ID A0A0E9NI51_SAICN Unreviewed; 1049 AA.
AC A0A0E9NI51;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Ubiquitin-activating enzyme E1-like {ECO:0008006|Google:ProtNLM};
GN ORFNames=G7K_3696-t1 {ECO:0000313|EMBL:GAO49547.1};
OS Saitoella complicata (strain BCRC 22490 / CBS 7301 / JCM 7358 / NBRC 10748
OS / NRRL Y-17804).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Taphrinomycotina incertae sedis; Saitoella.
OX NCBI_TaxID=698492 {ECO:0000313|EMBL:GAO49547.1, ECO:0000313|Proteomes:UP000033140};
RN [1] {ECO:0000313|EMBL:GAO49547.1, ECO:0000313|Proteomes:UP000033140}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-17804 {ECO:0000313|EMBL:GAO49547.1,
RC ECO:0000313|Proteomes:UP000033140};
RX PubMed=21914972; DOI=10.2323/jgam.57.243;
RA Nishida H., Hamamoto M., Sugiyama J.;
RT "Draft genome sequencing of the enigmatic yeast Saitoella complicata.";
RL J. Gen. Appl. Microbiol. 57:243-246(2011).
RN [2] {ECO:0000313|EMBL:GAO49547.1, ECO:0000313|Proteomes:UP000033140}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-17804 {ECO:0000313|EMBL:GAO49547.1,
RC ECO:0000313|Proteomes:UP000033140};
RX PubMed=24646756; DOI=10.2323/jgam.60.7;
RA Nishida H., Matsumoto T., Kondo S., Hamamoto M., Yoshikawa H.;
RT "The early diverging ascomycetous budding yeast Saitoella complicata has
RT three histone deacetylases belonging to the Clr6, Hos2, and Rpd3
RT lineages.";
RL J. Gen. Appl. Microbiol. 60:7-12(2014).
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC {ECO:0000256|ARBA:ARBA00004718}.
CC -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family.
CC {ECO:0000256|ARBA:ARBA00005673}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAO49547.1}.
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DR EMBL; BACD03000023; GAO49547.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0E9NI51; -.
DR STRING; 698492.A0A0E9NI51; -.
DR UniPathway; UPA00886; -.
DR Proteomes; UP000033140; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProt.
DR GO; GO:0019948; F:SUMO activating enzyme activity; IEA:UniProt.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR GO; GO:0016925; P:protein sumoylation; IEA:UniProtKB-UniPathway.
DR CDD; cd01489; Uba2_SUMO; 1.
DR Gene3D; 1.10.10.520; Ubiquitin activating enzymes (Uba3). Chain: B, domain 2; 1.
DR Gene3D; 3.50.50.80; Ubiquitin-activating enzyme E1, inactive adenylation domain, subdomain 1; 1.
DR Gene3D; 3.10.290.20; Ubiquitin-like 2 activating enzyme e1b. Chain: B, domain 3; 1.
DR InterPro; IPR006886; RNA_pol_III_Rpc5.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR028077; UAE_UbL_dom.
DR InterPro; IPR042449; Ub-E1_IAD_1.
DR InterPro; IPR023318; Ub_act_enz_dom_a_sf.
DR InterPro; IPR019572; UBA_E1_SCCH.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR InterPro; IPR033127; UBQ-activ_enz_E1_Cys_AS.
DR PANTHER; PTHR10953:SF5; SUMO-ACTIVATING ENZYME SUBUNIT 2; 1.
DR PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR Pfam; PF04801; RPC5; 1.
DR Pfam; PF00899; ThiF; 1.
DR Pfam; PF14732; UAE_UbL; 1.
DR Pfam; PF10585; UBA_E1_SCCH; 1.
DR SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
DR PROSITE; PS00865; UBIQUITIN_ACTIVAT_2; 1.
PE 3: Inferred from homology;
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Reference proteome {ECO:0000313|Proteomes:UP000033140};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 459..854
FT /note="THIF-type NAD/FAD binding fold"
FT /evidence="ECO:0000259|Pfam:PF00899"
FT DOMAIN 753..814
FT /note="Ubiquitin-activating enzyme SCCH"
FT /evidence="ECO:0000259|Pfam:PF10585"
FT DOMAIN 886..951
FT /note="Ubiquitin/SUMO-activating enzyme ubiquitin-like"
FT /evidence="ECO:0000259|Pfam:PF14732"
FT REGION 1..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 968..1027
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..32
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..96
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1000..1027
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 620
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ SEQUENCE 1049 AA; 116742 MW; 7A50F8491415867A CRC64;
MSLFNPLSDS EDEEMEVGVQ LPQEHIDEDM SIGNDQMAEQ PEDPIPPMMA QDISMHEADA
GTGPVHAEDL QEHHEEEPSD EEEEEEEEEE DDDDPVVKTY DIYTTDRLNE HLYLFQYPTR
PNTRPLTTSR NSEPLSAKIK PRAGMIEVDV PIALEKYYDE DRGRELGQAL EEGQGFESGE
GRLLDRQIFG ARIQNNWGNY MVGVLRGEEL HLSPVKSVVQ LKQTYNYVDK LDTLAKAQKK
TEGPAAPTAG PRAVTVTAKA ASSEGPQIDS NLAAKRLAEE DSWVRLKWHD VADPESINVS
GNLVQPPVAE GEDGLGRKPL KCVTSVGEYL TMLSAPKTQV EGELQMNAKP ARKISAPLVD
IKNVKGEEQP WEEISTSRGI RRRRSGDALF ADADAALQVL EDPPSTPFAR PLLDDVARTG
PQCAAAPERT TNAYDVEDKY VAIAMSRYSH LEKSLPTLSE KIKTSKVLMV GAGGIGCELL
KNLTLTGFGE IHMVDLDTID LSNLNRQFLF RKEHIKRSKA LVAKESAAKF NPDVKLVAHH
ANIKDPEFSV SWFASFDIVF NALDNLDARR YVNQMCLAAD VPLIESGTTG FLGQVQVIKG
GKTECYDCNP KEVPKSFPVC TIRSTPSQPI HCIVWAKSYL FPQLFGLDEE DAGDVTHTDE
DNKEEVKTLR AEAEQLKRIR ESMGTDGFAR MVWEKVFEKD VERLRGMEDM WKHREKPHVL
KYDDLGAKVA EGEELAKHDQ KVWDAEESFA VFIDSLNRLS TRLTALQKAG KEGSPPPILS
FDKDDTDTLD FVAAASNIRS LIFHIPTKSK FEIKQMAGNI IPAIATTNAI VAGVCVLQAF
KVLKGKWDEA RMVFLSRRAE RAFNSEPLRP PNSVCEVCAV GRASINVNLE RTTIEQLVSY
LTGPLGYGEE ISIMTDKLLY DVDFDDNLER TLGEMGITDG TFLTVVDEND ADDDYETRQN
LVLNVANSPE EEPQVQPADC SIPRKPKPAP MAQENDSIPA DVNPKKRSLE SDDHQDDIRK
RGRVAEEDGV VRATETIVIE DDDGVITLD
//
