ID Q2UL57_ASPOR Unreviewed; 368 AA.
AC Q2UL57;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE RecName: Full=Cyclin-like domain-containing protein {ECO:0000259|SMART:SM00385};
GN ORFNames=AO090003000541 {ECO:0000313|EMBL:BAE57708.1};
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516 {ECO:0000313|EMBL:BAE57708.1, ECO:0000313|Proteomes:UP000006564};
RN [1] {ECO:0000313|EMBL:BAE57708.1, ECO:0000313|Proteomes:UP000006564}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40 {ECO:0000313|Proteomes:UP000006564};
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
CC -!- FUNCTION: Component of the SRB8-11 complex. The SRB8-11 complex is a
CC regulatory module of the Mediator complex which is itself involved in
CC regulation of basal and activated RNA polymerase II-dependent
CC transcription. The SRB8-11 complex may be involved in the
CC transcriptional repression of a subset of genes regulated by Mediator.
CC It may inhibit the association of the Mediator complex with RNA
CC polymerase II to form the holoenzyme complex. The SRB8-11 complex
CC phosphorylates the C-terminal domain (CTD) of the largest subunit of
CC RNA polymerase II. {ECO:0000256|ARBA:ARBA00025278}.
CC -!- SUBUNIT: Component of the SRB8-11 complex, a regulatory module of the
CC Mediator complex. {ECO:0000256|ARBA:ARBA00011612}.
CC -!- SIMILARITY: Belongs to the cyclin family.
CC {ECO:0000256|RuleBase:RU000383}.
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DR EMBL; AP007155; BAE57708.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2UL57; -.
DR STRING; 510516.Q2UL57; -.
DR EnsemblFungi; BAE57708; BAE57708; AO090003000541.
DR VEuPathDB; FungiDB:AO090003000541; -.
DR HOGENOM; CLU_022000_7_2_1; -.
DR OMA; MYDMMKY; -.
DR OrthoDB; 4848277at2759; -.
DR Proteomes; UP000006564; Chromosome 2.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IEA:InterPro.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
DR CDD; cd20545; CYCLIN_SpCG1C-like_rpt1; 1.
DR CDD; cd20546; CYCLIN_SpCG1C_ScCTK2-like_rpt2; 1.
DR Gene3D; 1.10.472.10; Cyclin-like; 2.
DR InterPro; IPR013763; Cyclin-like_dom.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR043198; Cyclin/Ssn8.
DR InterPro; IPR006671; Cyclin_N.
DR PANTHER; PTHR10026; CYCLIN; 1.
DR PANTHER; PTHR10026:SF51; CYCLIN-K; 1.
DR Pfam; PF00134; Cyclin_N; 1.
DR PIRSF; PIRSF036580; Cyclin_L; 2.
DR SMART; SM00385; CYCLIN; 2.
DR SUPFAM; SSF47954; Cyclin-like; 2.
PE 3: Inferred from homology;
KW Activator {ECO:0000256|ARBA:ARBA00023159};
KW Cyclin {ECO:0000256|RuleBase:RU000383};
KW Reference proteome {ECO:0000313|Proteomes:UP000006564};
KW Repressor {ECO:0000256|ARBA:ARBA00022491}.
FT DOMAIN 60..166
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
FT DOMAIN 183..266
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
FT REGION 282..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..323
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..357
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 368 AA; 41856 MW; E9A13B130CA6FD87 CRC64;
MASTTSQPAE KQLVPAPSNP VLLATQAQWL FTDEELTRAP SQLDGMTLEA EHTSRSKGVN
FITQVGIMLK LPQLTIATAA VYLHRFFMRY SMVDLPQRPG MHPYPIAATA LFLSTKVEEN
VRRMRELVVA CCRVAQKQPN LVVDEQSKEF WKWRDTILHH EDLLLEALCF DLQLEQPYRI
LYDFICYFGV NENKPLRNAA WAFVNDSMFT VLCLQFSARN IAAAALYAAA RHCDVGFEDD
ASGRPWWEQV DVDLAQVRRA CTRMAQLYEN NAMQKHSQYY PTTPIFADEG GPPPRDRRNS
DRYREHEDPS RRRRSDLSST SRKSIDEQHP PPPPPPPPSD MPQNQQPPPP PPPPDQDEEG
GGSEEGEL
//
