ID   UBA5_BRAFL              Reviewed;         405 AA.
AC   C3YZ51;
DT   02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Ubiquitin-like modifier-activating enzyme 5;
DE            Short=Ubiquitin-activating enzyme 5;
GN   ORFNames=BRAFLDRAFT_113714;
OS   Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC   Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC   Branchiostomidae; Branchiostoma.
OX   NCBI_TaxID=7739;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S238N-H82; TISSUE=Testis;
RX   PubMed=18563158; DOI=10.1038/nature06967;
RA   Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA   Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA   Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA   Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA   Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA   Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA   Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA   Satoh N., Rokhsar D.S.;
RT   "The amphioxus genome and the evolution of the chordate karyotype.";
RL   Nature 453:1064-1071(2008).
CC   -!- FUNCTION: E1-like enzyme which activates UFM1. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family. UBA5
CC       subfamily. {ECO:0000305}.
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DR   EMBL; GG666565; EEN54559.1; -; Genomic_DNA.
DR   RefSeq; XP_002598547.1; XM_002598501.1.
DR   AlphaFoldDB; C3YZ51; -.
DR   SMR; C3YZ51; -.
DR   STRING; 7739.XP_002598547.1; -.
DR   eggNOG; KOG2336; Eukaryota.
DR   InParanoid; C3YZ51; -.
DR   OMA; FTPDQAG; -.
DR   OrthoDB; 1092362at2759; -.
DR   Proteomes; UP000001554; Partially assembled WGS sequence.
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..405
FT                   /note="Ubiquitin-like modifier-activating enzyme 5"
FT                   /id="PRO_0000391935"
FT   REGION          1..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..33
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        248
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         81
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         102
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         125
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         148
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         182
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         224
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         227
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         301
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         306
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   405 AA;  44879 MW;  3E3101AC769D55EC CRC64;
     MATVEELQTR VKQLEEELER ERTRNRGGTD GGGGRKKIDQ MSSEVVDSNP YSRLMALKRM
     GIVDNYERIR DFTVAIVGVG GVGSVTAEML TRCGIGKLLL FDYDKVELAN MNRLFFQPHQ
     AGLSKVQAAE ITLRDINPDV EFETHNYNIT TVDNFQHFMD RISHGHLKGD RPVDLVLSCV
     DNFEARMAIN TACNEQGQVW IESGVSENAV SGHIQVIKPG ETACFACAPP LVVASGIDEK
     TLKREGVCAA SLPTTMGIVA GFLVQNTLKY LLEFGSVTYY LGYNAMQDFF PSMAMKPNPN
     CDDSFCTKLQ TEYQEKLLAQ PKEEAKEETV EEVVHDANDW GIELVAETTE EELKAASHGH
     VPELVEGVHV AYVRPMTQED EEGAAGLTVD DQESLEDLMA KMKSI