ID M2R7V0_CERS8 Unreviewed; 844 AA.
AC M2R7V0;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 13-SEP-2023, entry version 44.
DE RecName: Full=Cc.Cdc5 protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=CERSUDRAFT_117334 {ECO:0000313|EMBL:EMD34487.1};
OS Ceriporiopsis subvermispora (strain B) (White-rot fungus) (Gelatoporia
OS subvermispora).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Gelatoporiaceae; Gelatoporia.
OX NCBI_TaxID=914234 {ECO:0000313|EMBL:EMD34487.1, ECO:0000313|Proteomes:UP000016930};
RN [1] {ECO:0000313|EMBL:EMD34487.1, ECO:0000313|Proteomes:UP000016930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B {ECO:0000313|EMBL:EMD34487.1,
RC ECO:0000313|Proteomes:UP000016930};
RX PubMed=22434909; DOI=10.1073/pnas.1119912109;
RA Fernandez-Fueyo E., Ruiz-Duenas F.J., Ferreira P., Floudas D.,
RA Hibbett D.S., Canessa P., Larrondo L.F., James T.Y., Seelenfreund D.,
RA Lobos S., Polanco R., Tello M., Honda Y., Watanabe T., Watanabe T.,
RA Ryu J.S., Kubicek C.P., Schmoll M., Gaskell J., Hammel K.E., St John F.J.,
RA Vanden Wymelenberg A., Sabat G., Splinter BonDurant S., Syed K.,
RA Yadav J.S., Doddapaneni H., Subramanian V., Lavin J.L., Oguiza J.A.,
RA Perez G., Pisabarro A.G., Ramirez L., Santoyo F., Master E., Coutinho P.M.,
RA Henrissat B., Lombard V., Magnuson J.K., Kuees U., Hori C., Igarashi K.,
RA Samejima M., Held B.W., Barry K.W., LaButti K.M., Lapidus A.,
RA Lindquist E.A., Lucas S.M., Riley R., Salamov A.A., Hoffmeister D.,
RA Schwenk D., Hadar Y., Yarden O., de Vries R.P., Wiebenga A., Stenlid J.,
RA Eastwood D., Grigoriev I.V., Berka R.M., Blanchette R.A., Kersten P.,
RA Martinez A.T., Vicuna R., Cullen D.;
RT "Comparative genomics of Ceriporiopsis subvermispora and Phanerochaete
RT chrysosporium provide insight into selective ligninolysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:5458-5463(2012).
CC -!- SIMILARITY: Belongs to the CEF1 family.
CC {ECO:0000256|ARBA:ARBA00010506}.
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DR EMBL; KB445803; EMD34487.1; -; Genomic_DNA.
DR AlphaFoldDB; M2R7V0; -.
DR STRING; 914234.M2R7V0; -.
DR HOGENOM; CLU_009082_0_0_1; -.
DR OrthoDB; 131128at2759; -.
DR Proteomes; UP000016930; 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:UP000016930};
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 112..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 429..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 508..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 778..841
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 128..162
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..282
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..537
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 844 AA; 94100 MW; 178C8788E40C3432 CRC64;
MVRIIIKGGV WKNTEDEVLK AAIAKYGKNQ WARISSLLVR KTPKQCKARW YEWLDPSIKK
TEWSKEEDEK LLHLAKLMPT QWRTIAPIVG RTATQCLERY QKLLDEAEAK ENEELGLAGP
GGEAGPSADD VRRLRPGEID PDPETKPARP DPIDMDEDEK EMLSEARARL ANTQGKKAKR
KARERQLEEA RRLAVLQKKR ELKAAGIIMR HKTKKKGMDY NADIPFEKKP AAGFYDTADE
QARETTAPVG QSLRRLENKR KPDAEEEERK KRQRRSGKEG NEAPHQTKFV AARDAQIQKL
KEAESIGRRR KLVLPAAQVG EAELEEIVKI GQAGEEAKAL VAGGNEATNR LLSDYDGLEK
ARMAKTPRTA AQHDNVMAEA RNLRNMTIQQ TPLLGDENTP LHVGPGGGTG FEGATPRHQV
AFTPNPLATP LHPGGDPSAT PRDVQATPGS AIGRTPVRDT LSINPNEGFS GVGATPREQR
IHMNSAKRAL KNAFMSLPKP ENNFELLVPE DEEDEETAES RRIAEEDAEE RDARLRRQRE
EEERKALARR SQVVQRGLPR PPMVDVERLL ANLTMEDGVP SDVAAAENLV HAEMVDLLRH
DSIAHPIPGT SIPGGTMSHY QIPVDEDIAA AQAAIHNELA STIGYQDANE EQIKEGLAAL
SKLEEIDETV SWAHIRPQLA FDTTTRIWVD PETLSEEARI TGYGALLEEC REAMAKEASK
AAKSEKKLNV TLGGYQARSK ALVKRITDAF DEMQKSKIEY ESFLQLRTNE SATGPARVSA
LKEEVEKLER RERLLQERYA ELDHERRDAA ERVAALEEKV MAEAEALNEA ALAEMETQEV
AVEA
//
