ID A1D761_NEOFI Unreviewed; 561 AA.
AC A1D761;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE SubName: Full=Cyclin, N-terminal domain protein, putative {ECO:0000313|EMBL:EAW21555.1};
GN ORFNames=NFIA_067220 {ECO:0000313|EMBL:EAW21555.1};
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117 {ECO:0000313|EMBL:EAW21555.1, ECO:0000313|Proteomes:UP000006702};
RN [1] {ECO:0000313|Proteomes:UP000006702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 /
RC NRRL 181 / WB 181 {ECO:0000313|Proteomes:UP000006702};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027690; EAW21555.1; -; Genomic_DNA.
DR RefSeq; XP_001263452.1; XM_001263451.1.
DR AlphaFoldDB; A1D761; -.
DR STRING; 331117.A1D761; -.
DR EnsemblFungi; EAW21555; EAW21555; NFIA_067220.
DR GeneID; 4590098; -.
DR KEGG; nfi:NFIA_067220; -.
DR VEuPathDB; FungiDB:NFIA_067220; -.
DR eggNOG; KOG0834; Eukaryota.
DR HOGENOM; CLU_022000_7_2_1; -.
DR OMA; FVIACCR; -.
DR OrthoDB; 4848277at2759; -.
DR Proteomes; UP000006702; Unassembled WGS sequence.
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 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:UP000006702};
KW Repressor {ECO:0000256|ARBA:ARBA00022491}.
FT DOMAIN 60..166
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
FT DOMAIN 179..266
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
FT REGION 279..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..328
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 474..503
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..545
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 561 AA; 62524 MW; DF8F9D72319C7782 CRC64;
MASAPSHSPE KRPLPAESNP VLHASQAQWL FTDEELTRTP SQLDGMKMEA EHTSRSKGVN
FITQVGIMLK LPQLTLATAA VYLHRFFMRY SMVDIPQRPG MHPYPIAATA LFLATKVEEN
VRRMRELVVA CCRVAQKQPN LVVDEQSKEF WKWRDTILHH EDLLLEALCF DLQLEQPYRI
LYDFICFFGV NENKPLRNAA WAFVNDSMFT VLCLQFNART IAAAALYAAA RHCDVGFPDD
DRGRAWWEQI DVDLTQVRRA CMRMAQLYEN NAMQKHSQYY PTTPILSDEG TEKTRIPHAG
SPANRPPAES YVTHGRKRSK EPEDSGEPRG DGSAPSNGER SPKRPRRELD AAPRGSSQDQ
QQSPSAPSSQ SLPNAGSPSS FSSQGRPHLN GQVPPSLPHP PTHHRHPHPL PPAPRPFPRR
DSDHHPPGGG KVAGPREADP IQQRIDEIVS QNMPSHGGPP VPPPPGAGAR IPNRRNSVDR
RGPDRYRGYD DPARRRRPSF GRRSQSFEEQ PPPPPGHPHH QPLPPPPPPP DIPQPPPPPP
PSQPEQAAQE DEGGGSEEGE L
//
