ID A0A167MF11_CALVF Unreviewed; 374 AA.
AC A0A167MF11;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KZO96646.1};
GN ORFNames=CALVIDRAFT_481164 {ECO:0000313|EMBL:KZO96646.1};
OS Calocera viscosa (strain TUFC12733).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Calocera.
OX NCBI_TaxID=1330018 {ECO:0000313|EMBL:KZO96646.1, ECO:0000313|Proteomes:UP000076738};
RN [1] {ECO:0000313|EMBL:KZO96646.1, ECO:0000313|Proteomes:UP000076738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TUFC12733 {ECO:0000313|EMBL:KZO96646.1,
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 cyclin family.
CC {ECO:0000256|RuleBase:RU000383}.
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DR EMBL; KV417283; KZO96646.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A167MF11; -.
DR STRING; 1330018.A0A167MF11; -.
DR OrthoDB; 5474295at2759; -.
DR Proteomes; UP000076738; Unassembled WGS sequence.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0044772; P:mitotic cell cycle phase transition; IEA:InterPro.
DR CDD; cd20512; CYCLIN_CLBs_yeast_rpt2; 1.
DR Gene3D; 1.10.472.10; Cyclin-like; 2.
DR InterPro; IPR039361; Cyclin.
DR InterPro; IPR013763; Cyclin-like_dom.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR046965; Cyclin_A/B-like.
DR InterPro; IPR004367; Cyclin_C-dom.
DR InterPro; IPR006671; Cyclin_N.
DR InterPro; IPR048258; Cyclins_cyclin-box.
DR PANTHER; PTHR10177:SF198; CYCLIN B; 1.
DR PANTHER; PTHR10177; CYCLINS; 1.
DR Pfam; PF02984; Cyclin_C; 1.
DR Pfam; PF00134; Cyclin_N; 1.
DR PIRSF; PIRSF001771; Cyclin_A_B_D_E; 1.
DR SMART; SM00385; CYCLIN; 2.
DR SMART; SM01332; Cyclin_C; 1.
DR SUPFAM; SSF47954; Cyclin-like; 2.
DR PROSITE; PS00292; CYCLINS; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Cyclin {ECO:0000256|ARBA:ARBA00023127, ECO:0000256|RuleBase:RU000383};
KW Reference proteome {ECO:0000313|Proteomes:UP000076738}.
FT DOMAIN 136..220
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
FT DOMAIN 230..344
FT /note="Cyclin C-terminal"
FT /evidence="ECO:0000259|SMART:SM01332"
FT DOMAIN 234..314
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..61
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 374 AA; 43176 MW; 076D09BD77CB5FEF CRC64;
MLAALEDAER RTPPPLVPSS DPEEAVERAV VARQLSPLST SPVRQEEEES ELEEEADEED
WVTLPSREHM KVMQELERVR KLVEEEIDPL DTTMVAEYTE EIFEYMNELE ASVMPSANYM
NSQTEIEWSM RTTLVDWLLQ VHLRYHMLPE TLWIAINIVD RFLSARVVSL VKLQLVGVTA
MFVAAKYEEI LAPSVDEFVF MTENGYTKDE ILKGERIILQ TLDFKVSNYC SPYSWVRRIS
KADDYDIHTR TLCKFLMEVT LLDERFLRAK PSMIAAVGMY VARRMLGGDW DDLFMFYSNY
TEHQLLPGAK FIVERLSAAD FESYYVCKKY ATKRFLKASV FARDWAKKHG KEMDRPVGNN
ALALDSEGGK LVAV
//
