KBTB1_CAMPS
ID KBTB1_CAMPS Reviewed; 564 AA.
AC Q8QQ16;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=Kelch repeat and BTB domain-containing protein 1;
GN Name=KBTB1; OrderedLocusNames=CMP172R;
OS Camelpox virus (strain CMS).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus.
OX NCBI_TaxID=203172;
OH NCBI_TaxID=9836; Camelus.
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11907336; DOI=10.1099/0022-1317-83-4-855;
RA Gubser C., Smith G.L.;
RT "The sequence of camelpox virus shows it is most closely related to variola
RT virus, the cause of smallpox.";
RL J. Gen. Virol. 83:855-872(2002).
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; AY009089; AAG37674.1; -; Genomic_DNA.
DR SMR; Q8QQ16; -.
DR Proteomes; UP000107153; 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; 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 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..564
FT /note="Kelch repeat and BTB domain-containing protein 1"
FT /id="PRO_0000396134"
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..539
FT /note="Kelch 6"
SQ SEQUENCE 564 AA; 64732 MW; 3906AF06A9E55E36 CRC64;
MNNSSELIAV INGFRNSGRF CDIDIVINDE RINAHRLILS GASEYFSILF SSDFIDSNKY
EVNLSHLDYQ SVNDLIDYIY GIPLSLTNDI VKYILSTADF LQIGSAITEC ENYILKNLCS
RNCIDFYIYA DKYNNKKIET ASFNTILLNI LRLINDENFK YLTEESMIKF LSDDMLNIKN
EDFAPLILIK WLESTQQPCT VELLRCLRIS LLSPQVIKSL YSHRLVGSIY ECITFLNNIS
FLDESFPRYH SIELISIGIS NSHDKISINC YNRKKNTWDI ISSRRYRCSF AVAVLDNIIY
MMGGYDQSPY RSSKVIAYNT CTNSWIYDIP ELKYPRSNCG GVADDEYIYC IGGIRDQDSS
LISSIDRWKP SKPYWQTYAK IREPKCDMGV AMLNGLIYVI GGVVKGDTCT DTLESLSQDG
WMMHQRLPIK MSNMSTIVHA GKIYISGGYN NSSVVNGISN LVLSYNPIYD EWTKLSSLNI
PRINPALWSV HNKLYVGGGI SDDIQTNTSE TYDKEKDCWT LDNGHMLPRN YIMYKCEPIK
HKYPLEKTQY TNDFLKYLES FIGS