ID   UBE1Y_OSPRU             Reviewed;         152 AA.
AC   P31255;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=Ubiquitin-activating enzyme E1 Y;
DE            EC=6.2.1.45 {ECO:0000250|UniProtKB:P22314};
DE   Flags: Fragment;
GN   Name=UBE1Y; Synonyms=SBY;
OS   Osphranter rufus (Red kangaroo) (Macropus rufus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Metatheria; Diprotodontia; Macropodidae; Osphranter.
OX   NCBI_TaxID=9321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX   PubMed=1406968; DOI=10.1038/359528a0;
RA   Mitchell M.J., Woods D.R., Wilcox S.A., Graves J.A., Bishop C.E.;
RT   "Marsupial Y chromosome encodes a homologue of the mouse Y-linked candidate
RT   spermatogenesis gene Ube1y.";
RL   Nature 359:528-531(1992).
CC   -!- FUNCTION: Activates ubiquitin by first adenylating its C-terminal
CC       glycine residue with ATP, and thereafter linking this residue to the
CC       side chain of a cysteine residue in E1, yielding a ubiquitin-E1
CC       thioester and free AMP (By similarity). The Y chromosome form could be
CC       involved in the survival and proliferation of differentiating
CC       spermatogonia. {ECO:0000250|UniProtKB:P22314, ECO:0000305}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine
CC         = AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-
CC         L-cysteine.; EC=6.2.1.45; Evidence={ECO:0000250|UniProtKB:P22314};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000250|UniProtKB:P22314}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- MISCELLANEOUS: There are two active sites within the E1 molecule,
CC       allowing it to accommodate two ubiquitin moieties at a time, with a new
CC       ubiquitin forming an adenylate intermediate as the previous one is
CC       transferred to the thiol site. {ECO:0000250|UniProtKB:P22314}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family.
CC       {ECO:0000305}.
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DR   EMBL; Z29668; CAA82766.1; -; Genomic_DNA.
DR   EMBL; X68940; CAA48758.1; -; mRNA.
DR   PIR; S29752; S29752.
DR   AlphaFoldDB; P31255; -.
DR   SMR; P31255; -.
DR   UniPathway; UPA00143; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004839; F:ubiquitin activating enzyme activity; IEA:UniProtKB-EC.
DR   Gene3D; 1.10.10.2660; -; 1.
DR   InterPro; IPR045886; ThiF/MoeB/HesA.
DR   InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR   InterPro; IPR019572; UBA_E1_SCCH.
DR   InterPro; IPR042063; Ubi_acti_E1_SCCH.
DR   InterPro; IPR035985; Ubiquitin-activating_enz.
DR   InterPro; IPR033127; UBQ-activ_enz_E1_Cys_AS.
DR   PANTHER; PTHR10953; PTHR10953; 1.
DR   Pfam; PF00899; ThiF; 1.
DR   Pfam; PF10585; UBA_e1_thiolCys; 1.
DR   SUPFAM; SSF69572; SSF69572; 1.
DR   PROSITE; PS00865; UBIQUITIN_ACTIVAT_2; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Ligase; Nucleotide-binding; Ubl conjugation pathway.
FT   CHAIN           <1..>152
FT                   /note="Ubiquitin-activating enzyme E1 Y"
FT                   /id="PRO_0000194940"
FT   ACT_SITE        51
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10132"
FT   NON_TER         1
FT   NON_TER         152
SQ   SEQUENCE   152 AA;  17719 MW;  5E434CFBACA5CD85 CRC64;
     MYMDRHCVYY RKPLLESGTL GTKGNIQVVI PFLTESYSSS QDPPEKSIPI CTLKNFPNAI
     EHTLQWARDE FESLFKQPAE NVNQYLTNPK FVERTLRLGG TQPLEVLEAV HRSLVLQRPH
     DWADCVTWAC LHWHSQYANN IRQLLHNFPP EQ