ID A0A395GSA8_9EURO Unreviewed; 757 AA.
AC A0A395GSA8;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Cyclin-like domain-containing protein {ECO:0000259|SMART:SM00385};
GN ORFNames=BO80DRAFT_427594 {ECO:0000313|EMBL:RAK98296.1};
OS Aspergillus ibericus CBS 121593.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448316 {ECO:0000313|EMBL:RAK98296.1, ECO:0000313|Proteomes:UP000249402};
RN [1] {ECO:0000313|EMBL:RAK98296.1, ECO:0000313|Proteomes:UP000249402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121593 {ECO:0000313|EMBL:RAK98296.1,
RC ECO:0000313|Proteomes:UP000249402};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KZ824455; RAK98296.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395GSA8; -.
DR STRING; 1448316.A0A395GSA8; -.
DR VEuPathDB; FungiDB:BO80DRAFT_427594; -.
DR OrthoDB; 5483352at2759; -.
DR Proteomes; UP000249402; 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; cd20335; BRcat_RBR; 1.
DR CDD; cd20554; CYCLIN_TFIIIB90_rpt2; 1.
DR Gene3D; 1.10.472.170; -; 1.
DR Gene3D; 1.10.472.10; Cyclin-like; 1.
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:SF4; TRANSCRIPTION FACTOR IIIB 90 KDA SUBUNIT; 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.
DR SUPFAM; SSF57783; Zinc beta-ribbon; 1.
PE 4: Predicted;
KW Activator {ECO:0000256|ARBA:ARBA00023159};
KW Reference proteome {ECO:0000313|Proteomes:UP000249402};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 142..224
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
FT DOMAIN 242..326
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 541..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..48
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..385
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..425
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..581
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..629
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..735
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 757 AA; 81926 MW; CCE95E338C2F5F83 CRC64;
MSVPRPGIRP PMPPKSGPRA PMGRLASLKP PNSTPIRRPQ PISRPQPTRP TTHPKTTTCP
NPGCPAPHIV EDDGQKVCSG CGTVISEANI VSEVTFGETS SGAAVVQGTF VGEDQSHVRS
YGPGFQRGGA ESREITEQNG NRYITQLSRA LMIPESAMKA AGQVFKLAVG LNFIQGRRTK
TVAAVCLYIA CRRQDGNTVM LIDFADVLMI NVFKLGRTYK ALLDELRLGG NVFLMNPIDP
ESLIYRFAKQ LEFGSATMQV ASEAVRIVQR MNRDWMTTGR RPAGICGAAL ILAARMNNFR
RTVREVVYVV KVTEITISQR LNEFSSTESG ELTVDQFRSV QLENAHDPPS FARARDGRKP
SRSFKRRPTE TAAEIEGDVQ EAQQPRRVDS DGFAIPNLPI DPALIAASSG QRRQSTASTA
SEATSEAGEE AAKPGRHKGP KRPPLPAPSP DQIASEEALE NEMTALLSKG SNMIETGVGP
PRKVVSDNAE IDATEFESDP EVSNCLLSPA EVEIKERIWV HENKDYLRAQ QAKALKRALA
EADARPGADG RVHKPRKRRR GRLGDVAYLE GDGEDGDGRS TRASTPAEAT RRMLERRGFS
KKINYRLLES LFGEEGADEA SKSKEESLSR SQSRSQSVIS RRSASIEPEA APRGAGLAAS
LTTSQPIGGP VSSVAPVRGS TEHVTHTGAP ADQAGKVGQN EEVLGPADGA KNGYSDGEQE
DDYDEEDDME DDPDGVDAAF AGNYGDYYDE GSDYDSN
//
