ID   A0A421JTL5_9ASCO        Unreviewed;       518 AA.
AC   A0A421JTL5;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=NEDD8-activating enzyme E1 regulatory subunit {ECO:0000256|PIRNR:PIRNR039099};
GN   ORFNames=JA1_001223 {ECO:0000313|EMBL:RLV95150.1};
OS   Spathaspora sp. JA1.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Spathaspora.
OX   NCBI_TaxID=2028339 {ECO:0000313|EMBL:RLV95150.1, ECO:0000313|Proteomes:UP000285775};
RN   [1] {ECO:0000313|EMBL:RLV95150.1, ECO:0000313|Proteomes:UP000285775}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JA1 {ECO:0000313|EMBL:RLV95150.1,
RC   ECO:0000313|Proteomes:UP000285775};
RA   Formighieri E.F., Steindorff A.S., Trichez D., Almeida J.R.;
RT   "Physiological and comparative genomic analysis of newly identified yeasts
RT   Spathaspora sp. JA1 and Meyerozyma sp. JA9 reveals insights into xylitol
RT   production.";
RL   Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Regulatory subunit of the dimeric UBA3-ULA1 E1 enzyme.
CC       {ECO:0000256|PIRNR:PIRNR039099}.
CC   -!- PATHWAY: Protein modification; protein neddylation.
CC       {ECO:0000256|ARBA:ARBA00005032, ECO:0000256|PIRNR:PIRNR039099}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family. ULA1
CC       subfamily. {ECO:0000256|ARBA:ARBA00006868,
CC       ECO:0000256|PIRNR:PIRNR039099}.
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:RLV95150.1}.
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DR   EMBL; NSGQ01000006; RLV95150.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A421JTL5; -.
DR   STRING; 2028339.A0A421JTL5; -.
DR   UniPathway; UPA00885; -.
DR   Proteomes; UP000285775; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0019781; F:NEDD8 activating enzyme activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0045116; P:protein neddylation; IEA:UniProtKB-UniRule.
DR   CDD; cd01493; APPBP1_RUB; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.40.50.12550; Ubiquitin-activating enzyme E1, inactive adenylation domain, subdomain 2; 1.
DR   InterPro; IPR030667; APP-BP1.
DR   InterPro; IPR045886; ThiF/MoeB/HesA.
DR   InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR   InterPro; IPR035985; Ubiquitin-activating_enz.
DR   PANTHER; PTHR10953:SF29; NEDD8-ACTIVATING ENZYME E1 REGULATORY SUBUNIT; 1.
DR   PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR   Pfam; PF00899; ThiF; 1.
DR   PIRSF; PIRSF039099; APP-BP1; 1.
DR   SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000285775};
KW   Ubl conjugation pathway {ECO:0000256|PIRNR:PIRNR039099}.
FT   DOMAIN          11..515
FT                   /note="THIF-type NAD/FAD binding fold"
FT                   /evidence="ECO:0000259|Pfam:PF00899"
SQ   SEQUENCE   518 AA;  59585 MW;  BB9F138EAF643026 CRC64;
     MVPAMDKDTR YDRQLRLWAA SGQSRLENSH ICLLNGTPTG SEILKNLILP GIGKFTIIDD
     RLVTKQDLSG NFFLQKKDLD TPIASAIQHN LKELNHEVEG SYIVKSIDQI LANEPESFWD
     QFNVVIVSDY ISHLKRLIDI LWLHEIPLLI VNSVGFYGSL NLIAPEINVI ETHDPSKLYD
     LRIDQPWPEL QEFSDSFDLD CLDNTEHSHV PYIVIFIKAL KQWKLQHNGQ SPVTYYEKTM
     FRSLIESMSR NIQLETNFIE AYTSYHRAFQ KTEIPNSIKP LLVASQEREL TASSSIFWIY
     IAALHNFIIR NNGLLPLSGK LPDMFSDTNN YIKLQKIYHK KALQDQNLFT QEVYFILESL
     GRSKEGISKD SIISFCKNVQ LLYVTTGSKY LSNDKLIEDL YQENENDGLG VYYGILTFNY
     FVDQFNRAPS LEDSEEFVNL FTDMFGQTKQ LPGSILNIFK EILSHNTRNY HNLCSLMGGI
     ASQEVLKLTT SQYIPLDNLF IFDGIKSTSE RFKIEPVV
//