ID A0A165J7G9_EXIGL Unreviewed; 653 AA.
AC A0A165J7G9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Ubiquitin-activating enzyme E1-like {ECO:0008006|Google:ProtNLM};
GN ORFNames=EXIGLDRAFT_611663 {ECO:0000313|EMBL:KZV94438.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV94438.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZV94438.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZV94438.1,
RC ECO:0000313|Proteomes:UP000077266};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC {ECO:0000256|ARBA:ARBA00004718}.
CC -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family.
CC {ECO:0000256|ARBA:ARBA00005673}.
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DR EMBL; KV425972; KZV94438.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165J7G9; -.
DR STRING; 1314781.A0A165J7G9; -.
DR InParanoid; A0A165J7G9; -.
DR OrthoDB; 20494at2759; -.
DR UniPathway; UPA00886; -.
DR Proteomes; UP000077266; Unassembled WGS sequence.
DR GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR GO; GO:0016925; P:protein sumoylation; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.10.520; Ubiquitin activating enzymes (Uba3). Chain: B, domain 2; 1.
DR Gene3D; 3.50.50.80; Ubiquitin-activating enzyme E1, inactive adenylation domain, subdomain 1; 1.
DR Gene3D; 3.10.290.20; Ubiquitin-like 2 activating enzyme e1b. Chain: B, domain 3; 1.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR042449; Ub-E1_IAD_1.
DR InterPro; IPR023318; Ub_act_enz_dom_a_sf.
DR InterPro; IPR019572; UBA_E1_SCCH.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR InterPro; IPR033127; UBQ-activ_enz_E1_Cys_AS.
DR PANTHER; PTHR10953:SF5; SUMO-ACTIVATING ENZYME SUBUNIT 2; 1.
DR PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR Pfam; PF00899; ThiF; 1.
DR Pfam; PF10585; UBA_E1_SCCH; 1.
DR SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS00865; UBIQUITIN_ACTIVAT_2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Reference proteome {ECO:0000313|Proteomes:UP000077266};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 3..446
FT /note="THIF-type NAD/FAD binding fold"
FT /evidence="ECO:0000259|Pfam:PF00899"
FT DOMAIN 355..392
FT /note="Ubiquitin-activating enzyme SCCH"
FT /evidence="ECO:0000259|Pfam:PF10585"
FT REGION 298..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 551..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 203..243
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 298..317
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..579
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..601
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 176
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ SEQUENCE 653 AA; 70306 MW; 84FC74846C4B6FE9 CRC64;
MSRNTHARAI LGADHARLDS TKVLLVGAGG IGCELLKNVV LTGFKNITLL DLDTIDLSNL
NRQFLFRKKD VKQSKALVAA KTAAAFNPDV HITPLHANIK EPQFDVAWFG GFDIVLNALD
NLDARRHVNK MCMAANVPLV ESGTAGYFGQ VQPLLKDRTE CFDCIPKPTP KTFPVCTIRS
TPSQPIHCIV WAKSYLVPQL FGEDEDEGEL DDAERQGENA EEIANLRKQA QAFRAVRQAL
RSTNDDPEAA AKAAFEKVYD ADIQNLLIMK DMWRSRAPPV PLDFDTIQSG SFVLRGTPAA
PQTNGTSNGT NGAATNGHSH APGLKDQKTL TLGDNLRLFV SSAVRLAERL RAGEGTISFD
KDDDDTLDFV TASSNLRSAA YGIPGKTRWE VKEMAGNIIP AIATTNAVVS GLIVLQALHL
LRQAPNAIRN VHLSASKAAI PLSSSSVIPP DPGCAVCRDC YTVVRCDPTR ATLGDVVHGV
MGGAGREVSV FEGQRVLSDP DWDDNFERTL DSLGIVQGKF VTIVDEDDEL ATIAVAICLL
PYNHPADGPA LVLPDPLPQP GKKSKPRAVP PPSPTPLDIV PNTPAKKRRR DEVDDMPEPS
AKRARVANGS PSKAQRLEED GLIIVDAMDV VDVDADAHGD AAATTGPEVI ELD
//
