ID G8BJ03_CANPC Unreviewed; 1012 AA.
AC G8BJ03;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=E1 ubiquitin-activating enzyme {ECO:0000256|ARBA:ARBA00012990};
DE EC=6.2.1.45 {ECO:0000256|ARBA:ARBA00012990};
GN OrderedLocusNames=CPAR2_404220 {ECO:0000313|CGD:CAL0000152747,
GN ECO:0000313|EMBL:CCE44618.1};
OS Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia
OS parapsilosis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=578454 {ECO:0000313|EMBL:CCE44618.1, ECO:0000313|Proteomes:UP000005221};
RN [1] {ECO:0000313|Proteomes:UP000005221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 317 / ATCC MYA-4646 {ECO:0000313|Proteomes:UP000005221};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
RN [2] {ECO:0000313|Proteomes:UP000005221}
RP GENOME REANNOTATION.
RC STRAIN=CDC 317 / ATCC MYA-4646 {ECO:0000313|Proteomes:UP000005221};
RX PubMed=22192698; DOI=10.1186/1471-2164-12-628;
RA Guida A., Lindstaedt C., Maguire S.L., Ding C., Higgins D.G., Corton N.J.,
RA Berriman M., Butler G.;
RT "Using RNA-seq to determine the transcriptional landscape and the hypoxic
RT response of the pathogenic yeast Candida parapsilosis.";
RL BMC Genomics 12:628-628(2011).
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, ECO:0000256|RuleBase:RU000519}.
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DR EMBL; HE605208; CCE44618.1; -; Genomic_DNA.
DR AlphaFoldDB; G8BJ03; -.
DR STRING; 578454.G8BJ03; -.
DR EnsemblFungi; CPAR2_404220-T; CPAR2_404220-T-p1; CPAR2_404220.
DR CGD; CAL0000152747; CPAR2_404220.
DR VEuPathDB; FungiDB:CPAR2_404220; -.
DR eggNOG; KOG2012; Eukaryota.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000005221; Chromosome 4.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:SF4; UBA_E1_C DOMAIN-CONTAINING PROTEIN; 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:UP000005221};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU000519}.
FT DOMAIN 881..1007
FT /note="Ubiquitin-activating enzyme E1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00985"
FT ACT_SITE 591
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ SEQUENCE 1012 AA; 113479 MW; 8024A654F8488AF5 CRC64;
MSDNMQIDSP LQEIDEGLYS RQLYVLGKEA MLKMQNANVL VIGLNGLGVE IAKNIALAGV
KSLSLYDPNP VQIQDLSTQF FLSESDIGQP RDQVSAVKLR ELNAYVPISV VDNIKEETLL
KFKCIVTTNI SLEEQIIINQ ITHANDIGYI NADVRGLFGQ IFVDFGDKFT IVDQTGEEPL
SGIVSDIEKN GTVTMLDENR HGLEDGNFVK FSEVEGLPGL NEGIYKVEVL GPYAFKIKMD
GIEGEYKKGG LYTQVKVPKD VKFEPLLEQL KNPEFLISDF AKFDKPAQLH IGFQALHAFK
TKRQRLPRPY NVEDANEAFA YTEQLAKQNN VEDIDESYLK ELFYQAQGDI PGMVAFYGGL
IAQEVLKCCS SKFTPIKQWL YFDSLESLPG KEEYPRNEEN NKPIGSRYDG QIAVFGKKFQ
DKIANLKIFL VGAGAIGCEM LKNWAMMGLG SGPDGKIFIT DNDSIEKSNL NRQFLFRPKD
VGKNKSDVAA QAVQAMNPAL KGKIESRLDK VGPETQNIFD DAFWSNLDLV TNALDNIEAR
TYVDSRCVFF QKPLLESGTL GTKGNTQVVV PFLTESYSSS HDPPEKSIPL CTLRSFPSKI
DHTIAWAKSL FQGYFVDSPE SVNLYLSQPN YVESSLKQNP DKKGTLENIS KYLNERPYSF
EDCIKWARLE FETKFNHEIK QLLYNFPHDA KTSTGEPFWS GPKRAPTPLK FDVNNKDHLD
FIIGGANLLA YIYGLKEQND IDIKVLEKIE IPEFQPKSGV KIAATDAEAE EQANNLSSSA
DDEEVRKIAA SLPEPSTLAG YRLSPIEFEK DDDTNHHIEF ITAASNCRAL NYGIETADAH
KTKFIAGKII PAIATTTALV TGLVCLELYK VVDKKDDIEQ YKNGFINLAL PFIGFSEPIK
SASGKYGAKE YDQVWDQIII DRDLTLQELI DKFANEDKLE ISILSYDVVV LYASFFPPKK
KQERLNLPIS QVIKLVTKKD IPAHVHYLVL QACCEDEEGE DVDVPPITIK YK
//