ID   UBC9_PAGMA              Reviewed;         158 AA.
AC   Q6Y1Z4;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=SUMO-conjugating enzyme UBC9;
DE            EC=2.3.2.-;
DE   AltName: Full=RING-type E3 SUMO transferase UBC9;
DE   AltName: Full=SUMO-protein ligase;
DE   AltName: Full=Ubiquitin carrier protein I;
DE   AltName: Full=Ubiquitin-conjugating enzyme E2 I;
DE   AltName: Full=Ubiquitin-protein ligase I;
GN   Name=ube2i;
OS   Pagrus major (Red sea bream) (Chrysophrys major).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Spariformes; Sparidae; Pagrus.
OX   NCBI_TaxID=143350;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Spleen;
RX   AGRICOLA=IND43674139; DOI=10.1016/j.aquaculture.2004.07.008;
RA   Chen S.-L., Xu M.-Y., Hu S.-L., Li L.;
RT   "Analysis of immune-relevant genes expressed in red sea bream spleen.";
RL   Aquaculture 240:115-130(2004).
CC   -!- FUNCTION: Accepts the ubiquitin-like proteins SUMO1, SUMO2 and SUMO3
CC       from the UBLE1A-UBLE1B E1 complex and catalyzes their covalent
CC       attachment to other proteins with the help of an E3 ligase such as
CC       RANBP2 or CBX4. Essential for nuclear architecture and chromosome
CC       segregation. {ECO:0000250}.
CC   -!- PATHWAY: Protein modification; protein sumoylation.
CC   -!- SUBUNIT: Forms a tight complex with RANGAP1 and RANBP2. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR   EMBL; AY190745; AAP20220.1; -; mRNA.
DR   AlphaFoldDB; Q6Y1Z4; -.
DR   SMR; Q6Y1Z4; -.
DR   UniPathway; UPA00886; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR   GO; GO:0016925; P:protein sumoylation; IEA:UniProtKB-UniPathway.
DR   CDD; cd00195; UBCc; 1.
DR   Gene3D; 3.10.110.10; -; 1.
DR   InterPro; IPR000608; UBQ-conjugat_E2.
DR   InterPro; IPR023313; UBQ-conjugating_AS.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   Pfam; PF00179; UQ_con; 1.
DR   SUPFAM; SSF54495; SSF54495; 1.
DR   PROSITE; PS00183; UBC_1; 1.
DR   PROSITE; PS50127; UBC_2; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cell cycle; Cell division; Chromosome partition; Mitosis;
KW   Nucleotide-binding; Nucleus; Transferase; Ubl conjugation pathway.
FT   CHAIN           1..158
FT                   /note="SUMO-conjugating enzyme UBC9"
FT                   /id="PRO_0000268878"
FT   DOMAIN          4..157
FT                   /note="UBC core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT   REGION          13..18
FT                   /note="Interaction with sumo1"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        93
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT                   ECO:0000255|PROSITE-ProRule:PRU10133"
FT   SITE            4
FT                   /note="Interaction with ranbp2"
FT                   /evidence="ECO:0000250"
FT   SITE            25
FT                   /note="Interaction with ranbp2"
FT                   /evidence="ECO:0000250"
FT   SITE            57
FT                   /note="Interaction with ranbp2"
FT                   /evidence="ECO:0000250"
FT   SITE            100..101
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   158 AA;  17813 MW;  BC13BB56A0687BD6 CRC64;
     MSGIALSRLA QERKAWRKDH PLGLVAVPTK NPDGTMNLMN GECAIPGKKG TPWEGGLFKL
     RMLFKDDYPS SPPKCKFEPP LFHPNVYPSG TVCLSILEED KDWRPAITIK QILLGIQELL
     NEPNIQDPAQ AEAYTIFCQD RTEYEKRVRA QAKKFSPS