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Database: UniProt
Entry: A0A3B4DP64_PYGNA
LinkDB: A0A3B4DP64_PYGNA
Original site: A0A3B4DP64_PYGNA 
ID   A0A3B4DP64_PYGNA        Unreviewed;       348 AA.
AC   A0A3B4DP64;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=SUMO-activating enzyme subunit 1 {ECO:0000256|ARBA:ARBA00044187};
DE   AltName: Full=Ubiquitin-like 1-activating enzyme E1A {ECO:0000256|ARBA:ARBA00044354};
OS   Pygocentrus nattereri (Red-bellied piranha).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC   Characoidei; Pygocentrus.
OX   NCBI_TaxID=42514 {ECO:0000313|Ensembl:ENSPNAP00000025263.1, ECO:0000313|Proteomes:UP000261440};
RN   [1] {ECO:0000313|Ensembl:ENSPNAP00000025263.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- PATHWAY: Protein modification; protein sumoylation.
CC       {ECO:0000256|ARBA:ARBA00004718}.
CC   -!- SUBUNIT: Heterodimer of SAE1 and UBA2/SAE2. The heterodimer corresponds
CC       to the two domains that are encoded on a single polypeptide chain in
CC       ubiquitin-activating enzyme E1. Interacts with UBE2I.
CC       {ECO:0000256|ARBA:ARBA00026003}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family.
CC       {ECO:0000256|ARBA:ARBA00005673}.
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DR   RefSeq; XP_017550322.1; XM_017694833.1.
DR   RefSeq; XP_017550323.1; XM_017694834.1.
DR   RefSeq; XP_017550324.1; XM_017694835.1.
DR   RefSeq; XP_017550325.1; XM_017694836.1.
DR   AlphaFoldDB; A0A3B4DP64; -.
DR   Ensembl; ENSPNAT00000008061.1; ENSPNAP00000025263.1; ENSPNAG00000010268.1.
DR   GeneID; 108425838; -.
DR   CTD; 10055; -.
DR   GeneTree; ENSGT00550000075007; -.
DR   OMA; EFFGQFD; -.
DR   OrthoDB; 5483037at2759; -.
DR   Proteomes; UP000261440; Unplaced.
DR   GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR   GO; GO:0032446; P:protein modification by small protein conjugation; IEA:UniProt.
DR   CDD; cd01492; Aos1_SUMO; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR045886; ThiF/MoeB/HesA.
DR   InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR   InterPro; IPR035985; Ubiquitin-activating_enz.
DR   InterPro; IPR000011; UBQ/SUMO-activ_enz_E1-like.
DR   PANTHER; PTHR10953:SF162; SUMO-ACTIVATING ENZYME SUBUNIT 1; 1.
DR   PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR   Pfam; PF00899; ThiF; 1.
DR   PRINTS; PR01849; UBIQUITINACT.
DR   SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
PE   3: Inferred from homology;
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT   DOMAIN          20..339
FT                   /note="THIF-type NAD/FAD binding fold"
FT                   /evidence="ECO:0000259|Pfam:PF00899"
SQ   SEQUENCE   348 AA;  38956 MW;  B3EEEB7C68498D25 CRC64;
     MIDMIEKEDN VISEEEAAQY DRQIRLWGLE AQKRLRGSRV LLVGLRGLGA EVAKNLILAG
     VKGLTLLDHE QVTEESRRAQ FLIPVDADGQ NQAQASLERA QFLNPMVEVK ADTDQVETKS
     DDFFLQFDAV CLTGCSRDLM VRVDQLCASK NIKVFCGDIF GYHGYMFSDL GQEHHYVEEK
     AKVVKPSEQA NDGPEVKKPK IDLNETTMVK KTASFCSLKE ALEIDWTSDD SKARLKRTPP
     EYFLLQVLLK FRTDKGRNPD PCSFAEDSLL LLQIRDDVLE AMGVNPELLP DSFVSYCFSE
     MAPVCAVVGG VLGQEIVKAL SQRDAPHRNF FFFDGLKGSG VVDYFGAK
//
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