ID D2V1X8_NAEGR Unreviewed; 773 AA.
AC D2V1X8;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Ubiquitin activating enzyme E1 {ECO:0000313|EMBL:EFC49389.1};
GN ORFNames=NAEGRDRAFT_56831 {ECO:0000313|EMBL:EFC49389.1};
OS Naegleria gruberi (Amoeba).
OC Eukaryota; Discoba; Heterolobosea; Tetramitia; Eutetramitia;
OC Vahlkampfiidae; Naegleria.
OX NCBI_TaxID=5762 {ECO:0000313|Proteomes:UP000006671};
RN [1] {ECO:0000313|EMBL:EFC49389.1, ECO:0000313|Proteomes:UP000006671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEG-M {ECO:0000313|EMBL:EFC49389.1,
RC ECO:0000313|Proteomes:UP000006671};
RX PubMed=20211133; DOI=10.1016/j.cell.2010.01.032;
RA Fritz-Laylin L.K., Prochnik S.E., Ginger M.L., Dacks J.B., Carpenter M.L.,
RA Field M.C., Kuo A., Paredez A., Chapman J., Pham J., Shu S., Neupane R.,
RA Cipriano M., Mancuso J., Tu H., Salamov A., Lindquist E., Shapiro H.,
RA Lucas S., Grigoriev I.V., Cande W.Z., Fulton C., Rokhsar D.S., Dawson S.C.;
RT "The genome of Naegleria gruberi illuminates early eukaryotic
RT versatility.";
RL Cell 140:631-642(2010).
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DR EMBL; GG738848; EFC49389.1; -; Genomic_DNA.
DR RefSeq; XP_002682133.1; XM_002682087.1.
DR AlphaFoldDB; D2V1X8; -.
DR STRING; 5762.D2V1X8; -.
DR EnsemblProtists; EFC49389; EFC49389; NAEGRDRAFT_56831.
DR GeneID; 8855247; -.
DR VEuPathDB; AmoebaDB:NAEGRDRAFT_56831; -.
DR eggNOG; KOG2012; Eukaryota.
DR InParanoid; D2V1X8; -.
DR OrthoDB; 20494at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000006671; Unassembled WGS sequence.
DR GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 1.10.10.2660; Ubiquitin-activating enzyme E1, SCCH domain; 1.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR042063; Ubi_acti_E1_SCCH.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR PANTHER; PTHR10953:SF102; ADENYLYLTRANSFERASE AND SULFURTRANSFERASE MOCS3; 1.
DR PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR Pfam; PF00899; ThiF; 1.
DR SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000006671}.
FT DOMAIN 234..668
FT /note="THIF-type NAD/FAD binding fold"
FT /evidence="ECO:0000259|Pfam:PF00899"
SQ SEQUENCE 773 AA; 89678 MW; F4269B3CE0087D78 CRC64;
MLVELTKNLI LLGFKAMALV AIEEGDLSTI HFDSYVKGEN FQEEIHRLNP DSNVKQVSAD
EVSNNLKQFS CIVKCGIEKS NFNDLSNTIV SVQVSGLIGR ILTIPKSETE QIPHFHRSCL
DGPILNAIFE NTSLEEFSTL VSNFIDNMDV NTLFDLFTEK MEEMENPIDS YDENEVKDQL
LNFYHEKFIQ HEKVRETSNY AMILELSKEK HPYYFFFDQL SLAPSQLKIQ ELGLEDLNIL
IVGAGAIGCE LVKNLMVMNA CTTRGSMYVT DMDSIELTNL NRQFFFSQSD IGSKKSQILK
KMVNYFNSKV NIESFEEKLT SDSESYLNQD SFWSSIDVVF GAVDNDHARQ FLSHKCNLYK
IPFINSGTQG FYSQNSFHLY ASTKPFHNEN QKTEEEEREE IRTSCTLKSN PEKHEDLIMW
SKMKYEDYFT RMVPRLLERV ELGNVNNHLY VLAREVFNQL FVSPFQENTL CNLDELNEDN
KIQYFLNESV EFTPRPAKLN YEKESHFSFM NTTIYLLYRH LDNNDLIPST RSVSSVEFPF
MPLTREELQQ YENKFHHQIT IPEKSEEMTH SNMKVNSPFK PLVYEKDDDL MVQFVQDTSN
IRAENFFLFG RKLCKPIEFF KAKKIAGAIH PALITTTSVA ASIQCFHLLQ YLQQLNQYSK
KLSYIKYNIC LDDLDIHYEN ISDNIKEIHM KFTDTIEELV KEARTLNQEM DTIFITNSKG
ETGSLFAPSI FSEHNEQSYL TTPLASLLKS NEKMRILNIS SEQEEITVHL ILQ
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