ID A0A1E4TC97_9ASCO Unreviewed; 500 AA.
AC A0A1E4TC97;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Ubiquitin-activating enzyme E1-like {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=CANCADRAFT_20431 {ECO:0000313|EMBL:ODV89268.1};
OS Tortispora caseinolytica NRRL Y-17796.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Trigonopsidaceae; Tortispora.
OX NCBI_TaxID=767744 {ECO:0000313|EMBL:ODV89268.1, ECO:0000313|Proteomes:UP000095023};
RN [1] {ECO:0000313|Proteomes:UP000095023}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-17796 {ECO:0000313|Proteomes:UP000095023};
RG DOE Joint Genome Institute;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goker M.,
RA Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K., Choi C.,
RA Clum A., Coughlan A.Y., Deshpande S., Douglass A.P., Hanson S.J.,
RA Klenk H.-P., Labutti K., Lapidus A., Lindquist E., Lipzen A.,
RA Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J., Peng Y.,
RA Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C., Stielow J.B.,
RA Sun H., Kurtzman C.P., Blackwell M., Jeffries T.W., Grigoriev I.V.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; KV453843; ODV89268.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E4TC97; -.
DR OrthoDB; 20494at2759; -.
DR UniPathway; UPA00886; -.
DR Proteomes; UP000095023; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019948; F:SUMO activating enzyme activity; IEA:InterPro.
DR GO; GO:0016925; P:protein sumoylation; IEA:UniProtKB-UniPathway.
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; 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; IPR030661; Uba2.
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; PF00899; ThiF; 1.
DR Pfam; PF14732; UAE_UbL; 1.
DR Pfam; PF10585; UBA_E1_SCCH; 1.
DR PIRSF; PIRSF039133; SUMO_E1B; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR039133-
KW 2}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR039133-3};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR039133-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000095023};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|PIRSR:PIRSR039133-3}.
FT DOMAIN 7..389
FT /note="THIF-type NAD/FAD binding fold"
FT /evidence="ECO:0000259|Pfam:PF00899"
FT DOMAIN 316..354
FT /note="Ubiquitin-activating enzyme SCCH"
FT /evidence="ECO:0000259|Pfam:PF10585"
FT DOMAIN 426..498
FT /note="Ubiquitin/SUMO-activating enzyme ubiquitin-like"
FT /evidence="ECO:0000259|Pfam:PF14732"
FT ACT_SITE 168
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR039133-1,
FT ECO:0000256|PROSITE-ProRule:PRU10132"
FT BINDING 18..23
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR039133-2"
FT BINDING 42
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR039133-2"
FT BINDING 50..53
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR039133-2"
FT BINDING 66
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR039133-2"
FT BINDING 112..117
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR039133-2"
FT BINDING 153
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR039133-3"
FT BINDING 156
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR039133-3"
FT BINDING 415
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR039133-3"
FT BINDING 418
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR039133-3"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ODV89268.1"
FT NON_TER 500
FT /evidence="ECO:0000313|EMBL:ODV89268.1"
SQ SEQUENCE 500 AA; 55745 MW; 685628FC7CDB5A41 CRC64;
LWQDKFATIR NSKVLLVGAG GIGCELIKNL VLSGFGEIHV VDLDTIDLSN LNRQFLFRHS
HIKQPKSVIA KKTASQFNPD VNIIAYHANI KLDAQFDTAW FSSFDIVFNA LDNLEARRHV
NHMCLATNTP LIESGTTGFN GQVQVIVPGQ TECYDCNPKP VTKAFPVCTI RSTPSEPIHC
IVWAKSYLFT QIFGEDDDFE AAAQPDEDQK ELEELRKESA ELNQVRDALE SDNFDQLLFN
KVFTDDIERL SKHEEVWKYR KAPVALDYSK LFKKAQTLDI NDVLSRDQTV WSPEENLAVY
MDAIKRLKQR ALVGGRTTLV FDKDDKDTLD FVAAVANLRA LTFGIPQKSI FEIKQIAGNI
IPAIATTNAI IAGICVIEGL KVLCPLGAEP CNAFLARRPE RFLSSESTHP PNAECAVCGV
ARATVHANLE ELTVQTIVDA LARDLEYGEE ISLITDQLIY DIDFDDNLAV KLTDLGIASD
SFITVVDDNE TNRVNLELLV
//
