UBC4_MIMIV
ID UBC4_MIMIV Reviewed; 1297 AA.
AC Q5UQ40;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 02-DEC-2020, entry version 96.
DE RecName: Full=Probable bifunctional E2/E3 enzyme R795;
DE Includes:
DE RecName: Full=E3 ubiquitin-protein ligase;
DE EC=2.3.2.27;
DE AltName: Full=RING-type E3 ubiquitin transferase;
DE Includes:
DE RecName: Full=Ubiquitin-conjugating enzyme E2;
DE EC=2.3.2.23;
DE AltName: Full=E2 ubiquitin-conjugating enzyme;
GN OrderedLocusNames=MIMI_R795;
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. Also acts as an E3 ubiquitin-protein ligase.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27;
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 -!- DOMAIN: The RING-type zinc finger domain mediates binding to an E2
CC ubiquitin-conjugating enzyme. {ECO:0000250}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the ubiquitin-
CC conjugating enzyme family. {ECO:0000305}.
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DR EMBL; AY653733; AAV51055.1; -; Genomic_DNA.
DR SMR; Q5UQ40; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000001134; Genome.
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:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd00195; UBCc; 1.
DR Gene3D; 3.10.110.10; -; 1.
DR Gene3D; 3.30.40.10; -; 2.
DR Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR003613; Ubox_domain.
DR InterPro; IPR000608; UBQ-conjugat_E2.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR024766; Znf_RING_H2.
DR Pfam; PF04564; U-box; 1.
DR Pfam; PF00179; UQ_con; 1.
DR Pfam; PF00092; VWA; 1.
DR Pfam; PF12678; zf-rbx1; 1.
DR SMART; SM00504; Ubox; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS51698; U_BOX; 1.
DR PROSITE; PS50127; UBC_2; 1.
DR PROSITE; PS50234; VWFA; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Metal-binding; Nucleotide-binding; Reference proteome;
KW Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..1297
FT /note="Probable bifunctional E2/E3 enzyme R795"
FT /id="PRO_0000309555"
FT DOMAIN 678..750
FT /note="U-box"
FT DOMAIN 899..1082
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 1133..1279
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT ZN_FING 74..128
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ACT_SITE 1217
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
SQ SEQUENCE 1297 AA; 150351 MW; BE177D02F78F6685 CRC64;
MEQIVTFGGI TIDNVSPDHI QQLYSVKLNG TSNNEEIPTE FPNIIQSVCS CDKHVVELTM
DVFKLVDTTE NSSCAICRYQ ENEPCIEHKS SESNTKCPIA QSVSCSHSFH ACCISRWLHT
KKTCPLCNIE WQLIGANNDS VVIYFDDKNQ EFKLSDNLVE DIGRQFGIDM DNYIVCKNKS
PVTEYKNSTY ALCTRDRHNS QNGQTNLKII CEFDSKTENL FIKYSTTIEE LRKLVSQTFD
LFKDQVKLIY NNIEISKDFD NLTVFNIGIK NDSNLAVECY KSFTYDMEIT NNFMVLYVPD
TFNTTNSSNN IQSVVSGSIA WIPQPFIDNV TNKDLRCLLS SLYILVKKVN LNTELIQSVT
DRFEKYMELY GMHYRQIKLA KDSLRCLLEM NHFNNKDRMI LSCTFYELID RIQRDNNINK
NPLLSSNLIC NLILSDKQVN EQTKINWKFL AKDVRITKVF NIYSPLVLTN SVPPLLTLNK
NLDVVVFTGK GKDVSLPIIL YDTLTNSETD VNAAELGKIV SDKGDLMMVD DRIYEEAIMV
CIDTSNSMSK ASDFDEDIKL KRSSIIETKN RFYEILKTES HSSPQESDIR QLTNTIIWFI
THPNFEDWYR KLYSQELIRS IACFEQKVYP NFAMMLVKYP WFFNKLLTSK KVVVNNTWYS
FIRNESNSNY NETKYSKEPL QEFLCPISHE IMEHPVVAKD GFTYEKSNIL KWFENKSTSP
MTNEKISKKI CDNKVLKSII RDWKENNTVI EQSDKLSVTI KLPDPWNETV IHYNETDNIW
DLIYQIYHIT GLSHDQYKLT SNYWAIDKSS LIKQISSKIK IHPFEKKMVD VKICDKTYFF
GTENTMTVSS FYTVGNLLYK LKSRKYHRYA VWYGLKDSGD GFQRGTILSP HDKLIDYSEM
TLEIHSSNRY KTPKGNHLSR LDVVKKLFDA YINRSIAYSF NTAIGLMSFS DKSVLECAIS
PFYESFREKV NELDTSGATA LYECLKDSIE NLIEWKNADL ENRSKAKLRI ICLTDGKDTG
LDKFKNTVKH KSQYHNVTID CILIGSDYDN YLGKIGEKTN GYVFNPSTIK YALDIMELET
MISSTNRKTI FYHNTIDEKT IPPIINPTKK LHAKAISPME IISKTNENTK LSQKLIRVQR
EIVDVMKNQH PDIDVYINEQ DISFWKIVFK GPDSTPYKNG TWLAYIQFTE EYPNIAPNIR
FVTPIKHCNI NNYGRVCHSI LDRNYTPNVK ISLILQCIYG LLLNPDVNDP LDTNLAMIYY
DANGLYEAQI IDYVNKFALK SREEWNQELA KNQFKNW
