ID   UBCX_PICAN              Reviewed;         188 AA.
AC   O60015;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   22-FEB-2023, entry version 93.
DE   RecName: Full=Ubiquitin-conjugating enzyme E2-21 kDa;
DE            EC=2.3.2.23;
DE   AltName: Full=E2 ubiquitin-conjugating enzyme PEX4;
DE   AltName: Full=Peroxin-4;
DE   AltName: Full=Ubiquitin carrier protein;
DE   AltName: Full=Ubiquitin-protein ligase;
GN   Name=PEX4;
OS   Pichia angusta (Yeast) (Hansenula polymorpha).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Pichiaceae; Ogataea.
OX   NCBI_TaxID=870730;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 34438 / CBS 4732 / DSM 70277 / JCM 3621 / NBRC 1476 / NRRL
RC   Y-5445;
RX   PubMed=9649431; DOI=10.1093/emboj/17.13.3608;
RA   van der Klei I.J., Hilbrands R.E., Kiel J.A.K.W., Rasmussen S.W.,
RA   Cregg J.M., Veenhuis M.;
RT   "The ubiquitin-conjugating enzyme Pex4p of Hansenula polymorpha is required
RT   for efficient functioning of the PTS1 import machinery.";
RL   EMBO J. 17:3608-3618(1998).
CC   -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other
CC       proteins. Essential for peroxisome biogenesis. Required for UBC4-
CC       independent ubiquitination of PEX5. {ECO:0000255|PROSITE-
CC       ProRule:PRU00388}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine +
CC         [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-
CC         activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-
CC         conjugating enzyme]-L-cysteine.; EC=2.3.2.23;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROSITE-
CC         ProRule:PRU10133};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF061604; AAC16238.1; -; Genomic_DNA.
DR   PDB; 5NKZ; X-ray; 2.85 A; A/B=3-188.
DR   PDB; 5NL8; X-ray; 2.20 A; A=3-188.
DR   PDBsum; 5NKZ; -.
DR   PDBsum; 5NL8; -.
DR   AlphaFoldDB; O60015; -.
DR   SMR; O60015; -.
DR   UniPathway; UPA00143; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IEA:UniProtKB-EC.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR   GO; GO:0007031; P:peroxisome organization; IEA:UniProtKB-KW.
DR   GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR   CDD; cd00195; UBCc; 1.
DR   Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR   InterPro; IPR000608; UBQ-conjugat_E2.
DR   InterPro; IPR023313; UBQ-conjugating_AS.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   PANTHER; PTHR24067:SF352; UBIQUITIN-CONJUGATING ENZYME; 1.
DR   PANTHER; PTHR24067; UBIQUITIN-CONJUGATING ENZYME E2; 1.
DR   Pfam; PF00179; UQ_con; 1.
DR   SMART; SM00212; UBCc; 1.
DR   SUPFAM; SSF54495; UBC-like; 1.
DR   PROSITE; PS00183; UBC_1; 1.
DR   PROSITE; PS50127; UBC_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Nucleotide-binding; Peroxisome biogenesis;
KW   Transferase; Ubl conjugation pathway.
FT   CHAIN           1..188
FT                   /note="Ubiquitin-conjugating enzyme E2-21 kDa"
FT                   /id="PRO_0000082557"
FT   DOMAIN          3..182
FT                   /note="UBC core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT   ACT_SITE        119
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT                   ECO:0000255|PROSITE-ProRule:PRU10133"
FT   HELIX           4..19
FT                   /evidence="ECO:0007829|PDB:5NL8"
FT   STRAND          20..22
FT                   /evidence="ECO:0007829|PDB:5NL8"
FT   HELIX           25..28
FT                   /evidence="ECO:0007829|PDB:5NL8"
FT   STRAND          31..40
FT                   /evidence="ECO:0007829|PDB:5NL8"
FT   STRAND          43..49
FT                   /evidence="ECO:0007829|PDB:5NL8"
FT   STRAND          52..54
FT                   /evidence="ECO:0007829|PDB:5NKZ"
FT   TURN            55..58
FT                   /evidence="ECO:0007829|PDB:5NKZ"
FT   STRAND          60..66
FT                   /evidence="ECO:0007829|PDB:5NL8"
FT   TURN            69..72
FT                   /evidence="ECO:0007829|PDB:5NL8"
FT   STRAND          77..80
FT                   /evidence="ECO:0007829|PDB:5NL8"
FT   HELIX           85..92
FT                   /evidence="ECO:0007829|PDB:5NL8"
FT   TURN            113..115
FT                   /evidence="ECO:0007829|PDB:5NL8"
FT   HELIX           121..124
FT                   /evidence="ECO:0007829|PDB:5NL8"
FT   HELIX           133..145
FT                   /evidence="ECO:0007829|PDB:5NL8"
FT   HELIX           155..162
FT                   /evidence="ECO:0007829|PDB:5NL8"
FT   HELIX           166..179
FT                   /evidence="ECO:0007829|PDB:5NL8"
FT   STRAND          180..182
FT                   /evidence="ECO:0007829|PDB:5NL8"
SQ   SEQUENCE   188 AA;  21531 MW;  0BC293A5E0787CB8 CRC64;
     MSSTEKRLLK EYRAVKKELT EKRSPIHDTG IVDLHPLEDG LFRWSAVIRG PDQSPFEDAL
     WKLEIDIPTN YPLDPPKIKF VVFGEEKIRQ LQRKTSSGAR KVCYKMPHPN VNFKTGEICL
     DILQQKWSPA WTLQSALVAI VVLLANPEPL SPLNIDMANL LKCDDTTAYK DLVHYYIAKY
     SAYESNDV
//