ID V2X5Y9_MONRO Unreviewed; 416 AA.
AC V2X5Y9;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=RNA polymerase II holoenzyme cyclin-like subunit {ECO:0000256|ARBA:ARBA00014912};
GN ORFNames=Moror_5224 {ECO:0000313|EMBL:ESK89177.1};
OS Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS (Crinipellis roreri).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK89177.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK89177.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK89177.1,
RC ECO:0000313|Proteomes:UP000017559};
RX PubMed=24571091; DOI=10.1186/1471-2164-15-164;
RA Meinhardt L.W., Costa G.G.L., Thomazella D.P.T., Teixeira P.J.P.L.,
RA Carazzolle M.F., Schuster S.C., Carlson J.E., Guiltinan M.J.,
RA Mieczkowski P., Farmer A., Ramaraj T., Crozier J., Davis R.E., Shao J.,
RA Melnick R.L., Pereira G.A.G., Bailey B.A.;
RT "Genome and secretome analysis of the hemibiotrophic fungal pathogen,
RT Moniliophthora roreri, which causes frosty pod rot disease of cacao:
RT mechanisms of the biotrophic and necrotrophic phases.";
RL BMC Genomics 15:164-164(2014).
CC -!- SIMILARITY: Belongs to the cyclin family. Cyclin C subfamily.
CC {ECO:0000256|ARBA:ARBA00008638}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ESK89177.1}.
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; AWSO01000579; ESK89177.1; -; Genomic_DNA.
DR RefSeq; XP_007851517.1; XM_007853326.1.
DR AlphaFoldDB; V2X5Y9; -.
DR STRING; 1381753.V2X5Y9; -.
DR KEGG; mrr:Moror_5224; -.
DR HOGENOM; CLU_034754_5_0_1; -.
DR OrthoDB; 102875at2759; -.
DR Proteomes; UP000017559; 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; cd20513; CYCLIN_CCNC_rpt1; 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:SF7; CYCLIN-C; 1.
DR Pfam; PF00134; Cyclin_N; 1.
DR SMART; SM00385; CYCLIN; 2.
DR SUPFAM; SSF47954; Cyclin-like; 2.
PE 3: Inferred from homology;
KW Cyclin {ECO:0000256|RuleBase:RU000383};
KW Reference proteome {ECO:0000313|Proteomes:UP000017559}.
FT DOMAIN 47..141
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
FT DOMAIN 189..315
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
FT REGION 167..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 327..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 416 AA; 45876 MW; 149290A26D278832 CRC64;
MATDFWASSH YQRWIVDRAT LRQARADDLL YVDNPEQLDF LNIYFANVIS KLGKKLQLRQ
RVIATATVFF RRFYLKSSYC ETDPFLVIAA CCYVAAKAEE SPVHIKNVVS ESRTLFSHQY
GIKNFPSDNS KLAEMEFYLV DDLDCDLVVF HPYRTLLALC RKESGAGDTP HEAEAGEVGV
GISGDEGPRY WGSDGEKLEL SDGALQTAWF IINDTYRSEL CLLYPPHLIA IAAIYLTFIL
HVPTQATIAH LLPSRSASDA SPPPPLTEEP SQIQPRRSSR QHSVEAKKQQ DPISFLAGLN
VSMPHIATIA QEIVSLYCLW DRYKEDSSPD AGSSTKQRLR GSGSGSNSGS VSRAPSEDDG
SSVSSGGGES ESVVTQAVLT KLLMKMREQR LADLAHPANG KPVAVNKMLE RTQAAG
//
