ID A0A3M2S1S7_9HYPO Unreviewed; 581 AA.
AC A0A3M2S1S7;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Ubiquitin-like 1-activating enzyme E1A {ECO:0000256|ARBA:ARBA00044354};
GN ORFNames=CDV36_008891 {ECO:0000313|EMBL:RMJ11478.1};
OS Fusarium kuroshium.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium solani species complex.
OX NCBI_TaxID=2010991 {ECO:0000313|EMBL:RMJ11478.1, ECO:0000313|Proteomes:UP000277212};
RN [1] {ECO:0000313|EMBL:RMJ11478.1, ECO:0000313|Proteomes:UP000277212}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCR3666 {ECO:0000313|EMBL:RMJ11478.1};
RA Stajich J.E., Carrillo J., Kijimoto T., Eskalen A., O'Donnell K.,
RA Kasson M.;
RT "Comparative genomic analysis of Ambrosia Fusariam Clade fungi.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC {ECO:0000256|ARBA:ARBA00004718}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family.
CC {ECO:0000256|ARBA:ARBA00005673}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RMJ11478.1}.
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DR EMBL; NKUJ01000166; RMJ11478.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M2S1S7; -.
DR STRING; 2010991.A0A3M2S1S7; -.
DR Proteomes; UP000277212; Unassembled WGS sequence.
DR GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR GO; GO:0036211; P:protein modification process; IEA:InterPro.
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 Reference proteome {ECO:0000313|Proteomes:UP000277212};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 124..455
FT /note="THIF-type NAD/FAD binding fold"
FT /evidence="ECO:0000259|Pfam:PF00899"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 532..581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 581 AA; 61841 MW; A2FC70A926460B2F CRC64;
MDASNNNQGQ PPVAPQVQQL PDASAAAAMA PIDAGANLNG NGNAIPQLPD HLLGSMNPEA
MVGMMADPSL MADPTMLAAM QMPLADPSAF MMQPGMAIPN GQPHAFGVPV AQPATVSADE
IALYDRQIRL WGMAAQAKIQ SANILLITIK ALANEIAKNL VLAGIGSLTL LDGAVVTEAD
RGSQFFLSED DSIIGQNRAQ AASAALQKLN PRVRVHVDTE GVKTKGPSYF AGFDIVIATD
LDPESFNIIN TATRLNCKAF YAAGCHGLYG FIFSDLIEHD YVIQRDLGNV PTVPGPETRT
RTIVDVQTRK EGPKTIESVT KRELYSTWFL ASDVGGLPEE YTQSRRRLKS VTPALSCLRA
LWEFMQIQGG RVPSNRDDLK MFTQIATQKH KALGLPSETL RPEFLRSFLQ NLVSEISPVA
AILGGQLAQD VINVLGQTQQ PIQNMVVFDG NTMEGLMYPL HPEGSLGSGL LTDHQVPNGG
APMMLPTGMD ALPMGIDPTA MGALPHHNNP IMIPGGLPQN GMGLAMQDAS MTDPTQQFNP
AQPPQQDPQQ VPQQAAPQPT AATAEQPAQE APANPSNAGA N
//
