GenomeNet

Database: UniProt
Entry: A0A0D2HHI4_9EURO
LinkDB: A0A0D2HHI4_9EURO
Original site: A0A0D2HHI4_9EURO 
ID   A0A0D2HHI4_9EURO        Unreviewed;       625 AA.
AC   A0A0D2HHI4;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=Ubiquitin-activating enzyme E1-like {ECO:0000256|PIRNR:PIRNR039133};
GN   ORFNames=Z520_02913 {ECO:0000313|EMBL:KIY01361.1};
OS   Fonsecaea multimorphosa CBS 102226.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX   NCBI_TaxID=1442371 {ECO:0000313|EMBL:KIY01361.1, ECO:0000313|Proteomes:UP000053411};
RN   [1] {ECO:0000313|EMBL:KIY01361.1, ECO:0000313|Proteomes:UP000053411}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 102226 {ECO:0000313|EMBL:KIY01361.1,
RC   ECO:0000313|Proteomes:UP000053411};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Fonsecaea multimorphosa CBS 102226.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Protein modification; protein sumoylation.
CC       {ECO:0000256|ARBA:ARBA00004718, ECO:0000256|PIRNR:PIRNR039133}.
CC   -!- SUBUNIT: Heterodimer. {ECO:0000256|PIRNR:PIRNR039133}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family.
CC       {ECO:0000256|ARBA:ARBA00005673, ECO:0000256|PIRNR:PIRNR039133}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KN848065; KIY01361.1; -; Genomic_DNA.
DR   RefSeq; XP_016635483.1; XM_016773426.1.
DR   AlphaFoldDB; A0A0D2HHI4; -.
DR   STRING; 1442371.A0A0D2HHI4; -.
DR   GeneID; 27708659; -.
DR   VEuPathDB; FungiDB:Z520_02913; -.
DR   OrthoDB; 20494at2759; -.
DR   UniPathway; UPA00886; -.
DR   Proteomes; UP000053411; Unassembled WGS sequence.
DR   GO; GO:0031510; C:SUMO activating enzyme complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019948; F:SUMO activating enzyme activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016925; P:protein sumoylation; IEA:UniProtKB-UniRule.
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; PS51257; PROKAR_LIPOPROTEIN; 1.
DR   PROSITE; PS00865; UBIQUITIN_ACTIVAT_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR039133};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR039133,
KW   ECO:0000256|PIRSR:PIRSR039133-3};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRNR:PIRNR039133};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053411};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PIRNR:PIRNR039133};
KW   Zinc {ECO:0000256|PIRNR:PIRNR039133, ECO:0000256|PIRSR:PIRSR039133-3}.
FT   DOMAIN          15..413
FT                   /note="THIF-type NAD/FAD binding fold"
FT                   /evidence="ECO:0000259|Pfam:PF00899"
FT   DOMAIN          311..373
FT                   /note="Ubiquitin-activating enzyme SCCH"
FT                   /evidence="ECO:0000259|Pfam:PF10585"
FT   DOMAIN          441..521
FT                   /note="Ubiquitin/SUMO-activating enzyme ubiquitin-like"
FT                   /evidence="ECO:0000259|Pfam:PF14732"
FT   REGION          544..598
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        544..562
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        574..588
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        176
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039133-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU10132"
FT   BINDING         27..32
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039133-2"
FT   BINDING         51
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039133-2"
FT   BINDING         59..62
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039133-2"
FT   BINDING         75
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039133-2"
FT   BINDING         120..125
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039133-2"
FT   BINDING         161
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039133-3"
FT   BINDING         164
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039133-3"
FT   BINDING         431
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039133-3"
FT   BINDING         434
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039133-3"
SQ   SEQUENCE   625 AA;  69153 MW;  1B076A4CF5BEA3EF CRC64;
     MPRDRYTRKS LGATQRLVKE SRVLLVGAGG IGCELLKNLV LTGFGEIHII DLDTIDLSNL
     NRQFLFRQEH IKKPKALVAK DVAQKFNPNV QLFAYHANIK DKQFNLEWFS GFNIVFNALD
     NMDARRHVNK MCLAVDVPLV ESGTTGFRGQ VQVIKKGKTA CYDCTPKTTP ISYPVCTIRS
     TPSQPIHCIV WAKSYLLPEL FGVSEDEAAE MDSSEDSENA EEIQKLKEEA QALKRIRALM
     GSNDFAKQVF DKVFKEDIER LAKMEDMWKD KKPPEPLSYD TLEQLASEVG PGVATNGQVT
     WSAVENFVVF KDSLDRLVKR LSQEQAAASR SGALQPSISF DKDDDDTMDF VAATGNLRAI
     IFGIEPKSKF DIKQMAGNII PAIATTNAMV AGLCVLQAFK VLKGDYARTR WLWLGIGSLR
     TDHLDSPNPE CPVCSVAMAR VHVNIERATL GDLVQDILRT RLGYGEEVTV MTEAGVVYDP
     DLEDNLEKKL SDLNIVDASF VLVKDEDENP RVDLQIAIEA KKPEDETKAV LLVEKEGEAL
     EIPRKPKESV SDGIHDEDDD MNGLIVSNGV SGGKRKRPLD DEGDESAQPA KKLQGLSSAE
     VAKNQIMAAI VIDEEDGALV IADDD
//
DBGET integrated database retrieval system