ID A0A507FKQ2_9FUNG Unreviewed; 1643 AA.
AC A0A507FKQ2;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Cilia- and flagella-associated protein 251 {ECO:0000256|ARBA:ARBA00040994};
GN ORFNames=CcCBS67573_g02432 {ECO:0000313|EMBL:TPX76290.1};
OS Chytriomyces confervae.
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Chytridiomycetes; Chytridiales;
OC Chytriomycetaceae; Chytriomyces.
OX NCBI_TaxID=246404 {ECO:0000313|EMBL:TPX76290.1, ECO:0000313|Proteomes:UP000320333};
RN [1] {ECO:0000313|EMBL:TPX76290.1, ECO:0000313|Proteomes:UP000320333}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 675.73 {ECO:0000313|EMBL:TPX76290.1,
RC ECO:0000313|Proteomes:UP000320333};
RX PubMed=31209237; DOI=.1038/s41598-019-45128-9;
RA van de Vossenberg B.T.L.H., Warris S., Nguyen H.D.T.,
RA van Gent-Pelzer M.P.E., Joly D.L., van de Geest H.C., Bonants P.J.M.,
RA Smith D.S., Levesque C.A., van der Lee T.A.J.;
RT "Comparative genomics of chytrid fungi reveal insights into the obligate
RT biotrophic and pathogenic lifestyle of Synchytrium endobioticum.";
RL Sci. Rep. 9:8672-8672(2019).
CC -!- FUNCTION: Regulatory subunit of casein kinase II/CK2 (By similarity).
CC As part of the kinase complex regulates the basal catalytic activity of
CC the alpha subunit a constitutively active serine/threonine-protein
CC kinase that phosphorylates a large number of substrates containing
CC acidic residues C-terminal to the phosphorylated serine or threonine.
CC {ECO:0000256|ARBA:ARBA00029397}.
CC -!- SIMILARITY: Belongs to the casein kinase 2 subunit beta family.
CC {ECO:0000256|ARBA:ARBA00006941}.
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:TPX76290.1}.
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DR EMBL; QEAP01000051; TPX76290.1; -; Genomic_DNA.
DR STRING; 246404.A0A507FKQ2; -.
DR Proteomes; UP000320333; Unassembled WGS sequence.
DR GO; GO:0005956; C:protein kinase CK2 complex; IEA:InterPro.
DR GO; GO:0019887; F:protein kinase regulator activity; IEA:InterPro.
DR Gene3D; 2.20.25.20; -; 1.
DR Gene3D; 1.10.1820.10; protein kinase ck2 holoenzyme, chain C, domain 1; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 3.
DR InterPro; IPR016149; Casein_kin_II_reg-sub_N.
DR InterPro; IPR035991; Casein_kinase_II_beta-like.
DR InterPro; IPR000704; Casein_kinase_II_reg-sub.
DR InterPro; IPR026992; DIOX_N.
DR InterPro; IPR044861; IPNS-like_FE2OG_OXY.
DR InterPro; IPR027443; IPNS-like_sf.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR13720:SF13; CILIA- AND FLAGELLA-ASSOCIATED PROTEIN 251; 1.
DR PANTHER; PTHR13720; WD-40 REPEAT PROTEIN; 1.
DR Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR Pfam; PF01214; CK_II_beta; 1.
DR Pfam; PF14226; DIOX_N; 1.
DR Pfam; PF00400; WD40; 1.
DR PRINTS; PR00472; CASNKINASEII.
DR SMART; SM01085; CK_II_beta; 1.
DR SMART; SM00320; WD40; 11.
DR SUPFAM; SSF57798; Casein kinase II beta subunit; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 2.
DR PROSITE; PS01101; CK2_BETA; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000320333};
KW WD repeat {ECO:0000256|PROSITE-ProRule:PRU00221}.
