., Kroger N., Kroth P.G.,
RA   La Roche J., Lindquist E., Lommer M., Martin-Jezequel V., Lopez P.J.,
RA   Lucas S., Mangogna M., McGinnis K., Medlin L.K., Montsant A.,
RA   Oudot-Le Secq M.P., Napoli C., Obornik M., Parker M.S., Petit J.L.,
RA   Porcel B.M., Poulsen N., Robison M., Rychlewski L., Rynearson T.A.,
RA   Schmutz J., Shapiro H., Siaut M., Stanley M., Sussman M.R., Taylor A.R.,
RA   Vardi A., von Dassow P., Vyverman W., Willis A., Wyrwicz L.S.,
RA   Rokhsar D.S., Weissenbach J., Armbrust E.V., Green B.R., Van de Peer Y.,
RA   Grigoriev I.V.;
RT   "The Phaeodactylum genome reveals the evolutionary history of diatom
RT   genomes.";
RL   Nature 456:239-244(2008).
RN   [2] {ECO:0000313|Proteomes:UP000000759}
RP   GENOME REANNOTATION.
RC   STRAIN=CCAP 1055/1 {ECO:0000313|Proteomes:UP000000759};
RG   Diatom Consortium;
RA   Grigoriev I., Grimwood J., Kuo A., Otillar R.P., Salamov A., Detter J.C.,
RA   Lindquist E., Shapiro H., Lucas S., Glavina del Rio T., Pitluck S.,
RA   Rokhsar D., Bowler C.;
RL   Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine
CC         = AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-
CC         L-cysteine.; EC=6.2.1.45; Evidence={ECO:0000256|ARBA:ARBA00000488};
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}.
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DR   EMBL; CM000610; EEC48718.1; -; Genomic_DNA.
DR   RefSeq; XP_002179732.1; XM_002179696.1.
DR   AlphaFoldDB; B7FYG1; -.
DR   STRING; 556484.B7FYG1; -.
DR   TCDB; 3.A.25.1.1; the symbiont-specific erad-like machinery (selma) family.
DR   PaxDb; 2850-Phatr5043; -.
DR   GeneID; 7200448; -.
DR   KEGG; pti:PHATRDRAFT_54460; -.
DR   eggNOG; KOG2012; Eukaryota.
DR   HOGENOM; CLU_002556_0_0_1; -.
DR   InParanoid; B7FYG1; -.
DR   OrthoDB; 36498at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000000759; Chromosome 7.
DR   GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
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; 3.40.50.12550; 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; 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; 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; IPR000011; UBQ/SUMO-activ_enz_E1-like.
DR   PANTHER; PTHR10953:SF4; UBA_E1_C DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR   Pfam; PF09358; E1_UFD; 1.
DR   Pfam; PF00899; ThiF; 1.
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.
PE   3: Inferred from homology;
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000759};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..1108
FT                   /note="E1 ubiquitin-activating enzyme"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002852814"
FT   DOMAIN          947..1101
FT                   /note="Ubiquitin-activating enzyme E1 C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00985"
FT   NON_TER         1108
FT                   /evidence="ECO:0000313|EMBL:EEC48718.1"
SQ   SEQUENCE   1108 AA;  123352 MW;  6C0F8592122D613A CRC64;
     MNYCWRFCLG LLLEQALLRD SFGVRFVPIF HPSPRRVKVH IRNALSSRGG GGGDAVGETE
     DDEERYSRQV FALGAEAHKR IRSSTVYLDG PGLDAAYFKG ELDDLGRAYH RAARSETGKS
     DDDCDVSDEE VLMEYLKRLN PSVQVSVVKY SDFRPLDDSL RGVLLCVDRC HEKLLVMNGL
     ARRHNLAFVG TETAGVYGRV FCDFGTSFEV NDTDGETPLV IPLDRVERGI SDEILFVTCL
     EGQQHDVSKG EEIRFIDPNG DSSEQKCTVI EVHTPLRLSI EVDKKGGSCQ EWIESVNKKY
     VAFSRIKASK KLSFDDLAIA SKKASSDASI FTPSDLGKSF DDNRRAALFA CFRAASSFVG
     DHLRWADDND LDDFCELVRT FMSNCESEHC FLSESQHFNV EQFLEVGRAK FSPIQAFFGA
     IASQEALKAL TGLYHPIQQF LLYDCDEILN SPSDRTCSVN EKEGSDRNTC GLRHILGDSI
     VEDLQSMRVF VVGAGAIGCE ILKNLAAMGI GSKSKGRVII TDMDTIEKSN LSRQLLFRDS
     DVGKFKSSAA TQAILRFNNK MKIDSHSSKV GDSEHNPFDD LFWRKGVDIV LNALDNMEAR
     FFTDRQCVAN GKPLIDSGTL GPKGNVQVVI PHKSESYSSS ADPPDPAIAV CTLKNFPYAI
     SHTIQWGRDL FEDVFSRRPS QVNDARDSLS STCVEAFVSR LIQERGENGF QQFAAELKED
     VSPDLESSDI RAHSLEWAAS TAVKLFRDSI ETLLLKHPPG SLDDDGEPFW SGTRRQPRVL
     SFSGSVPLDA MQSSVNENLI DFVRYAARLR AEMYASKPIR DPFEFSRNDA EASLNSAEQA
     QPSDKEVMDT DTVNVLIDSL RRLSSFSKPL NTAEFEKDDD SNGHIAFVTA ASNLRAMSYG
     IPPVNRLQTR RIAGNIVPAV ISTTAAVSAL SCIELVKLAQ GAQLKLHRNA FMNLALPFFA
     FTSPLPAEVM PGLQGRQYTI WDRLKVRESK KALAKGGISL RKLIRRIKQL ASTNPKKVSV
     LSISFGPYLL YASFLHDDDK NHLKSSLWNI LEELTEVDDD FVSTRSNDNR STEYSPTQKF
     VDLSVIVEDP DNGSECELPL VRVFRRFL
//
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