UBC3_MIMIV
ID UBC3_MIMIV Reviewed; 1441 AA.
AC Q5UQ88;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 29-SEP-2021, entry version 87.
DE RecName: Full=Probable ubiquitin-conjugating enzyme E2 R521;
DE EC=2.3.2.23;
DE AltName: Full=E2 ubiquitin-conjugating enzyme R521;
DE AltName: Full=Ubiquitin carrier protein;
DE AltName: Full=Ubiquitin-protein ligase;
GN OrderedLocusNames=MIMI_R521;
OS Acanthamoeba polyphaga mimivirus (APMV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC Imitervirales; Mimiviridae; Mimivirus.
OX NCBI_TaxID=212035;
OH NCBI_TaxID=5757; Acanthamoeba polyphaga (Amoeba).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rowbotham-Bradford;
RX PubMed=15486256; DOI=10.1126/science.1101485;
RA Raoult D., Audic S., Robert C., Abergel C., Renesto P., Ogata H.,
RA La Scola B., Susan M., Claverie J.-M.;
RT "The 1.2-megabase genome sequence of Mimivirus.";
RL Science 306:1344-1350(2004).
CC -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other
CC proteins. {ECO:0000255|PROSITE-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};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR EMBL; AY653733; AAV50785.1; -; Genomic_DNA.
DR SMR; Q5UQ88; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000001134; Genome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0042262; P:DNA protection; IEA:InterPro.
DR CDD; cd00195; UBCc; 1.
DR Gene3D; 3.10.110.10; -; 2.
DR Gene3D; 3.10.470.10; -; 1.
DR InterPro; IPR036620; MC1_sf.
DR InterPro; IPR000608; UBQ-conjugat_E2.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR Pfam; PF00179; UQ_con; 1.
DR SUPFAM; SSF102875; SSF102875; 1.
DR SUPFAM; SSF54495; SSF54495; 2.
DR PROSITE; PS50127; UBC_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Coiled coil; Membrane; Nucleotide-binding; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix; Ubl conjugation pathway.
FT CHAIN 1..1441
FT /note="Probable ubiquitin-conjugating enzyme E2 R521"
FT /id="PRO_0000243982"
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 1217..1380
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT REGION 180..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 283..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 505..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 577..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 63..89
FT /evidence="ECO:0000255"
FT COILED 340..368
FT /evidence="ECO:0000255"
FT COMPBIAS 180..201
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1306
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
SQ SEQUENCE 1441 AA; 165046 MW; 0F605583124D4F0A CRC64;
MHDYLGSFYN PLTLQKKLKY IHHIIINYIT NSILYFFLIM QSKNNPKHNS MKFKEQTESP
ILNQSKLVNT LDIIKDEINK WEEKNTDKDI KIVSIDNGKI VLSMVYGKQH IIEILCPKDY
PNVKSGFSCK EIKTVNTIPL SFISQANNQL KSKKNLSVHR IISHLSTTFQ NYKKALKSKV
SKDKMKDKSE SNSEHEQESK SVVSNEIPSE VSIDSKLTKD INFINDLIKE ANKCSNDVPS
DSDETHQEVD DRPLTEEVVV PDPTRIVRRR NSKLQTGSTK IKIFGKSKNS GPSSSKTSIS
SMSKVEELED KNPYLQEQDI MSIIQDEWNK VQESKSICPT TNEDNNDLDN LINEVERLVQ
ETKDQETKDQ ETKDQKEIWA SSLTIEEPNG ENFEEFSWEV PNETSQITVV EPVQEATEEP
VQNVTEELIQ LVADEPVQET VKDSVQEVAE ESVQETTVEA VQEIAEESVQ QVVEESVQET
TVEPVQEVAE EAVQQVVEES VQETTVEPVQ EVAEEPVQQE VAEEPVQQEV AEEPVQQEVA
EEPVQEVAEE PVQKATEELV QQEVAEDIVK LDVTVQNDFS DHSDSPEPSD SSDSEEEITN
SNNLGRYFKI YDPTTGKTTG VYVGKTPTQA ANKAFIKTFS NDNTGNKKEF YLQEYTGNKP
GKIYKYEGTR QKLNQPQKIS IPLYGDGQYK TITYNYKNTV VKKNVPDSIK NPPKTIKKSI
KPVKKSIKPV KKLSTTKLDS QTNSVKEKSE NKDIINYNDT GDKYGLYIDF GKFFKNSKIP
FDLEKLRDNA LKLSNQENQD DNYSTMKLRN FKNNNAVNLM INDFTKLYND GVKNGYNIEP
VNNNIYDLDI LLSSNFLDKD SVLYQDMINL KIDHIKINIK INHKMYPFYP PQVSLIRPTI
ENNVAAIIAT IDYLFANKWN PMISIVNIVN DIRNILNKYG ALDEKKYQNN LDPIFHDLVE
LSLLTGTQCS MYQSDQKVID LSNNSTNEKQ SKYWKKGTGF GHSGLSDWDF NQTKENIKNR
ELKIYQCLRK IVVKLTKIIL GKNQVDVINI LKESCFIPYL KLVFIDGSLF DLVKDLSYFE
LVLNSMRILT KEYLPLFLHK YNDKSLLEVL DQFNKDCHSY LNTLKNIKES DCQNEIDIIE
NFMSFYKRLS TSIEKFNEIT ESNNKEEVIS NDVKDLYKIT LGNEVFQEYN LDLNKFANML
TNDTKKEGLI HKDALKAISR ELLSHSKNLP VEYGSSIYYR YSPENIRYHE FIITGPEDSP
YDSGCFHFRM YNPSAYPNTS PFVSMTTTGH GSVRFNPNLY ADGKVCLSIL GTWRGQAGES
WIPGVSSMLQ VMISIQSLVL ISEPYFNEPG YESSRGTDKG NKLSTEYNQK VRFNCMKWAM
IDVIKNPVPG FESMIKKHFS IKAPHIKQVC QTWINEAPDN NKSEYQKLYD ELIGLLDSLV
A
