KBTB2_CWPXG
ID KBTB2_CWPXG Reviewed; 557 AA.
AC O72756;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Kelch repeat and BTB domain-containing protein 2;
GN Name=KBTB2; OrderedLocusNames=B19R;
OS Cowpox virus (strain GRI-90 / Grishak) (CPV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus.
OX NCBI_TaxID=265871;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
OH NCBI_TaxID=9685; Felis catus (Cat) (Felis silvestris catus).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9785; Loxodonta africana (African elephant).
OH NCBI_TaxID=29092; Microtus agrestis (Short-tailed field vole).
OH NCBI_TaxID=10090; Mus musculus (Mouse).
OH NCBI_TaxID=447135; Myodes glareolus (Bank vole) (Clethrionomys glareolus).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Shchelkunov S.N., Safronov P.F., Totmenin A.V., Miheev M.V.,
RA Ryazankina O.I., Petrov N.A., Gutorov V.V., Kotwal G.J., Sandakhchiev L.S.;
RT "Structure-function and organization of cowpox virus strain GRI-90 complete
RT genome.";
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBUNIT: Interacts (via BTB domain) with host CUL3. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000250}.
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:0000250}.
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DR EMBL; X94355; CAD90745.1; -; Genomic_DNA.
DR SMR; O72756; -.
DR PRIDE; O72756; -.
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 3: Inferred from homology;
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..557
FT /note="Kelch repeat and BTB domain-containing protein 2"
FT /id="PRO_0000396132"
FT DOMAIN 26..95
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT DOMAIN 133..223
FT /note="BACK"
FT REPEAT 305..352
FT /note="Kelch 1"
FT REPEAT 353..399
FT /note="Kelch 2"
FT REPEAT 401..464
FT /note="Kelch 3"
SQ SEQUENCE 557 AA; 64913 MW; FC7CD74C0B7553D7 CRC64;
MDIENDIRNR RIIRNISNLL DDDILCDVII TIGDGEEIKA HKTILAAGST YFKTMFTTPM
IARDLVTRVN LQMFDKDAVK NIVQYLYNRH ISSMNVIDVL KCADYLLIDD LVADCESYIK
DYINHDTCIY MYHKLYEMVH IPIVKYIKRM LMSNIPTLIT TDAFKKTVFE ILFDIISTND
NVYLYREGYK VTILLKWLEY NHITEEQLLC ILSCIDIQNL DKKSRLLLYS NKTINMYPSC
IQFLLDNKQN RNIIPRQLCL ACHDTNYNVC NPCILVYNIN TMEYSVISTI PNHIINYASA
IVDNEIIIAG GYNFNNPSLN KVYKINIENK IHVELPPMIK NRCRFSLAVI DDTIYAIGGQ
NGTNVERTIE CYTLGDDKWK MLPDMPIALS SYGMCVLDQY IYIIGGRTQH IDYTSVHTVN
SIDMEEDTNI SNKVIRYDTV NNIWETLPNF WTGTINPGVV SHKDDIYVVC DIKDEKNVKT
CIFRYNTNTY NGWELVTTTE SRLSALHTIL HDNTIMMLHC YESYMLQDTF NVYTREWNHM
CHQHSNSYIM HNILPIY