ID K1X3P4_MARBU Unreviewed; 504 AA.
AC K1X3P4;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=Cyclin-like domain-containing protein {ECO:0000259|SMART:SM00385};
GN ORFNames=MBM_01574 {ECO:0000313|EMBL:EKD19622.1};
OS Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS spot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Drepanopezizaceae; Drepanopeziza.
OX NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD19622.1, ECO:0000313|Proteomes:UP000006753};
RN [1] {ECO:0000313|EMBL:EKD19622.1, ECO:0000313|Proteomes:UP000006753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MB_m1 {ECO:0000313|EMBL:EKD19622.1,
RC ECO:0000313|Proteomes:UP000006753};
RX PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA Huang M.-R., Wu R., Zhou Y.;
RT "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT evolution.";
RL BMC Genomics 13:382-382(2012).
CC -!- SIMILARITY: Belongs to the cyclin family.
CC {ECO:0000256|RuleBase:RU000383}.
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DR EMBL; JH921430; EKD19622.1; -; Genomic_DNA.
DR RefSeq; XP_007289463.1; XM_007289401.1.
DR AlphaFoldDB; K1X3P4; -.
DR STRING; 1072389.K1X3P4; -.
DR GeneID; 18757509; -.
DR KEGG; mbe:MBM_01574; -.
DR eggNOG; KOG0834; Eukaryota.
DR HOGENOM; CLU_038278_0_0_1; -.
DR InParanoid; K1X3P4; -.
DR OMA; GITWIDN; -.
DR OrthoDB; 1332948at2759; -.
DR Proteomes; UP000006753; 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; cd20546; CYCLIN_SpCG1C_ScCTK2-like_rpt2; 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:SF112; CTD KINASE SUBUNIT BETA; 1.
DR PANTHER; PTHR10026; CYCLIN; 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:UP000006753}.
FT DOMAIN 118..217
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
FT DOMAIN 230..316
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
FT REGION 368..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..410
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 504 AA; 57681 MW; EF1DB6545349D5C4 CRC64;
MDTITPELGS KLSSLYSRYY QTPSTLGSRG DENFPDLDFQ QYQLWQYGPY SGPRVVIRIE
KRRRKMAPAV VPESRIGPHP SYIHVAQVFM FQQQLNGMMM ALGTNPTRED TFRLQGVQWI
NDVRTALQLP IRTFCTASHY YHRFRMQHKD NEYQFHDAAA AALLTACKIE DTLKKSREIL
CAAHNLTKSP AEYLSPDDST FEASSRIVIG LERLMLESSG FDFRVRYPHK HIIKLGKEAG
IEKDVSRVAY NMMLDLYRTF APLKQSCSTM AFACIELSTL LLEKQQSAIR GERSPKYRKW
GTTRTEIIET ILDLLDLYTH FPKFNIVGAD HNVDKFFRLR ITINKEMEES SLKRYTEHQE
IRRINGVKPN VKTPKTPATP ASPADTRVNG MDVASPVTLS PRSSGSARRG TGARGQEGTV
RFMLDSDQAK REKDVTAEYF KTEYEEYEVE IEEPIKAKVD ERERPRHDGP RHGFGRGGGG
YDRGRGGFDR GGGGYNHHKR VRKY
//