ID   A0A0D9ZF17_9ORYZ        Unreviewed;       511 AA.
AC   A0A0D9ZF17;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=NEDD8-activating enzyme E1 regulatory subunit {ECO:0000256|PIRNR:PIRNR039099};
OS   Oryza glumipatula.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=40148 {ECO:0000313|EnsemblPlants:OGLUM03G38890.1};
RN   [1] {ECO:0000313|EnsemblPlants:OGLUM03G38890.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Wing R.A., Panaud O., Oliveira A.C.;
RT   "Oryza genome evolution.";
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:OGLUM03G38890.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
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   AlphaFoldDB; A0A0D9ZF17; -.
DR   STRING; 40148.A0A0D9ZF17; -.
DR   EnsemblPlants; OGLUM03G38890.1; OGLUM03G38890.1; OGLUM03G38890.
DR   Gramene; OGLUM03G38890.1; OGLUM03G38890.1; OGLUM03G38890.
DR   eggNOG; KOG2016; Eukaryota.
DR   HOGENOM; CLU_019618_2_1_1; -.
DR   UniPathway; UPA00885; -.
DR   Proteomes; UP000026961; Unassembled WGS sequence.
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   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000026961};
KW   Ubl conjugation pathway {ECO:0000256|PIRNR:PIRNR039099}.
FT   DOMAIN          16..506
FT                   /note="THIF-type NAD/FAD binding fold"
FT                   /evidence="ECO:0000259|Pfam:PF00899"
SQ   SEQUENCE   511 AA;  56954 MW;  3BDE135964F6B0BD CRC64;
     MAAATAAAFA EPKTKYDRQL RIWGDQGQAA LEKASICLLT CGPTGTEAMK NLVLGGVGSV
     TVVDGSKVEQ SDMGNNFLLD AECLGQSRAK SVCSFLQELN DAVNAKFVEE SPLVLIDTNP
     SFFSQFTVVI ATQLPERSLL KLDDICRKAN IVLVAARSYG LTGLVRISVK EHNVIESKPD
     HFLDDLRLHN PWVELKQFAK SIDINDKDPV VHKHTPYIVI LVRLAEKWAD AHDGRLPSTR
     QEKNEFKALI REHMLNLDEE NYKEAVESSY KVSVTPGISD EIRQIIDDSS AEVNSSSSDF
     WVLVAALKEF IANEGNGELP LEGTIPDMTS LTEYYVSLQK IYQAKAESDC LALEHHVKDI
     LKRIDRDPDS ISRAYIKTFC KNARKLRVCR YRSMEEEFSS PVLSEVQKYF TDEDYCFVMN
     FYVLLRAVDR LAANYNRCPG IFESEIDEDV PRLKTAAVSV MSEMGMNGAP LSEDLITEMC
     RFGGAEIHPV AAFIGGVASQ EVIKWINLSS G
//