ID   A0A3Q3H0D3_KRYMA        Unreviewed;       345 AA.
AC   A0A3Q3H0D3;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
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   Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX   NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000028827.1, ECO:0000313|Proteomes:UP000264800};
RN   [1] {ECO:0000313|Ensembl:ENSKMAP00000028827.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-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_017291753.1; XM_017436264.1.
DR   AlphaFoldDB; A0A3Q3H0D3; -.
DR   STRING; 37003.ENSKMAP00000028827; -.
DR   Ensembl; ENSKMAT00000029190.1; ENSKMAP00000028827.1; ENSKMAG00000021368.1.
DR   GeneID; 108247878; -.
DR   KEGG; kmr:108247878; -.
DR   CTD; 10055; -.
DR   GeneTree; ENSGT00550000075007; -.
DR   OMA; EFFGQFD; -.
DR   OrthoDB; 5483037at2759; -.
DR   Proteomes; UP000264800; Unplaced.
DR   GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR   GO; GO:0060216; P:definitive hemopoiesis; IEA:Ensembl.
DR   GO; GO:0061484; P:hematopoietic stem cell homeostasis; IEA:Ensembl.
DR   GO; GO:0016925; P:protein sumoylation; IEA:Ensembl.
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   Reference proteome {ECO:0000313|Proteomes:UP000264800};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT   DOMAIN          17..334
FT                   /note="THIF-type NAD/FAD binding fold"
FT                   /evidence="ECO:0000259|Pfam:PF00899"
SQ   SEQUENCE   345 AA;  38405 MW;  2F9DF906E8D0B142 CRC64;
     MIEKEDPIIS EEEAAQYDRQ IRLWGLDAQK RLRGSRVLLA GLGGLGAEVA KNLILAGVKG
     LTLLDHEQVS EDSCRAQFLV PVSAQGQNRA RASLERAQNL NPMVEVHADP DRVEDKPDDF
     FLQFDAVCLT GCSRDLMVRV DQLCSQRSIK VFCGDVFGYY GYMFCNLGQE HNYVEEKPKV
     VKPSGDSSGG PEAKKAKIDP NETTMVKKTA RFCSLKEALE VDWTSEKAKA ALKRTPLDYF
     LLHVLLKFRT DKGRDPDPKS FTEDGQLLRQ IRDDVLEALA LSSDLLNDDF ISYCFSEVSP
     VCAVVGGVLG QEVVKALSQR DAPHRNFFFF NGRKGSGVVD YFGPN
//