ID S3E9N5_GLAL2 Unreviewed; 611 AA.
AC S3E9N5;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Activating enzyme of the ubiquitin-like protein {ECO:0000313|EMBL:EPE35033.1};
GN ORFNames=GLAREA_10728 {ECO:0000313|EMBL:EPE35033.1};
OS Glarea lozoyensis (strain ATCC 20868 / MF5171).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Helotiaceae; Glarea.
OX NCBI_TaxID=1116229 {ECO:0000313|EMBL:EPE35033.1, ECO:0000313|Proteomes:UP000016922};
RN [1] {ECO:0000313|EMBL:EPE35033.1, ECO:0000313|Proteomes:UP000016922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 20868 / MF5171 {ECO:0000313|Proteomes:UP000016922};
RX PubMed=23688303; DOI=10.1186/1471-2164-14-339;
RA Chen L., Yue Q., Zhang X., Xiang M., Wang C., Li S., Che Y.,
RA Ortiz-Lopez F.J., Bills G.F., Liu X., An Z.;
RT "Genomics-driven discovery of the pneumocandin biosynthetic gene cluster in
RT the fungus Glarea lozoyensis.";
RL BMC Genomics 14:339-339(2013).
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DR EMBL; KE145355; EPE35033.1; -; Genomic_DNA.
DR RefSeq; XP_008078020.1; XM_008079829.1.
DR AlphaFoldDB; S3E9N5; -.
DR STRING; 1116229.S3E9N5; -.
DR GeneID; 19469774; -.
DR KEGG; glz:GLAREA_10728; -.
DR eggNOG; KOG2018; Eukaryota.
DR HOGENOM; CLU_013325_9_3_1; -.
DR OMA; CKLAEYP; -.
DR OrthoDB; 10004at2759; -.
DR Proteomes; UP000016922; Unassembled WGS sequence.
DR GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR CDD; cd00755; YgdL_like; 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 PANTHER; PTHR43267; TRNA THREONYLCARBAMOYLADENOSINE DEHYDRATASE; 1.
DR PANTHER; PTHR43267:SF2; TRNA THREONYLCARBAMOYLADENOSINE DEHYDRATASE 1-RELATED; 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:UP000016922}.
FT DOMAIN 210..464
FT /note="THIF-type NAD/FAD binding fold"
FT /evidence="ECO:0000259|Pfam:PF00899"
FT REGION 1..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 611 AA; 68004 MW; 17803953A54ED53A CRC64;
MDRPYNRPYY DYDHEYPTIS PPRSWSSYTS ADSEDSLDED GYPIDSDERN RRRAQGLHYS
RFYNPGGRVY SETSAPSSPE SSRRAGKQSE RAPKAPEEKV EEKESMASWI GRITGSREAQ
FAATAVVSGA IVAGAIFGYQ NVRRRERVGE LKADIPDLND RTQGHSVGEL TDFGGASTVL
SKEDERSVRL AERAQKGDYD DDLILEQLAR NRVFLTDEGL HRLREAFVIV VGCGGVGSHC
AAALARSGVS NIRLIDFDQV TLSSLNRHAV ATLGDVGTPK VACLKKRLHQ ITPWVHFDLR
NELYREEAAE VLLEPYRGRK PDFIIDAIDN IDSKVSLLTY CHKHDLPIIS SMGAGCKSDP
TRIFIGDISS STEDPLSRST RRRLRALGVA SGIPVVYSTE KPGPGKAQLL PLPEEEFQKG
KVGELGVLPD FRVRILPVLG TMPAVFGYAV ANHVILKITG YPHEYVPAKG REKMYDGILA
QLQGSEEKLA RLTTPGEDAQ GLKLGLSVYD VGYLVEEVYR GKSVLSGITT RLALVRWRKP
EAGSTIKVDV EGQKNSIVRL GDLVCMTKEE ANVHEREVVK GDKTPEQFYD EEIVELVESR
LREEKSFEKY R
//
