ID A0A167LLJ2_CALVF Unreviewed; 848 AA.
AC A0A167LLJ2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Cc.Cdc5 protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=CALVIDRAFT_555553 {ECO:0000313|EMBL:KZO95816.1};
OS Calocera viscosa (strain TUFC12733).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Calocera.
OX NCBI_TaxID=1330018 {ECO:0000313|EMBL:KZO95816.1, ECO:0000313|Proteomes:UP000076738};
RN [1] {ECO:0000313|EMBL:KZO95816.1, ECO:0000313|Proteomes:UP000076738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TUFC12733 {ECO:0000313|EMBL:KZO95816.1,
RC ECO:0000313|Proteomes:UP000076738};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- SIMILARITY: Belongs to the CEF1 family.
CC {ECO:0000256|ARBA:ARBA00010506}.
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DR EMBL; KV417287; KZO95816.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A167LLJ2; -.
DR STRING; 1330018.A0A167LLJ2; -.
DR OrthoDB; 131128at2759; -.
DR Proteomes; UP000076738; Unassembled WGS sequence.
DR GO; GO:0000974; C:Prp19 complex; IEA:InterPro.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IEA:InterPro.
DR CDD; cd00167; SANT; 1.
DR CDD; cd11659; SANT_CDC5_II; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 2.
DR InterPro; IPR047242; CDC5L/Cef1.
DR InterPro; IPR021786; Cdc5p/Cef1_C.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR047240; SANT_CDC5L_II.
DR PANTHER; PTHR45885; CELL DIVISION CYCLE 5-LIKE PROTEIN; 1.
DR PANTHER; PTHR45885:SF1; CELL DIVISION CYCLE 5-LIKE PROTEIN; 1.
DR Pfam; PF11831; Myb_Cef; 1.
DR Pfam; PF13921; Myb_DNA-bind_6; 1.
DR SMART; SM00717; SANT; 2.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR PROSITE; PS51294; HTH_MYB; 2.
DR PROSITE; PS50090; MYB_LIKE; 2.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW mRNA splicing {ECO:0000256|ARBA:ARBA00023187};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000076738};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Spliceosome {ECO:0000256|ARBA:ARBA00022728}.
FT DOMAIN 3..58
FT /note="HTH myb-type"
FT /evidence="ECO:0000259|PROSITE:PS51294"
FT DOMAIN 3..54
FT /note="Myb-like"
FT /evidence="ECO:0000259|PROSITE:PS50090"
FT DOMAIN 55..104
FT /note="Myb-like"
FT /evidence="ECO:0000259|PROSITE:PS50090"
FT DOMAIN 59..108
FT /note="HTH myb-type"
FT /evidence="ECO:0000259|PROSITE:PS51294"
FT REGION 115..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 234..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 395..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 436..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 781..844
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 127..154
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..281
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 848 AA; 94522 MW; 40BDF667CD059994 CRC64;
MVRTIIKGGV WQNTEDEVLK AAIAKYGKNQ WARISSLLVR KTPKQCKARW YEWLDPSIKK
TEWSKTEDEK LLHLAKLMPT QWRTIAPIVG RTATQCLERY QKLLDDAEAK ENEELGLAGP
GAEAGPAEDI RKLRPGEIDP DPETKPARPD PIDMDEDEKE MLSEARARLA NTQGKKAKRK
ARERQLEEAR RLAMLQKKRE LKAAGIIMRL KTKKKGMDYN ADIPFEKAPA AGFYDTSDEQ
SKTYSAPVGQ SLRRLEGKRK PEEEEAERKK RQRRDAEKKG TPQHQTQFVA ARDAQIQKLK
EAEQIQKRRK LDLPAAQVGE VELEQIVKIG QAGESARALV AGESDGASGQ LLGEYEGLAQ
ARMARTPRTA PQEDTIMAEA RNLRNMTQAQ TPLLGEENTP MHGPDAPGTG FEGATPRRSV
NYTPNPLLTP RESAALDAST TPRTEVGTTY GQTPLRTPMR DTLNINASED ASVYGLTPRL
RRGQLTSAKR SLQQGFMSLP APKNDFEVMI PDDDEEEETG DGVVLTEEDA AERDARLQRR
REEEERRALA RRSIVVQKGL PRPPNVNASQ VLQQLLSEYS DEDENAAVER LIDTEMVMLM
KHDSVAHPVA GTTTAGGTRS SYVQPDDAAM AWARDAVHQE LAETLGFPGA NDDHIKNMVI
MLSADEEKET RDIGWSKIKE ELCYDVKTQT WVPKESLSPA DRVEGMSALL ETYRDQVNKE
GAKAGKAEKK LAVTLGGYQA RFAALSKRVG DAFTELQKTN GDLETFSALA AQEAINGPRR
LESLKEEVDK LERREKNLQG RYQELDEARR ESLARIAALE EKMLADAEAA NDAAMAELDG
VAEDVEMS
//
