KBTB2_HSPV
ID KBTB2_HSPV Reviewed; 547 AA.
AC Q0GNN1;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 29-SEP-2021, entry version 47.
DE RecName: Full=Kelch repeat and BTB domain-containing protein 2;
GN Name=KBTB2; OrderedLocusNames=HSPV197;
OS Horsepox virus (HSPV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX NCBI_TaxID=397342;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
OH NCBI_TaxID=9796; Equus caballus (Horse).
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MNR-76;
RX PubMed=16940536; DOI=10.1128/jvi.00945-06;
RA Tulman E.R., Delhon G., Afonso C.L., Lu Z., Zsak L., Sandybaev N.T.,
RA Kerembekova U.Z., Zaitsev V.L., Kutish G.F., Rock D.L.;
RT "Genome of horsepox virus.";
RL J. Virol. 80:9244-9258(2006).
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; DQ792504; ABH08310.1; -; Genomic_DNA.
DR SMR; Q0GNN1; -.
DR Proteomes; UP000111173; Genome.
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; 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; PF00651; BTB; 1.
DR Pfam; PF01344; Kelch_1; 2.
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..547
FT /note="Kelch repeat and BTB domain-containing protein 2"
FT /id="PRO_0000396130"
FT DOMAIN 20..89
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT REPEAT 295..342
FT /note="Kelch 1"
FT REPEAT 343..389
FT /note="Kelch 2"
FT REPEAT 391..454
FT /note="Kelch 3"
SQ SEQUENCE 547 AA; 63734 MW; B97C5035D047DFD7 CRC64;
MDIKNDIRNI SNLLDDDILC DVIITIGDGE EIKAHKTILA AGSTYFKTMF TTPMIARDLV
TRVNLQMFDK DVVKNIVQYL YNRHISSMNV IDVLKCADYL LINDLVTNCE SYIKDYINHD
IYHKLYEMVH IPIVKYIKRM LISNIPTLIT TNAFKKTVFE ILFDIISTND SVYLYREGYK
VTILLKWLEY NYITEEQLLC ILSCIDIQNL DKKSRLLLYS NKTINMHPSC IQFLLDNKQN
RNIIPHQLCL ACHDTNYNVC NPCIVVYNIN TMEYSVISTI PNHIINYASA IVDNDIIIAR
GYNFNNPSLN KVYKINIENK IHVELPPIIK NRCRFSLAVI DDTIYAIGGQ NGTNVERTIE
CYTMGDDKWK MLPNMPIALS SYGMCVLDQY IYIIGGRTQH IDYTSVHTVN SIDMEEDTNI
SNKVMRYDTV NNIWETLPNF WTGTINPGVV SHKDDIYVVC DIKDEKNVKT CIFRYNTNTY
NGWELVTTTE SRLSALHTIL YNNTIMMLHC YESYMLQDTF NVYTREWNHM CHQHSNSYIM
YNILPIY
