ID   KBTB1_ECTVM             Reviewed;         563 AA.
AC   Q8JL69;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   02-JUN-2021, entry version 71.
DE   RecName: Full=Kelch repeat and BTB domain-containing protein 1;
GN   Name=KBTB1; OrderedLocusNames=EVM150;
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; AAM92455.1; -; Genomic_DNA.
DR   RefSeq; NP_671669.1; NC_004105.1.
DR   SMR; Q8JL69; -.
DR   GeneID; 951507; -.
DR   KEGG; vg:951507; -.
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   InterPro; IPR024182; Vaccinia_A55R.
DR   Pfam; PF07707; BACK; 1.
DR   Pfam; PF00651; BTB; 1.
DR   Pfam; PF01344; Kelch_1; 2.
DR   PIRSF; PIRSF003716; VAC_F3L; 1.
DR   SMART; SM00875; BACK; 1.
DR   SMART; SM00225; BTB; 1.
DR   SMART; SM00612; Kelch; 5.
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..563
FT                   /note="Kelch repeat and BTB domain-containing protein 1"
FT                   /id="PRO_0000396133"
FT   DOMAIN          21..88
FT                   /note="BTB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT   DOMAIN          123..219
FT                   /note="BACK"
FT   REPEAT          252..297
FT                   /note="Kelch 1"
FT   REPEAT          298..346
FT                   /note="Kelch 2"
FT   REPEAT          347..395
FT                   /note="Kelch 3"
FT   REPEAT          397..441
FT                   /note="Kelch 4"
FT   REPEAT          442..492
FT                   /note="Kelch 5"
FT   REPEAT          494..540
FT                   /note="Kelch 6"
SQ   SEQUENCE   563 AA;  64622 MW;  E1C4D7E8414EF993 CRC64;
     MNNSSELIAA INGFRNSGRF CDINIVINDE RINAHRLILS GASEYFSILF SSDFIDSNEY
     EVNLSHLDYQ SVNDLIDYIY GIPLSLTNDS VKYILSTADF LQIGSAITEC ENYILKNLCS
     RNCIDFYIYA DKYNNKKIET ASFNTILRNI LRLINDENFK YLTEESMIKI LSDDMLNIKN
     EDFAPLILIK WLESTQQPCT VELLRCLRIS LLSPQVIKSL YSHRLVSSIY ECITFLNNIA
     FLDESFPRYN SIELISIGIS NSRDKISINC YNRKKNTWEM ISSRGYRCSF AVAVMDNIIY
     MMGGYDQSPY RSSKVIAYNT CTNSWIYDIP ELKYPRSNCG GVVDDEYIYC IGGIRDQDSS
     LISDIDRWKP SKPYWQTYAK MREPKCDMGV AMLNGLIYVI GGVVKGGTCT DTLESLSEDG
     WMMHRRLPIK MSNMSTIVHA GKIYISGGYT NSSIVNEISN LVLSYNPIYD EWTKLSSLNI
     PRINPALWSV HNKLYVGGIS DDVQTNTSET YDKEKDCWTL DNGHVLPYNY IMYKCEPIKH
     KYPLEKIQYT NDFLKCLESF IGS