ID C4R5S2_KOMPG Unreviewed; 1029 AA.
AC C4R5S2;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=E1 ubiquitin-activating enzyme {ECO:0000256|ARBA:ARBA00012990};
DE EC=6.2.1.45 {ECO:0000256|ARBA:ARBA00012990};
GN OrderedLocusNames=PAS_chr3_0856 {ECO:0000313|EMBL:CAY70908.1};
OS Komagataella phaffii (strain GS115 / ATCC 20864) (Yeast) (Pichia pastoris).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Komagataella.
OX NCBI_TaxID=644223 {ECO:0000313|EMBL:CAY70908.1, ECO:0000313|Proteomes:UP000000314};
RN [1] {ECO:0000313|EMBL:CAY70908.1, ECO:0000313|Proteomes:UP000000314}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GS115 / ATCC 20864 {ECO:0000313|Proteomes:UP000000314};
RX PubMed=19465926; DOI=10.1038/nbt.1544;
RA De Schutter K., Lin Y.C., Tiels P., Van Hecke A., Glinka S.,
RA Weber-Lehmann J., Rouze P., Van de Peer Y., Callewaert N.;
RT "Genome sequence of the recombinant protein production host Pichia
RT pastoris.";
RL Nat. Biotechnol. 27:561-566(2009).
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; FN392321; CAY70908.1; -; Genomic_DNA.
DR RefSeq; XP_002493087.1; XM_002493042.1.
DR AlphaFoldDB; C4R5S2; -.
DR SMR; C4R5S2; -.
DR STRING; 644223.C4R5S2; -.
DR EnsemblFungi; CAY70908; CAY70908; PAS_chr3_0856.
DR GeneID; 8200344; -.
DR KEGG; ppa:PAS_chr3_0856; -.
DR eggNOG; KOG2012; Eukaryota.
DR HOGENOM; CLU_002556_0_0_1; -.
DR InParanoid; C4R5S2; -.
DR OMA; GANLHAF; -.
DR OrthoDB; 20494at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000000314; Chromosome 3.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004839; F:ubiquitin activating enzyme activity; IEA:UniProtKB-EC.
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; IPR018074; UBQ-activ_enz_E1_CS.
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; PS00536; UBIQUITIN_ACTIVAT_1; 1.
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:UP000000314};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU000519}.
FT DOMAIN 898..1024
FT /note="Ubiquitin-activating enzyme E1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00985"
FT REGION 776..810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 788..810
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 605
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ SEQUENCE 1029 AA; 115150 MW; E8A626EFBC7F1751 CRC64;
MAIRHTNEVQ ENKMQIDKPE EGKIDEDLYS RQLYVLGKEA MLKMQNSNVL IIGLKGLGVE
IAKNVALAGV KSLSLYDPEP VTLQDLSSQF FLSEKDIGEQ RAFATSSKLS ELNHYVPISI
ITELSESSLK SFQVIVTTET SLEKQVQINE FTHANNIKFI SAATRGLFGQ AFIDFGDSFT
VLDQTGEEPK QGIVSDIEPD GTVTMLDDSR HDLEDGRYVK FSEVQGIERL NDGQLFKIKV
LGPYAFKIDF DNSWGTYEKG GIFTEVKVPQ TVSFKKLSDQ LNDPEYLYSD FAKLDRPPQL
HLGFQALHQF QNAHEGQLPK PHHEEDANQL LKLTENLAEQ VPSILGEGTE VDSKLIKELS
YQARGDLPAV NAFFGGLVAQ EVLKACSGKF NPIKQWLYYD SLESLPDSDR TEETCASINS
RYDNQIAVFG LSHIQKIANL KVFLVGAGAI GCEMLKNWAM MGLGSGPNGK IVLTDNDSIE
KSNLNRQFLF RPKDVGQNKS EVAARAVVEM NPDLAGKIEA KVDKVGPETE NIFDNSFWQG
LDVVTNALDN IEARAYVDRR CVFFKKPLLE SGTLGTKGNT QVVIPRLTES YSSSQDPPEK
SIPLCTLRSF PNKIDHTIAW AKSLFQGYFS EAPENVNLYL SQPNYVENIL KQSGDAKGTL
ETISQYLNER PYTFEDCIKW ARLQFETKFN HEIQQLLYNF PKDSVTSTGA PFWSGPKRAP
TPLEFDIDNE DHFNFVVGGA NLLAFIYGLK GDQGEPDKAH YKAVLDTLKI EPFKPRSDVK
IQADDNDPDP NANGNDLNDD VIQKLSDSLP PPSSLAGYRL TPAEFEKDDD TNHHIQFIAA
ASNCRALNYS IETADKQKTK FIAGRIVPAI ATTTALVTGL ITLELYKVVF GKEKIEDYKN
GFVNLALPFF GFSEPIASPQ SKYNDKSFDQ IWDRFDIDKD LTLQELLDKF EKDEGLAINM
LSYGVSLLYA SFHPPKKLKD RLPLKLTELI KTVSKKAIPA HESKLIFEIC ADDKEGEDVE
VPYICLHLD
//
