ID A0A0M8N5J6_9HYPO Unreviewed; 406 AA.
AC A0A0M8N5J6;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=CTD kinase subunit beta {ECO:0000313|EMBL:KOS20341.1};
GN ORFNames=ESCO_005330 {ECO:0000313|EMBL:KOS20341.1};
OS Escovopsis weberi.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Escovopsis.
OX NCBI_TaxID=150374 {ECO:0000313|EMBL:KOS20341.1, ECO:0000313|Proteomes:UP000053831};
RN [1] {ECO:0000313|EMBL:KOS20341.1, ECO:0000313|Proteomes:UP000053831}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA de Man T.J., Stajich J.E., Kubicek C.P., Chenthamara K., Atanasova L.,
RA Druzhinina I.S., Birnbaum S., Barribeau S.M., Teiling C., Suen G.,
RA Currie C., Gerardo N.M.;
RT "The genome of the fungus Escovopsis weberi, a specialized disease agent of
RT ant agriculture.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the cyclin family.
CC {ECO:0000256|RuleBase:RU000383}.
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:KOS20341.1}.
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DR EMBL; LGSR01000017; KOS20341.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M8N5J6; -.
DR STRING; 150374.A0A0M8N5J6; -.
DR OrthoDB; 1332948at2759; -.
DR Proteomes; UP000053831; Unassembled WGS sequence.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IEA:InterPro.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
DR Gene3D; 1.10.472.10; Cyclin-like; 1.
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:SF112; CTD KINASE SUBUNIT BETA; 1.
DR PANTHER; PTHR10026; CYCLIN; 1.
DR Pfam; PF00134; Cyclin_N; 1.
DR SMART; SM00385; CYCLIN; 1.
DR SUPFAM; SSF47954; Cyclin-like; 2.
PE 3: Inferred from homology;
KW Cyclin {ECO:0000256|RuleBase:RU000383};
KW Kinase {ECO:0000313|EMBL:KOS20341.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053831};
KW Transferase {ECO:0000313|EMBL:KOS20341.1}.
FT DOMAIN 64..162
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 363..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..406
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 406 AA; 45612 MW; BECB9C4AFF596BCC CRC64;
MTPPPRTDEP MAVNGNGASA RVGPHPGYIS SSNQYTTELN IRRMLKENGC DPAREDNYRL
QGVHLIDTVR EHLCLPVRTF DTACTYFHKF RLNFRDAEYN YQDAALASLF VACKVEDTIK
KSKDILAAAY NVKNPEKPAA SDDKIFESPG KIIIGLERLI LETIGFDFRT RYPQKLLVKV
VRGMLGAEEG RPFFATAYAM SIDMYKTFVP IKRTTFSMVM ALVELTARMT ETETGLAAVR
QFAAARRQYS RPVVLETMLD VLDLYVQHHK STRLGARFDL NRFMDIKIAL NAELERDALP
RHTHLGGNGG GGAASAVLDA GMRRTARSHD GTMRFVFDPD KAREEQETVR QYFHEEYDEV
EVEVEEAIPP PSQPARGGEA DARAAWRGHG HRDRGEHRRG GHGGPL
//
