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Database: UniProt
Entry: R0GGI2_9BRAS
LinkDB: R0GGI2_9BRAS
Original site: R0GGI2_9BRAS 
ID   R0GGI2_9BRAS            Unreviewed;       575 AA.
AC   R0GGI2;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=Cyclin-like domain-containing protein {ECO:0000259|SMART:SM00385};
GN   ORFNames=CARUB_v10020048mg {ECO:0000313|EMBL:EOA34962.1};
OS   Capsella rubella.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Capsella.
OX   NCBI_TaxID=81985 {ECO:0000313|EMBL:EOA34962.1, ECO:0000313|Proteomes:UP000029121};
RN   [1] {ECO:0000313|Proteomes:UP000029121}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Monte Gargano {ECO:0000313|Proteomes:UP000029121};
RX   PubMed=23749190; DOI=10.1038/ng.2669;
RA   Slotte T., Hazzouri K.M., Agren J.A., Koenig D., Maumus F., Guo Y.L.,
RA   Steige K., Platts A.E., Escobar J.S., Newman L.K., Wang W., Mandakova T.,
RA   Vello E., Smith L.M., Henz S.R., Steffen J., Takuno S., Brandvain Y.,
RA   Coop G., Andolfatto P., Hu T.T., Blanchette M., Clark R.M., Quesneville H.,
RA   Nordborg M., Gaut B.S., Lysak M.A., Jenkins J., Grimwood J., Chapman J.,
RA   Prochnik S., Shu S., Rokhsar D., Schmutz J., Weigel D., Wright S.I.;
RT   "The Capsella rubella genome and the genomic consequences of rapid mating
RT   system evolution.";
RL   Nat. Genet. 45:831-835(2013).
RN   [2] {ECO:0000313|EMBL:EOA34962.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Schmutz J., Prochnik S., Nordborg M., Weigel D., Rokhsar D., Wright S.;
RT   "Genome sequencing of Capsella rubella.";
RL   Nat. Genet. 0:0-0(2013).
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DR   EMBL; KB870806; EOA34962.1; -; Genomic_DNA.
DR   EMBL; KB870806; EOA34963.1; -; Genomic_DNA.
DR   RefSeq; XP_006302064.1; XM_006302002.1.
DR   RefSeq; XP_006302065.1; XM_006302003.1.
DR   AlphaFoldDB; R0GGI2; -.
DR   STRING; 81985.R0GGI2; -.
DR   GeneID; 17894733; -.
DR   KEGG; crb:17894733; -.
DR   eggNOG; KOG1598; Eukaryota.
DR   OrthoDB; 5483352at2759; -.
DR   Proteomes; UP000029121; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0017025; F:TBP-class protein binding; IEA:InterPro.
DR   GO; GO:0070897; P:transcription preinitiation complex assembly; IEA:InterPro.
DR   CDD; cd20553; CYCLIN_TFIIIB90_rpt1; 1.
DR   CDD; cd20554; CYCLIN_TFIIIB90_rpt2; 1.
DR   Gene3D; 1.10.472.10; Cyclin-like; 2.
DR   Gene3D; 1.20.5.650; Single helix bin; 1.
DR   InterPro; IPR011665; BRF1_TBP-bd_dom.
DR   InterPro; IPR013763; Cyclin-like_dom.
DR   InterPro; IPR036915; Cyclin-like_sf.
DR   InterPro; IPR000812; TFIIB.
DR   InterPro; IPR013150; TFIIB_cyclin.
DR   PANTHER; PTHR11618:SF64; CYCLIN_BRF1-LIKE TBP-BINDING PROTEIN; 1.
DR   PANTHER; PTHR11618; TRANSCRIPTION INITIATION FACTOR IIB-RELATED; 1.
DR   Pfam; PF07741; BRF1; 1.
DR   Pfam; PF00382; TFIIB; 2.
DR   PRINTS; PR00685; TIFACTORIIB.
DR   SMART; SM00385; CYCLIN; 2.
DR   SUPFAM; SSF47954; Cyclin-like; 2.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000029121};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   DOMAIN          76..160
FT                   /note="Cyclin-like"
FT                   /evidence="ECO:0000259|SMART:SM00385"
FT   DOMAIN          178..265
FT                   /note="Cyclin-like"
FT                   /evidence="ECO:0000259|SMART:SM00385"
FT   REGION          342..391
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          452..477
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          507..575
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        345..373
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        374..391
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        456..471
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        514..534
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        535..549
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        557..575
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   575 AA;  64571 MW;  8DFB07368128C658 CRC64;
     MVWCNHCAKN VPGIRPFDGG LACDLCGRIL ENFNFSTDVT FVKNAAGQSQ ASGNIVKSVE
     SGSSSSRERR LGIATYELRN LKDALGIGDE KEDVVRMAAK IFEMAIDQNF TKGRRTELVL
     SSCLYLTCRE KKIPLLLIDF SSYLRVSVYE LGSVYLQLCE LLYLVENNNY EELVDPSIFI
     LRFVNSLLKG VDKQRKGEFE KTVRSIISSM KRDWMQTGRK PSGICGAAIY IAALSHGIMC
     SRADIAKMVH MCEATITKRL NEFANTEAAS LTVFKLEESE KILVDEREKI LRENPITSKP
     NSDKGVVNCK HKDLEPFAYG LCKSCHDKFI IISGGVVGGS DPPAFQRAEK ERMEKAAKED
     NEGGGIEKSE GETDWDAEAS DESGNLSDLD GDAEVDGCFL NEDEMIMTKI SWELENRPYL
     EEQAAKEAAL KKASEAFNAN CPEYARNLVE TSKASVIQSR KEKRQKRAEE ARNAPPPATA
     MEAVCRTLER KKLSRCINYG ALDELFGTSP SEKSPKKSRT ETVTEKKREE KEDHEIVEDE
     EDEEDYAAPY EMNADEKFYE DEVEEEEDGY DFGLY
//
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