ID K0KC37_WICCF Unreviewed; 338 AA.
AC K0KC37;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 13-SEP-2023, entry version 34.
DE SubName: Full=SUMO-activating enzyme subunit 1 {ECO:0000313|EMBL:CCH42640.1};
GN ORFNames=BN7_2184 {ECO:0000313|EMBL:CCH42640.1};
OS Wickerhamomyces ciferrii (strain ATCC 14091 / BCRC 22168 / CBS 111 / JCM
OS 3599 / NBRC 0793 / NRRL Y-1031 F-60-10) (Yeast) (Pichia ciferrii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Wickerhamomyces.
OX NCBI_TaxID=1206466 {ECO:0000313|EMBL:CCH42640.1, ECO:0000313|Proteomes:UP000009328};
RN [1] {ECO:0000313|EMBL:CCH42640.1, ECO:0000313|Proteomes:UP000009328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14091 / BCRC 22168 / CBS 111 / JCM 3599 / NBRC 0793 / NRRL
RC Y-1031 F-60-10 {ECO:0000313|Proteomes:UP000009328};
RX PubMed=23193139; DOI=10.1128/EC.00258-12;
RA Schneider J., Andrea H., Blom J., Jaenicke S., Ruckert C., Schorsch C.,
RA Szczepanowski R., Farwick M., Goesmann A., Puhler A., Schaffer S.,
RA Tauch A., Kohler T., Brinkrolf K.;
RT "Draft genome sequence of Wickerhamomyces ciferrii NRRL Y-1031 F-60-10.";
RL Eukaryot. Cell 11:1582-1583(2012).
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:CCH42640.1}.
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DR EMBL; CAIF01000049; CCH42640.1; -; Genomic_DNA.
DR AlphaFoldDB; K0KC37; -.
DR STRING; 1206466.K0KC37; -.
DR eggNOG; KOG2014; Eukaryota.
DR HOGENOM; CLU_002556_4_1_1; -.
DR InParanoid; K0KC37; -.
DR Proteomes; UP000009328; Unassembled WGS sequence.
DR GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
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; PTHR10953:SF162; SUMO-ACTIVATING ENZYME SUBUNIT 1; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000009328}.
FT DOMAIN 12..334
FT /note="THIF-type NAD/FAD binding fold"
FT /evidence="ECO:0000259|Pfam:PF00899"
FT COILED 244..271
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 338 AA; 38470 MW; FFD0F2672CEDC42D CRC64;
MSELSADELA LYDRQLRVWG ADGQNKIKNA SILVINLNGV GTEIIKNLTL SGIGSIEILD
PSVVTEDDLT TQFFLEESDL GKSKVEAVLP KIQDMNPRVQ LTINSKELPI DDLEYFKKFK
LIIANNLDAK LLQKLNNITR DLNISLYTTT THGLYGYFFS DLILDISQFT KKKMPISRKL
EKISSNQEII QIETTHNKET NEFFEKFTLK SKFIKFEDCF HSKNLTKLTK RAKKNVSPLL
SIFLALYELE LNSIEINLDS LKTKSNEIQL NLGLNEITNL EIFEKILKQL NFEISPVAAI
LGGTLSQDVI NYISKKEIPI NNLLILDGDN FTMPIYEL
//
