ID   KBTB2_ECTVM             Reviewed;         559 AA.
AC   Q9JFS4;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   23-FEB-2022, entry version 71.
DE   RecName: Full=Kelch repeat and BTB domain-containing protein 2;
GN   Name=KBTB2; OrderedLocusNames=C13R;
OS   Ectromelia virus (strain Moscow) (ECTV) (Mousepox virus).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus.
OX   NCBI_TaxID=265874;
OH   NCBI_TaxID=10090; Mus musculus (Mouse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Chen N., Danila M.I., Feng Z., Buller M.L., Wang C., Han X., Lefkowitz E.,
RA   Upton C.;
RT   "The genomic sequence of Ectromelia virus, the causative agent of
RT   mousepox.";
RL   Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH HOST CUL3, AND DOMAIN BTB
RP   AND KELCH.
RX   PubMed=18221766; DOI=10.1016/j.virol.2007.11.036;
RA   Wilton B.A., Campbell S., Van Buuren N., Garneau R., Furukawa M., Xiong Y.,
RA   Barry M.;
RT   "Ectromelia virus BTB/kelch proteins, EVM150 and EVM167, interact with
RT   cullin-3-based ubiquitin ligases.";
RL   Virology 374:82-99(2008).
CC   -!- FUNCTION: Probable substrate-specific adapter of CUL3-containing E3
CC       ubiquitin-protein ligases which mediate the ubiquitination and
CC       subsequent proteasomal degradation of host target proteins.
CC       {ECO:0000269|PubMed:18221766}.
CC   -!- SUBUNIT: Interacts (via BTB domain) with host CUL3.
CC       {ECO:0000269|PubMed:18221766}.
CC   -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000269|PubMed:18221766}.
CC   -!- DOMAIN: The BTB domain is responsible for the interaction with CUL3
CC       while the Kelch repeat domains supposely serve to recruit the cellular
CC       substrates. {ECO:0000269|PubMed:18221766}.
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DR   EMBL; AF012825; AAC99572.1; -; Genomic_DNA.
DR   RefSeq; NP_671686.1; NC_004105.1.
DR   SMR; Q9JFS4; -.
DR   GeneID; 951519; -.
DR   KEGG; vg:951519; -.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0039648; P:modulation by virus of host protein ubiquitination; IEA:UniProtKB-KW.
DR   GO; GO:0039649; P:modulation by virus of host ubiquitin-protein ligase activity; IEA:UniProtKB-KW.
DR   Gene3D; 2.120.10.80; -; 1.
DR   Gene3D; 3.30.710.10; -; 1.
DR   InterPro; IPR011705; BACK.
DR   InterPro; IPR000210; BTB/POZ_dom.
DR   InterPro; IPR015915; Kelch-typ_b-propeller.
DR   InterPro; IPR006652; Kelch_1.
DR   InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR   Pfam; PF07707; BACK; 1.
DR   Pfam; PF00651; BTB; 1.
DR   Pfam; PF01344; Kelch_1; 3.
DR   SMART; SM00225; BTB; 1.
DR   SMART; SM00612; Kelch; 3.
DR   SUPFAM; SSF117281; SSF117281; 1.
DR   SUPFAM; SSF54695; SSF54695; 1.
DR   PROSITE; PS50097; BTB; 1.
PE   1: Evidence at protein level;
KW   Host cytoplasm; Host-virus interaction; Kelch repeat;
KW   Modulation of host E3 ubiquitin ligases by virus;
KW   Modulation of host ubiquitin pathway by virus; Repeat;
KW   Ubl conjugation pathway.
FT   CHAIN           1..559
FT                   /note="Kelch repeat and BTB domain-containing protein 2"
FT                   /id="PRO_0000396129"
FT   DOMAIN          26..95
FT                   /note="BTB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT   DOMAIN          128..223
FT                   /note="BACK"
FT   REPEAT          305..352
FT                   /note="Kelch 1"
FT   REPEAT          353..399
FT                   /note="Kelch 2"
FT   REPEAT          401..463
FT                   /note="Kelch 3"
SQ   SEQUENCE   559 AA;  65192 MW;  B95EFD6DCF0439EF CRC64;
     MDIDDIKHNR RVVSNISSLL DNDILCDVII TIGDGEEIKA HKTILAAGSK YFRTLFTTPM
     IIRDLVTRVN LQMFDKDAVK NIVQYLYNRH ISSMNVIDVL KCADYLLIDD LVTDCESYVK
     DYTNHDTCIY IYHRLYEMSH IPIVKYVKRM VMRNIPTLIT TDAFKNAVFE ILLDIISTND
     GEYVYREGYK VTILLKWLDY NYITEEQLLC ILSCIDIQNL DKKSRLLLYS NTTINMYSSC
     VKFLLDNKQN RNIIPRQLCL VYHDTNYNIS NPCILVYNIN TMEYNTIYTI HNNIINYSSA
     VVDNEIIIAG GYNFNNISLN KVYKINIEHR TCVELPPMIK NRCHFSLAVI DDMIYAIGGQ
     NGTIVERSVE CYTMGDDTWK MLPDMPDAIS SYGMCVFDQY IYIIGGRTEH VKYIPVQHMN
     EIVDINEHSS DKVIRYDTVN NIWEKLPNLC SGTIRPSVVS HKDDIYVVCD IKDDEINGFK
     TCIFRYNTKD NYKGWELITT IDSKLTVLHT ILHDDAITIL HWYESCMIQD KFNIDTYKWT
     NICYQRSNSY IVHDTLPIY