(data stored in ACNUC7421 zone)

SWISSPROT: Q4WNL6_ASPFU

ID   Q4WNL6_ASPFU            Unreviewed;       364 AA.
AC   Q4WNL6;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   11-DEC-2019, entry version 82.
DE   RecName: Full=Casein kinase II subunit beta {ECO:0000256|RuleBase:RU361268};
DE            Short=CK II beta {ECO:0000256|RuleBase:RU361268};
GN   ORFNames=AFUA_4G06180 {ECO:0000313|EMBL:EAL90168.1};
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=330879 {ECO:0000313|EMBL:EAL90168.1, ECO:0000313|Proteomes:UP000002530};
RN   [1] {ECO:0000313|EMBL:EAL90168.1, ECO:0000313|Proteomes:UP000002530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100
RC   {ECO:0000313|Proteomes:UP000002530};
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.,
RA   Fedorova N., Fedorova N., Feldblyum T.V., Fischer R., Fosker N., Fraser A.,
RA   Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B., Haas H., Harris D., Horiuchi H.,
RA   Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K.,
RA   Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafon A., Latge J.P.,
RA   Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y.,
RA   Molina M., Monod M., Mouyna I., Mulligan S., Murphy L., O'Neil S.,
RA   Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
RA   Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H.,
RA   Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M.,
RA   Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D.,
RA   Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G.,
RA   Vazquez de Aldana C.R., Weidman J., White O., Woodward J., Yu J.H.,
RA   Fraser C., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.,
RA   Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
CC   -!- FUNCTION: Plays a complex role in regulating the basal catalytic
CC       activity of the alpha subunit. {ECO:0000256|RuleBase:RU361268}.
CC   -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC       {ECO:0000256|RuleBase:RU361268}.
CC   -!- SIMILARITY: Belongs to the casein kinase 2 subunit beta family.
CC       {ECO:0000256|RuleBase:RU361268}.
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:EAL90168.1}.
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DR   EMBL; AAHF01000005; EAL90168.1; -; Genomic_DNA.
DR   RefSeq; XP_752206.1; XM_747113.1.
DR   STRING; 746128.CADAFUBP00006155; -.
DR   EnsemblFungi; EAL90168; EAL90168; AFUA_4G06180.
DR   GeneID; 3508920; -.
DR   KEGG; afm:AFUA_4G06180; -.
DR   EuPathDB; FungiDB:Afu4g06180; -.
DR   HOGENOM; HOG000039270; -.
DR   InParanoid; Q4WNL6; -.
DR   KO; K03115; -.
DR   OMA; PRTHCEQ; -.
DR   OrthoDB; 1335521at2759; -.
DR   Proteomes; UP000002530; Chromosome 4.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005956; C:protein kinase CK2 complex; IBA:GO_Central.
DR   GO; GO:0034456; C:UTP-C complex; IBA:GO_Central.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0019887; F:protein kinase regulator activity; IBA:GO_Central.
DR   GO; GO:0030291; F:protein serine/threonine kinase inhibitor activity; IBA:GO_Central.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; IBA:GO_Central.
DR   GO; GO:0035690; P:cellular response to drug; IBA:GO_Central.
DR   GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR   GO; GO:0006356; P:regulation of transcription by RNA polymerase I; IBA:GO_Central.
DR   Gene3D; 1.10.1820.10; -; 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   PANTHER; PTHR11740; PTHR11740; 1.
DR   Pfam; PF01214; CK_II_beta; 1.
DR   PRINTS; PR00472; CASNKINASEII.
DR   SMART; SM01085; CK_II_beta; 1.
DR   SUPFAM; SSF57798; SSF57798; 1.
DR   PROSITE; PS01101; CK2_BETA; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q4WNL6.
DR   SWISS-2DPAGE; Q4WNL6.
KW   Kinase {ECO:0000313|EMBL:EAL90168.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002530};
KW   Transferase {ECO:0000313|EMBL:EAL90168.1}.
FT   REGION          59..94
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          220..263
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          342..364
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        59..82
FT                   /note="Acidic"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        221..242
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   364 AA;  40675 MW;  716F1283D42DC5DA CRC64;
     MSSSEGAPES WISSFCSLMG HEFFAEVSED FIEDDFNLTG LQSQVPMYKE ALEMILDVEP
     EEDEDEEEEE EEEEEDDDEI LGDERPPGYR RAGDRRHARV ASDLSVIESS AELLYGLIHQ
     RYITSRPGIQ QMLEKYEMQH FGVCPRTYCN GSKVLPVGCS DTPGQETVKL FCPSCQDLYT
     PPNSRFHSVD GAFFGTTFGY LFFMTFPDLD IGPRLDPSML TAAPTNANNQ SRSSSLTSGV
     NRATPDLPPP PPNQPTEING VRTSNFCPGL GPGRIYESKI YGFRVSERSR VGPRMKWLRM
     KPADIRELDE LAQYEAIHGS ANDGGDTEMN IEAQNAAAIA ARKKAPMRRR RHHPDQMSIN
     GAEG
//

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