UBA5_ARATH
ID UBA5_ARATH Reviewed; 431 AA.
AC O23034;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 02-MAR-2010, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Ubiquitin-like modifier-activating enzyme 5;
DE Short=Ubiquitin-activating enzyme 5;
GN OrderedLocusNames=At1g05350; ORFNames=YUP8H12.3;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
CC -!- FUNCTION: E1-like enzyme which activates UFM1. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family. UBA5
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB71466.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC000098; AAB71466.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE27828.1; -; Genomic_DNA.
DR PIR; D86188; D86188.
DR RefSeq; NP_172027.2; NM_100414.4.
DR AlphaFoldDB; O23034; -.
DR SMR; O23034; -.
DR STRING; 3702.AT1G05350.1; -.
DR iPTMnet; O23034; -.
DR PaxDb; O23034; -.
DR PRIDE; O23034; -.
DR ProteomicsDB; 228684; -.
DR EnsemblPlants; AT1G05350.1; AT1G05350.1; AT1G05350.
DR GeneID; 837034; -.
DR Gramene; AT1G05350.1; AT1G05350.1; AT1G05350.
DR KEGG; ath:AT1G05350; -.
DR Araport; AT1G05350; -.
DR TAIR; locus:2207185; AT1G05350.
DR eggNOG; KOG2336; Eukaryota.
DR HOGENOM; CLU_013325_0_1_1; -.
DR InParanoid; O23034; -.
DR OMA; FTPDQAG; -.
DR OrthoDB; 1092362at2759; -.
DR PhylomeDB; O23034; -.
DR PRO; PR:O23034; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O23034; baseline and differential.
DR Genevisible; O23034; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0071566; F:UFM1 activating enzyme activity; IBA:GO_Central.
DR GO; GO:0032446; P:protein modification by small protein conjugation; IBA:GO_Central.
DR GO; GO:0071569; P:protein ufmylation; IBA:GO_Central.
DR InterPro; IPR029752; D-isomer_DH_CS1.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR PANTHER; PTHR10953; PTHR10953; 1.
DR Pfam; PF00899; ThiF; 1.
DR SUPFAM; SSF69572; SSF69572; 1.
PE 3: Inferred from homology;
KW ATP-binding; Metal-binding; Nucleotide-binding; Reference proteome;
KW Ubl conjugation pathway; Zinc.
FT CHAIN 1..431
FT /note="Ubiquitin-like modifier-activating enzyme 5"
FT /id="PRO_0000391953"
FT REGION 339..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..377
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 263
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000250"
FT BINDING 92
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 113
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 136
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 159
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 197
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 239
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 242
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 316
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 321
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 431 AA; 47020 MW; 4809072C8873287F CRC64;
MEVGFKALLD DLDVLEKSLS DPALINKLRS HVENLATLSK CNPHRRSKVK ELSSEVVDSN
PYSRLMALQR MGIVDNYERI REFSVAIVGI GGVGSVAAEM LTRCGIGRLL LYDYDTVELA
NMNRLFFRPD QVGMTKTDAA VQTLAEINPD VVLESFTMNI TTVQGFETFT SSLTNKSFCP
SKEGGSGVDL VLSCVDNYEA RMAVNQACNE LRQTWMESGV SEDAVSGHIQ LLVPGETACF
ACAPPLVVAS GIDERTLKRE GVCAASLPTT MGVVAGLLVQ NSLKFLLNFG EVSPYLGYNS
LKDFFPTMKM RPNPQCSNVA CLERQKEYML AKPERDAAAK AKMEADASTT IDEGPLHDDN
EWNISVVDDE NEKDTTKAAS SSDTLPEGLT RELPVADEYE KAIAIASGSG ETEEEDDLED
LKKQLEALNA A
