ID A0A061E937_THECC Unreviewed; 524 AA.
AC A0A061E937;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=NEDD8-activating enzyme E1 regulatory subunit {ECO:0000256|PIRNR:PIRNR039099};
GN ORFNames=TCM_011349 {ECO:0000313|EMBL:EOY01476.1};
OS Theobroma cacao (Cacao) (Cocoa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Byttnerioideae; Theobroma.
OX NCBI_TaxID=3641 {ECO:0000313|EMBL:EOY01476.1, ECO:0000313|Proteomes:UP000026915};
RN [1] {ECO:0000313|EMBL:EOY01476.1, ECO:0000313|Proteomes:UP000026915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Matina 1-6 {ECO:0000313|Proteomes:UP000026915};
RX PubMed=23731509; DOI=10.1186/gb-2013-14-6-r53;
RA Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Iii D.L.,
RA Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C.,
RA Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C., Feltus F.A.,
RA Mustiga G.M., Amores F., Phillips W., Marelli J.P., May G.D., Shapiro H.,
RA Ma J., Bustamante C.D., Schnell R.J., Main D., Gilbert D., Parida L.,
RA Kuhn D.N.;
RT "The genome sequence of the most widely cultivated cacao type and its use
RT to identify candidate genes regulating pod color.";
RL Genome Biol. 14:R53.1-R53.24(2013).
CC -!- FUNCTION: Regulatory subunit of the dimeric E1 enzyme. E1 activates
CC RUB1/NEDD8 by first adenylating its C-terminal glycine residue with
CC ATP, thereafter linking this residue to the side chain of the catalytic
CC cysteine, yielding a RUB1-ECR1 thioester and free AMP. E1 finally
CC transfers RUB1 to the catalytic cysteine of RCE1.
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}.
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DR EMBL; CM001880; EOY01476.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A061E937; -.
DR STRING; 3641.A0A061E937; -.
DR EnsemblPlants; EOY01476; EOY01476; TCM_011349.
DR Gramene; EOY01476; EOY01476; TCM_011349.
DR eggNOG; KOG2016; Eukaryota.
DR HOGENOM; CLU_019618_2_1_1; -.
DR InParanoid; A0A061E937; -.
DR OMA; KLITHQY; -.
DR UniPathway; UPA00885; -.
DR Proteomes; UP000026915; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0019781; F:NEDD8 activating enzyme activity; IBA:GO_Central.
DR GO; GO:0045116; P:protein neddylation; IBA:GO_Central.
DR CDD; cd01493; APPBP1_RUB; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
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:UP000026915};
KW Ubl conjugation pathway {ECO:0000256|PIRNR:PIRNR039099}.
FT DOMAIN 8..501
FT /note="THIF-type NAD/FAD binding fold"
FT /evidence="ECO:0000259|Pfam:PF00899"
SQ SEQUENCE 524 AA; 58291 MW; BA2E5190B6C85FF8 CRC64;
MAEPKTKYDR QLRIWGEQGQ AALEKASICL LNCGPTGSET LKNLVLGGVG SITIVDGSKV
ELGDLGNNFM VDESSLGQSK AKCVCSFLQE LNDAVKAKFI EEYPEALIDT NPSFFSQFTL
VVATQLVEES MVKLDRICRE ANVMLIFARS YGLTGLVRIS VKEHAVIESK PDHFLDDLRL
NNPWPELRGF AEAIDLNVQD PVAHKHIPYV VILVKMADEW IKSHGGSLPS TREEKREFKE
LLKARMVAMD EDNYKEAIDA SFKVFAPRGI SSDLQQIIID SCAEVASNSS DFWVMVAALK
EFIANEGGGE APLEGSIPDM TSSTEHYVNL QKIYQAKSEA DFLVIEKRVR NILKKIGRDP
NSIPKATIKS FCKNARKLKV CRYRLIEDEY NNPSLPELQK YLTDEDYSIA VGFYILLRAV
DRYAANFNSF PGQFDGGMDE DISRLKTTAV GLLNDFGCNG LTLTEDLINE MCRFGAAELH
AVAAFIGGIA SQEVIKLITK QFVPMSGTYV FNGIDHKSQL LSLY
//