FT REPEAT 402..443
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT DOMAIN 1495..1606
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT REGION 374..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1430..1449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1430..1444
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1643 AA; 181588 MW; 3E5D543B96891D54 CRC64;
MEQHKHVLAL NWTFGLNRSL VGGVHSLAEG SARKVLFYAS SHTGVLLDWT SGKQQLLQGH
CNEISATAVT SNKRWIVTAD KGENPVLIIW DTMPHMIHQN LANLVPGTAT GPPLLNALPI
KTMFDIHDGA GVVSCEFSSD SKYLVTLGNE LEQTIMIWSW TTESEEPLRK LVIHGEPQKS
VKINPEDPFE IVTTGTTTVN FITWDLEAGI EQHVPLLSSK DFLHNPAKFT YSMFIPNKGQ
AITATADGDV VVWANHSLNN LSSDLGKGKM ACVKFMKLHQ SAINYLTMIG STYIVTGGED
GTIKIFDMQL RLILWFEKMK AGAIMSVSFC STFTKPTESK DSIVSDLNIP EMIVSTRQSK
IMYMRKHGFR SEKPDANKAV VSRQASASGE ESNEGPEIEV LLETQFESVH ALAAHPKMKR
FAVGGHSGFL QVWDYANKSV VNSRIFEVPP PPEDPNNSHT TKNKTKAVVE RYKIESIAYS
ACGDILGIGF SDGTLRILDA ATLAEIDGQR SVSGDIMTPY YILAKPTAEK TETGNSVNKV
TFSPCGNYLA ASDSQHAVSL FKKEWKTGPK KAIEGVGKAV EKLASGDTYT VWTQIGKCKA
HYKEVISLHF IPPTQLEPTK TRLLSTSSDR HTAEYDVAAS SITRGIKLVS LKRIEQTARP
LAATWHPALR LNPQSQPPMS LAVAETNDSV SERLDATSVN NFTPTDTYVL TCNSDFKIRL
HNANTQLCRK TALGPTFGGN LRALCVVPDA SAGASDAAAA AAPIDADEPI HGSNTLSAQP
AAQTFNYVAY STFEKVVGLT KLPFDGNPHK FMGLIAHPCR VSNIVPTCDG LYLLTSGMHD
AAVHMWSINP AALEAQIALG GKDLEPFLDM LDETGAGESS PFYKEMEDYF YYAQLRSQGE
DAATTRLIQD TVNISEIPAI MQAMGFYPSE NDIENMINEV KYSAVAEGDI VEDITFPDLI
KLYINHRPVF DYSEADLLDA LGYAVKNQPG LSPEKKASLP ELTPDSIIGK EGLFSLLQQY
GETMTREDLL VSFRALLLND AVYNATLPEK FSGRQFVEEI MGLQPATDPE SSTYSESDVS
TAYWIEWFLS LKGNEFFCEI DEDYINDRFN LTGISADVPH YSEAFALMTD SLDEDIDALP
DSARMEMENA ARHLYGLIHQ RFIVTTRGLV KMFEKLRHAE FGRCPRVLCH NQAVLPIGLS
DVPGYRSVML YCPRCEDVYA PPSRRHAVID GAYFGTTFPH LLLQVYPQLM PTKPNDRYVP
KIFGFKVHAV ANEQRLQDEI RDEQKRRLTG GGGGGVIMTN NSHLYELDNA PTDTAPPELV
PIIDFSPFTA SGTSDHARAA TTAALAAAFS TSGFVYLKNH GIQQSVIDSI FSSSKSFFAL
PQAEKELVQW ECPESNRGYV AIGKEKLSDL DKEGRAEDIK SLNQESPDLK EAFDVREDRD
PNSPYKNRFP SPEFGTECMH LFHLLRDLNF KVMAALAEGL GLGAEYFDFS TRLGGNNTLR
LLHYPRVQAN EINDRSRRCG AHSDYGTVTF LLQDGVGGLE ILDPSSQRFV QVRPIPGTLI
VNIGDLLQRW TNDTLVSRMH RVVKPYTVDA DGFLPARYSI AYFCDPDEEV VVETIDKFVV
GEKKYAPVKA GEYLLARLSN TYF
//
