ID B5DFY9_SALSA Unreviewed; 533 AA.
AC B5DFY9;
DT 14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2008, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=NEDD8-activating enzyme E1 regulatory subunit {ECO:0000256|ARBA:ARBA00015407, ECO:0000256|PIRNR:PIRNR039099};
GN Name=nae1 {ECO:0000313|EMBL:ACH70663.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|EMBL:ACH70663.1};
RN [1] {ECO:0000313|EMBL:ACH70663.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=White muscle {ECO:0000313|EMBL:ACH70663.1};
RX PubMed=19878547; DOI=10.1186/1471-2164-10-502;
RA Andreassen R., Lunner S., Hoyheim B.;
RT "Characterization of full-length sequenced cDNA inserts (FLIcs) from
RT Atlantic salmon (Salmo salar).";
RL BMC Genomics 10:502-502(2009).
CC -!- FUNCTION: Regulatory subunit of the dimeric UBA3-NAE1 E1 enzyme. E1
CC activates NEDD8 by first adenylating its C-terminal glycine residue
CC with ATP, thereafter linking this residue to the side chain of the
CC catalytic cysteine, yielding a NEDD8-UBA3 thioester and free AMP. E1
CC finally transfers NEDD8 to the catalytic cysteine of UBE2M.
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; BT043548; ACH70663.1; -; mRNA.
DR AlphaFoldDB; B5DFY9; -.
DR UniPathway; UPA00885; -.
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; 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 2: Evidence at transcript level;
KW Ubl conjugation pathway {ECO:0000256|PIRNR:PIRNR039099}.
FT DOMAIN 12..531
FT /note="THIF-type NAD/FAD binding fold"
FT /evidence="ECO:0000259|Pfam:PF00899"
SQ SEQUENCE 533 AA; 60285 MW; 9BB65927C8CD398F CRC64;
MALTKASKEQ KYDRQLRLWG DHGQEELENA HVCLINSTAS GTEILKNLVL PGIGAFTIVD
GHKVSGEDVG NNFFLSNSCI GRNRAQAATE LLQELNTDVS GNFVEESPEK LLDNDPEFFH
RFTLVVGVQL PESTCLRLGS VLWNANIPFL VCRTYGLVGY MRLVVKEHTV IESHPDNALE
DLRLDQPFAE LKNHIQSYDL EGMGKKDHSH TPWIIIVAKY LEKWFSEHNF QLPKNYKEKE
AFKQLIRQGI LNNEKGTPED EENFEEAIKN VNTALNPTKI SSGVDDIFNG EQCNDITSQT
PAFWVMTRAV REFVQNDGGG NLPVRGSIPD MIADSEKFIN LQNIYREKAM QDASVVSKHV
ESLLQSVGKP SESISEQDIK LFCKNAAFLR VVRCRSLAEE YSVETVNKDE ITSCMDSADG
EMVLYLMLRS VDRFYQQHSR YPGVYNYQVE EDISKLKLCV NSLLQEYSLN VNVKDDYIHE
FCRYGAAEPH TVASFLGGSA AQEAIKIITR QFVPFNNTFI YNAMSQTTAT FQL
//
