LOCUS NP_001094537 404 aa linear MAM 18-DEC-2022
DEFINITION ubiquitin-like modifier-activating enzyme 5 [Bos taurus].
ACCESSION NP_001094537 XP_586224
VERSION NP_001094537.1
DBSOURCE REFSEQ: accession NM_001101067.2
KEYWORDS RefSeq.
SOURCE Bos taurus (cattle)
ORGANISM Bos taurus
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
REFERENCE 1 (residues 1 to 404)
AUTHORS Duan R, Shi Y, Yu L, Zhang G, Li J, Lin Y, Guo J, Wang J, Shen L,
Jiang H, Wang G and Tang B.
TITLE UBA5 Mutations Cause a New Form of Autosomal Recessive Cerebellar
Ataxia
JOURNAL PLoS One 11 (2), e0149039 (2016)
PUBMED 26872069
REMARK Publication Status: Online-Only
REFERENCE 2 (residues 1 to 404)
AUTHORS Zimin AV, Delcher AL, Florea L, Kelley DR, Schatz MC, Puiu D,
Hanrahan F, Pertea G, Van Tassell CP, Sonstegard TS, Marcais G,
Roberts M, Subramanian P, Yorke JA and Salzberg SL.
TITLE A whole-genome assembly of the domestic cow, Bos taurus
JOURNAL Genome Biol 10 (4), R42 (2009)
PUBMED 19393038
COMMENT PROVISIONAL REFSEQ: This record has not yet been subject to final
NCBI review. The reference sequence was derived from BC151254.1.
On Aug 14, 2007 this sequence version replaced XP_586224.2.
##Evidence-Data-START##
Transcript exon combination :: BC151254.1, SRR5571263.44533.1
[ECO:0000332]
RNAseq introns :: mixed/partial sample support
SAMN03145412, SAMN03145413
[ECO:0000350]
##Evidence-Data-END##
FEATURES Location/Qualifiers
source 1..404
/organism="Bos taurus"
/db_xref="taxon:9913"
/chromosome="1"
/map="1"
/breed="Hereford"
Protein 1..404
/product="ubiquitin-like modifier-activating enzyme 5"
/note="UFM1-activating enzyme; ubiquitin-activating enzyme
5; ubiquitin-activating enzyme E1 domain-containing
protein 1"
/calculated_mol_wt=44566
Site 45
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0000250|UniProtKB:Q9GZZ9; propagated from
UniProtKB/Swiss-Prot (A7MAZ3.1)"
Region 52..297
/region_name="ThiF_MoeB_HesA_family"
/note="ThiF_MoeB_HesA. Family of E1-like enzymes involved
in molybdopterin and thiamine biosynthesis family. The
common reaction mechanism catalyzed by MoeB and ThiF, like
other E1 enzymes, begins with a nucleophilic attack of the
C-terminal carboxylate of MoaD...; cd00757"
/db_xref="CDD:238386"
Site order(80,82,84,104,106,115,127,181,187)
/site_type="other"
/note="ATP binding site [chemical binding]"
/db_xref="CDD:238386"
Site order(84,182..184,188,206..207,213,215,282,286,293,
295..296)
/site_type="other"
/note="substrate interface [chemical binding]"
/db_xref="CDD:238386"
Region 334..346
/region_name="UFM1-interacting sequence (UIS).
/evidence=ECO:0000250|UniProtKB:Q9GZZ9"
/note="propagated from UniProtKB/Swiss-Prot (A7MAZ3.1)"
Site 358
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0000250|UniProtKB:Q9GZZ9; propagated from
UniProtKB/Swiss-Prot (A7MAZ3.1)"
Site 393
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0000250|UniProtKB:Q8VE47; propagated from
UniProtKB/Swiss-Prot (A7MAZ3.1)"
CDS 1..404
/gene="UBA5"
/coded_by="NM_001101067.2:194..1408"
/db_xref="BGD:BT24476"
/db_xref="GeneID:509292"
/db_xref="VGNC:VGNC:36564"
ORIGIN
1 maesverlqq rveelerela qersrralgs gdggggrari ekmssevvds npysrlmalk
61 rmgivsdyek irtftvaivg vggvgsvtae mltrcgigkl llfdydkvel anmnrlffqp
121 hqaglskvqa aehtlrninp dvlfevhnyn ittvenfehf mnrisnggle egkpvdlvls
181 cvdnfearmt intacnelgq twmesgvsen avsghiqlii pgesacfaca pplvvaanid
241 ektlkregvc aaslpttmgv vagilvqnvl kfllnfgtvs fylgynamqd ffptmsmkpn
301 pqcddrncrk qqkeykkkva alpkqeviqe egeiihedne wgielvseis eeelkkssgp
361 ipdlpegiiv aytvpqkqed svpevtveds gesledlmak mkni
//