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Database: UniProt
Entry: G7E7U6_MIXOS
LinkDB: G7E7U6_MIXOS
Original site: G7E7U6_MIXOS 
ID   G7E7U6_MIXOS            Unreviewed;      1001 AA.
AC   G7E7U6;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   Name=Mo05594 {ECO:0000313|EMBL:GAA98906.1};
GN   ORFNames=E5Q_05594 {ECO:0000313|EMBL:GAA98906.1};
OS   Mixia osmundae (strain CBS 9802 / IAM 14324 / JCM 22182 / KY 12970).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina; Mixiomycetes;
OC   Mixiales; Mixiaceae; Mixia.
OX   NCBI_TaxID=764103 {ECO:0000313|EMBL:GAA98906.1, ECO:0000313|Proteomes:UP000009131};
RN   [1] {ECO:0000313|Proteomes:UP000009131}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 9802 / IAM 14324 / JCM 22182 / KY 12970
RC   {ECO:0000313|Proteomes:UP000009131};
RX   PubMed=21478649; DOI=10.2323/jgam.57.63;
RA   Nishida H., Nagatsuka Y., Sugiyama J.;
RT   "Draft genome sequencing of the enigmatic basidiomycete Mixia osmundae.";
RL   J. Gen. Appl. Microbiol. 57:63-67(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001433};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 32 family.
CC       {ECO:0000256|ARBA:ARBA00009003}.
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:GAA98906.1}.
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DR   EMBL; BABT02000165; GAA98906.1; -; Genomic_DNA.
DR   RefSeq; XP_014567070.1; XM_014711584.1.
DR   AlphaFoldDB; G7E7U6; -.
DR   STRING; 764103.G7E7U6; -.
DR   GeneID; 26262952; -.
DR   eggNOG; KOG0612; Eukaryota.
DR   HOGENOM; CLU_299581_0_0_1; -.
DR   InParanoid; G7E7U6; -.
DR   OrthoDB; 1701665at2759; -.
DR   Proteomes; UP000009131; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:1901135; P:carbohydrate derivative metabolic process; IEA:UniProt.
DR   Gene3D; 3.90.550.20; -; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR007577; GlycoTrfase_DXD_sugar-bd_CS.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   PANTHER; PTHR24356:SF430; MYOTONIN-PROTEIN KINASE; 1.
DR   PANTHER; PTHR24356; SERINE/THREONINE-PROTEIN KINASE; 1.
DR   Pfam; PF04488; Gly_transf_sug; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009131};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        899..917
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          5..286
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          398..421
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          438..492
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          977..1001
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        398..420
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        452..470
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1001 AA;  111020 MW;  8BF3D212137E7CEF CRC64;
     MLDRLEVIKL LHRGDCGEVR LARATRSSQE SLLFAVKSVS RSHARKLSDQ LFPQHERQIL
     LLQLSERCPA ICRLLAADSD EQNLYLITEY CPGGDLGALL DTLGPEGVQT SWIRAWLHDT
     LAALTWLHAH SWVHRDLKPS NLLIAMTGQL RLTDFGSAAP LNPATGNVKR PFAEALVGTV
     DYISPHMLRA HQAAINRCQT QADEQSYGAE ADLWSLGVMM YEIIVGACPF YAEDVATTYD
     LILEDSEIRL PSHCSISQDG RDLLQLLLTR PGHAPPAHEL ARHPFVRFED PRSLDRFVPE
     HPVIDIANLS AYQSATKPST GIDFSAFFSS PGLSILRIAK ADTPTQSDEI EHADWAFVPS
     EDAWEEIGYR EPGETALPTI AHSPAWFVTP ARRSTISLSS LSRSKTTDSS TTSATKRQRR
     DMSAFSARHE MVQHAVLSTA QKRRPSTHME RNESASQDQG AHMLQSEESS IEGTELDDSP
     TRSRSASISL LSKSLGSSRH SRSLSDRSFT PLADFTNRSR QASQDRELPA QEPEFLNATF
     RYWQCGICWR SSTATSPRLG IFHGEFCDAI GAGTPRHSVI APRAAVFPPA ADDFPWPLTR
     LATSLHGIMV CSWRLAGIAT LLTALALLSI CRHRLVIVFS LASAYTFDLR TINEVGSLDD
     GLACNGTYCG SADSKSQQNN YVIPNVFHSI LLGPSYVMRP SWQVSLDSCR ALHPTAEFKM
     WTDESAAAFV AKEYPELLRT WLSYGQTIQR SNTLRYMLLA RLGGIYMDLD LACRVNLDPL
     RRLTLVTPPA TPTGRTNAFI AAIPNHPYMN ALVSALPVYN LEWFFPYATN MFSTGCLYFS
     AIDVALPAEV RRSMKILPGK AHRLSGHTFT PLFEHLGAST WHSWDSSVIM ALGHAVNSLM
     SLWLPLASVA IVAIFGWHMR SRSTMQRHVR FLPSPVTEKS AARRTSRRRQ RPMLALDLSA
     TRKIQFKWND KIVDLSARSG SSTPSSSGSD SSSIQAQKVL L
//
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