ID G0S0H1_CHATD Unreviewed; 1844 AA.
AC G0S0H1;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Enzyme regulator-like protein {ECO:0000313|EMBL:EGS23332.1};
GN ORFNames=CTHT_0010000 {ECO:0000313|EMBL:EGS23332.1};
OS Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
OS (Thermochaetoides thermophila).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Thermochaetoides.
OX NCBI_TaxID=759272 {ECO:0000313|Proteomes:UP000008066};
RN [1] {ECO:0000313|EMBL:EGS23332.1, ECO:0000313|Proteomes:UP000008066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1495 / CBS 144.50 / IMI 039719
RC {ECO:0000313|Proteomes:UP000008066};
RX PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA Arumugam M., Bork P., Hurt E.;
RT "Insight into structure and assembly of the nuclear pore complex by
RT utilizing the genome of a eukaryotic thermophile.";
RL Cell 146:277-289(2011).
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}.
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DR EMBL; GL988037; EGS23332.1; -; Genomic_DNA.
DR RefSeq; XP_006691523.1; XM_006691460.1.
DR STRING; 759272.G0S0H1; -.
DR GeneID; 18255038; -.
DR KEGG; cthr:CTHT_0010000; -.
DR eggNOG; KOG0406; Eukaryota.
DR eggNOG; KOG2006; Eukaryota.
DR eggNOG; KOG3092; Eukaryota.
DR HOGENOM; CLU_002060_2_0_1; -.
DR OrthoDB; 121525at2759; -.
DR Proteomes; UP000008066; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005956; C:protein kinase CK2 complex; IEA:InterPro.
DR GO; GO:0034066; C:Ric1-Rgp1 guanyl-nucleotide exchange factor complex; IEA:InterPro.
DR GO; GO:0019887; F:protein kinase regulator activity; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR CDD; cd00570; GST_N_family; 1.
DR Gene3D; 2.20.25.20; -; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 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; 1.
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; IPR040079; Glutathione_S-Trfase.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR009771; Ribosome_control_1.
DR InterPro; IPR040096; Ric1.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR22746:SF10; GUANINE NUCLEOTIDE EXCHANGE FACTOR SUBUNIT RIC1; 1.
DR PANTHER; PTHR22746; RAB6A-GEF COMPLEX PARTNER PROTEIN 1; 1.
DR Pfam; PF01214; CK_II_beta; 1.
DR Pfam; PF13417; GST_N_3; 1.
DR Pfam; PF07064; RIC1; 1.
DR PRINTS; PR00472; CASNKINASEII.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SFLD; SFLDG00358; Main_(cytGST); 1.
DR SMART; SM01085; CK_II_beta; 1.
DR SUPFAM; SSF57798; Casein kinase II beta subunit; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 2.
DR PROSITE; PS01101; CK2_BETA; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000008066};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1358..1438
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT REGION 23..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1045..1086
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1178..1213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1274..1312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1498..1523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1780..1819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1276..1312
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1782..1803
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1844 AA; 206090 MW; AEC128137B5ECD95 CRC64;
MYWPLGAPRI YAISSSRNAD FRPIVSHDGL SQPDHPDQRS DANSHLYPDS AAPLDTSFSP
VTPVTPLTPG IKPVYDDQPE ENGSDLPDGP APLILPSREP IVALRMARLG QMFAVITATS
LTIWQTKPTV VLAIVVRSES SLKTYGTNIN LLLRPDSAIL VIHTSLGYLI TYSLATDQDS
RIYRPHFPNH TNVQRRRQTY AGEPGHAAPD QILWGPGEGS GVRDVSVRFR MVIKVDAGIE
SALALDDELV VATRKPAAVQ CIRWSPDSSG NQTSTELLSR AGWLEKKVTI KEMTHDRPMN
LSTWITSDGR AYAVQRLTPG QQDAGSNDSP SDPKKLFKGY CFHIPETEQD YAVRCMINAR
FSLIAVGCAN GVIRVYSARD YSGNIPPSHI HTLPVSAAVS GKLTSISYSP DGYCLFAGYE
KGWATWSVYG KLLFNSFSID HSIASANEEK WLLGVQDAAW IGGACDLLLA SREHEAVWLL
EMARSALTGC YNQANLFRTV LQSTSSIMVY RGYGLPDLTS ISAEPSLWHT TRIPSVYLLN
QWPIRCTAVS SDGRYVAVAG KRGLAHYSVN SGRWKTFSNE DMENEFQVRG GMCWYQNILV
AAVETNNRTF ELRLYSREAS LENGTVTFSL QMPAPVVLIT TTGEDSLLVY TYENLLYHYV
FTSTSGSVRL VEAGHIAFHG IVRSPARVRG LSWSLPDHQL LEGDPSQDVA HASVLFLVDG
KLVLLRPSYS EGNLKYDMRI IAHNVEYYMN MRDQPRSFET TSARLDQLMS PVRGRILDNS
LWLFDGDELK VWANIEHVFA AVSGESSREL PSAFSIASDF YPLSILLQKG IVLGVESDLI
QRRDINFSFF RFSIRTQLFL PDTLRFLLSA DRSVEALQLA QQYEHLEYFP HALEVLLHHV
LDEEVDANPT PTPEEALLPR VLSLLSSFKQ YLDIVVQCTR KTEVRSWRTL FAYLPPPQEL
FEESLQRGNL KTAGGYLLIL HTFDELATAS EQSVRLLSRA MLEEDWDLCK ELARFLAALD
DTGKTLREAM ELATARVQRG CDSEDGSVRN GFMSSLDPPS RGLDASSDGS LGGAGSGRVA
GTDSDADDAN IDALGFKFRQ TRQRHTSCSA PDQPPNLVEW RTRLFDLDEP VIMSEEEYKT
YFCWIDNVYS HRSTQPLKRG GGNATAYYYD CRLKGRPAGG SPSSSANKKA NEDDDNNPGP
PKKKRKRKSR PLNQCSVKVK LTHYLGGPGC SLESLLRDHD GGGLAPDSGP VKDALARGVT
GERPFWVMQR IVNHNGAKTG EERGKEQGDE ADGRDNKRRK ASDSTRHTHT LERSDEIKKC
SVLREFAARL QRARRRERGI WTPTGEAAKT VENRSQEAPV KFYSACFCPF SQRVWIALEV
KKLDYQYCEI YPLRKPKPTP LLEANPRGLV PAIREGDWAC SESSVILEYL EERPMPEKGG
AVPPLHPSDS RLRANCRLWI DFINTRIVPS FFNVIAASTE NIRQEGLRGG VPGQTLSKAK
PPSDLHACTP AQRRPPVSRS PEPLPLVSSV SAADTCSLLR VFASIVGLNV CNTDYMDEYG
TESDSDYTSY WRDWFISSRG NEYFCEIDEE YLTDRFNLTG LNTEVQYYQY ALDLVTDVFD
LDCDDEMREA IEKSARQLYG LVHARYIVTT RGLAKMLEKY KKADFGKCPR VMCHSHPLLP
MGLSDVPNVK PVKLYCAKCE DIYNPKSSRH ASIDGAYFGT SFHNILFQVY PALIPPKSVE
RYVPRVYGFK VHAAAALMRW QDQQREDMRR RLRKLEIDDG FKDGESDLED EEEDEDDLED
DEEQGQGQST RESNMQLAEY RGSGAISVAG ASSYAGETHM GSVA
//
