ID D8RVZ4_SELML Unreviewed; 542 AA.
AC D8RVZ4;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 24-JAN-2024, entry version 56.
DE RecName: Full=NEDD8-activating enzyme E1 regulatory subunit {ECO:0000256|PIRNR:PIRNR039099};
GN Name=AXR1-1 {ECO:0000313|EMBL:EFJ23460.1};
GN ORFNames=SELMODRAFT_103350 {ECO:0000313|EMBL:EFJ23460.1};
OS Selaginella moellendorffii (Spikemoss).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella.
OX NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514};
RN [1] {ECO:0000313|EMBL:EFJ23460.1, ECO:0000313|Proteomes:UP000001514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551031; DOI=10.1126/science.1203810;
RA Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M.,
RA dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., Ashton N.W.,
RA Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., Bonawitz N.D.,
RA Chapple C., Cheng C., Correa L.G., Dacre M., DeBarry J., Dreyer I.,
RA Elias M., Engstrom E.M., Estelle M., Feng L., Finet C., Floyd S.K.,
RA Frommer W.B., Fujita T., Gramzow L., Gutensohn M., Harholt J., Hattori M.,
RA Heyl A., Hirai T., Hiwatashi Y., Ishikawa M., Iwata M., Karol K.G.,
RA Koehler B., Kolukisaoglu U., Kubo M., Kurata T., Lalonde S., Li K., Li Y.,
RA Litt A., Lyons E., Manning G., Maruyama T., Michael T.P., Mikami K.,
RA Miyazaki S., Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R.,
RA Obara M., Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B.,
RA Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y.,
RA Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N.,
RA Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N.,
RA Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., Wakazuki S.,
RA Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., Zimmer A.D., Zhu Q.,
RA Mitros T., Hellsten U., Loque D., Otillar R., Salamov A., Schmutz J.,
RA Shapiro H., Lindquist E., Lucas S., Rokhsar D., Grigoriev I.V.;
RT "The Selaginella genome identifies genetic changes associated with the
RT evolution of vascular plants.";
RL Science 332:960-963(2011).
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; GL377592; EFJ23460.1; -; Genomic_DNA.
DR RefSeq; XP_002975259.1; XM_002975213.1.
DR AlphaFoldDB; D8RVZ4; -.
DR STRING; 88036.D8RVZ4; -.
DR EnsemblPlants; EFJ23460; EFJ23460; SELMODRAFT_103350.
DR GeneID; 9629389; -.
DR Gramene; EFJ23460; EFJ23460; SELMODRAFT_103350.
DR KEGG; smo:SELMODRAFT_103350; -.
DR eggNOG; KOG2016; Eukaryota.
DR HOGENOM; CLU_019618_2_1_1; -.
DR InParanoid; D8RVZ4; -.
DR OMA; TMEHSHI; -.
DR OrthoDB; 5488891at2759; -.
DR UniPathway; UPA00885; -.
DR Proteomes; UP000001514; Unassembled WGS sequence.
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:UP000001514};
KW Ubl conjugation pathway {ECO:0000256|PIRNR:PIRNR039099}.
FT DOMAIN 26..536
FT /note="THIF-type NAD/FAD binding fold"
FT /evidence="ECO:0000259|Pfam:PF00899"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 542 AA; 58835 MW; AF6B86781B8EBA7E CRC64;
MAHANGGSGD EQKKAAAAAA TRSNKYDRQL RIWGEHGQGA LEQASVCLLN CGATGSEALK
NLVLGGIGNV TAVDGGLVQE SDLGNNFLLS AENLGQPRAK SMAALLQEMN DSVLIDHIDA
SPESLLDSDP GFFARFTLVI ATQMRDRSLV ILDEVCRRFS VMLLVARSYG LTGYVRISLR
EHAVIESKPD NTVSDLRLHR PWPELTTFVK EFNLETEDSL VHKHIPFAII LLKVCEEWRS
KHGGALPSTT KERSEFKSLV ASKKQAQDED NYKEAVAAAS KVWSPPSLSS EVKAILEDGA
ADVDSSSSDF WILVAALKGF VASEGGGEFP LDGAIPDMHS FTEYYILLQR CYQAKAESDV
SAVEAHVRSI LSQLGRDPDS ISRAAIKHFC KNSRNLRVLR YSSLAEELGL KEVGAKLQKY
LPFEGDNANY AIYLMFRAVD RFAEEFGRFP GAMADETVEE DAAKLGAIAH KLAGEIGVDG
GVSEEFVYEF SRFGGGEIHC VGAVVGGIAS QEAIKLVTKQ FTPTAGTLIY NAISSTTTIF
QL
//
