ID   A0A024U7Q9_9STRA        Unreviewed;      1014 AA.
AC   A0A024U7Q9;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Ubiquitin-like 1-activating enzyme E1A {ECO:0000256|ARBA:ARBA00044354};
GN   ORFNames=H310_05960 {ECO:0000313|EMBL:ETW02451.1};
OS   Aphanomyces invadans.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC   Aphanomyces.
OX   NCBI_TaxID=157072 {ECO:0000313|EMBL:ETW02451.1};
RN   [1] {ECO:0000313|EMBL:ETW02451.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NJM9701 {ECO:0000313|EMBL:ETW02451.1};
RG   The Broad Institute Genomics Platform;
RA   Russ C., Tyler B., van West P., Dieguez-Uribeondo J., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Chapman S.B.,
RA   Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA   Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Aphanomyces invadans NJM9701.";
RL   Submitted (DEC-2013) 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}.
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DR   EMBL; KI913961; ETW02451.1; -; Genomic_DNA.
DR   RefSeq; XP_008869056.1; XM_008870834.1.
DR   AlphaFoldDB; A0A024U7Q9; -.
DR   STRING; 157072.A0A024U7Q9; -.
DR   EnsemblFungi; H310_05960-t26_1; H310_05960-t26_1-p1; H310_05960.
DR   EnsemblProtists; ETW02451; ETW02451; H310_05960.
DR   GeneID; 20083010; -.
DR   VEuPathDB; FungiDB:H310_05960; -.
DR   eggNOG; KOG2012; Eukaryota.
DR   OrthoDB; 56850at2759; -.
DR   GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR   GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 2.40.30.180; Ubiquitin-activating enzyme E1, FCCH domain; 1.
DR   Gene3D; 3.50.50.80; Ubiquitin-activating enzyme E1, inactive adenylation domain, subdomain 1; 1.
DR   Gene3D; 3.40.50.12550; Ubiquitin-activating enzyme E1, inactive adenylation domain, subdomain 2; 1.
DR   InterPro; IPR032420; E1_4HB.
DR   InterPro; IPR042302; E1_FCCH_sf.
DR   InterPro; IPR045886; ThiF/MoeB/HesA.
DR   InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR   InterPro; IPR042449; Ub-E1_IAD_1.
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; PF16191; E1_4HB; 1.
DR   Pfam; PF00899; ThiF; 2.
DR   PRINTS; PR01849; UBIQUITINACT.
DR   SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 2.
PE   3: Inferred from homology;
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT   DOMAIN          16..398
FT                   /note="THIF-type NAD/FAD binding fold"
FT                   /evidence="ECO:0000259|Pfam:PF00899"
FT   DOMAIN          276..343
FT                   /note="Ubiquitin-activating enzyme E1 four-helix bundle"
FT                   /evidence="ECO:0000259|Pfam:PF16191"
FT   DOMAIN          439..855
FT                   /note="THIF-type NAD/FAD binding fold"
FT                   /evidence="ECO:0000259|Pfam:PF00899"
SQ   SEQUENCE   1014 AA;  110352 MW;  0D698831C34F0D7C CRC64;
     MAEPTPSPVT PKEYYTRPLL LFGSTWMKSI TTMQVLVVGL RGVGVDIVRT LLGHGLKSVT
     IHDDDCVCDD DVASHPVYAR MDVGRKKSSA VKDKLSGIAP STVLLTLSGT LTSELLLHYH
     AVVFSSGPMS REEIVGLSEF CHAQTPPIAV VVAESRGLLG SVFVDFGPHH MAMEDESAAF
     TVVQMDVGAG NVVVQEQCVH LMLQPGDLVE FAFARQSGTD GVTSDLTWLD RRQFSIAQVA
     PPSTVHVNFG VSPLFVFDLT QHSRLRVKRV RGSRAIHHTS FRENIIAPRL VHGPNRSSSN
     EERPAQLHAI MQGLYAYRQL HGFFPQSNNV HHALEILSLT RDFIAKTTAA AQFGPTVVPS
     KPVPDVLVHD VARVASTEFA PLSALVAGLA CRELVKFCGF GCPVSQLLYL DLVGILPKDF
     KKERVFHDPA GLSSDSNAMA LFGRAAVDRL RDARVVVVGC GSVGCQVVEN LTRIGVKNGV
     MVDGGRVKRQ DLATQCGYRD ADVGSNKAHA LQVHHPSWTA IPLHYQQSQS VHFNEAFWQP
     TDVVVTTVDA NHTTLLLDDE CFLYSKPFVL GQSHGLKAFT QSFAPHVTER WAESKLKTDP
     ASTSLFLLDR LAIFRASISP SHKSLPHHVD HATDPTAFEI DHIVQWARAV FDNTFHQSLV
     CLRAVWTDKV GASRAKRRDP AFIQLAHDAY DRYQALTSIS ACVAAAQFFL KAVLAPHGIA
     LSTATHGDLV AVAAVLFGRT VSTLQPTCRD VITAAVAPSA QPALSQEAFQ AMTAIQMQSV
     VDRIRPTPCN VMDDANMHVH FVQLLANTVA AVHGIAPASF FCCKAMCGCR ADSLATATIV
     GALAAIEATK ILFRKPTALR SCEYVGSSGS LHFHTPRPPA VMASTSMDRS RGMPLRICPE
     NMTLWHKVVI QCTDIPRLIT VEDILRHLKA LYEVHVERLT CHNMDIYAAN DPTSLKSNVF
     ETCAAVSHAV PMRKPRTLLV TALCKDHDSD VILPPILLLA PPEINISPSP GADC
//