GenomeNet

Database: UniProt
Entry: R7RZP3_PUNST
LinkDB: R7RZP3_PUNST
Original site: R7RZP3_PUNST 
ID   R7RZP3_PUNST            Unreviewed;       840 AA.
AC   R7RZP3;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 64.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   ORFNames=PUNSTDRAFT_109351 {ECO:0000313|EMBL:EIN03585.1};
OS   Punctularia strigosozonata (strain HHB-11173) (White-rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Corticiales; Punctulariaceae; Punctularia.
OX   NCBI_TaxID=741275 {ECO:0000313|EMBL:EIN03585.1, ECO:0000313|Proteomes:UP000054196};
RN   [1] {ECO:0000313|Proteomes:UP000054196}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB-11173 SS5 {ECO:0000313|Proteomes:UP000054196};
RX   PubMed=22745431; DOI=10.1126/science.1221748;
RA   Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA   Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA   Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA   Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA   Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA   Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA   Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA   Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA   Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA   Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA   Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA   Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA   Hibbett D.S.;
RT   "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT   31 fungal genomes.";
RL   Science 336:1715-1719(2012).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. STE20 subfamily.
CC       {ECO:0000256|ARBA:ARBA00008874}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JH687561; EIN03585.1; -; Genomic_DNA.
DR   RefSeq; XP_007389242.1; XM_007389180.1.
DR   AlphaFoldDB; R7RZP3; -.
DR   GeneID; 18876228; -.
DR   KEGG; psq:PUNSTDRAFT_109351; -.
DR   eggNOG; KOG0578; Eukaryota.
DR   HOGENOM; CLU_000288_26_2_1; -.
DR   OMA; KDSQHAN; -.
DR   OrthoDB; 460351at2759; -.
DR   Proteomes; UP000054196; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd01093; CRIB_PAK_like; 1.
DR   CDD; cd06614; STKc_PAK; 1.
DR   Gene3D; 3.90.810.10; CRIB domain; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR000095; CRIB_dom.
DR   InterPro; IPR036936; CRIB_dom_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR033923; PAK_BD.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR48015:SF6; SERINE/THREONINE-PROTEIN KINASE CLA4-RELATED; 1.
DR   PANTHER; PTHR48015; SERINE/THREONINE-PROTEIN KINASE TAO; 1.
DR   Pfam; PF00786; PBD; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00285; PBD; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50108; CRIB; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EIN03585.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000054196};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          89..185
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          189..202
FT                   /note="CRIB"
FT                   /evidence="ECO:0000259|PROSITE:PS50108"
FT   DOMAIN          568..819
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          259..333
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          358..525
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        264..294
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        312..326
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        367..392
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        421..465
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         597
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   840 AA;  91286 MW;  2FCFA729E386EC29 CRC64;
     MAYSQALTPS RPAPPAPQRR ATEQSTLNSA GYNLNLAPAS PYANSPSNYL SSSSPYAANY
     SGIGGSPNRI SLAQQQQQGN HGGDSMNGFE VRSGTVSVKE EGGLASLLGW RPKWLVLTEQ
     QLEICKNQNA GTQSAIRLHD ISNVERTDLK PYCLLIEAKD KRIWLALKSD DELYGWQDDI
     YSRSPLMGVS NPTNFMHKVH VGFDPVSGAF TGMPEQWSKL LTKSAITRED YAKDPQAVLD
     VLEFYTDHQK REMEEMVGIP QSSIPLRAGS SASSTLAPGS AYSSSTSTLS PDPPARFNAG
     TGLGGISKDG RPSISRQDSA PPSVGTPLSS AARAAAEQVN GTYAGTISAA NGQIRPLGAG
     VGALQPSRPA PPRPLLTGTR PAPSPGQKPP VPDHTPSSAD LRARARAQGP PAAEGAQLPA
     RKDSLAEEQR QRQRDVDRIR ERERERERER ERERERERNY DEEEYIQRPP IVPSKSAPAN
     DTPANAPAHG PAGATAGPPP VKPLQPKKAP AVTVTPSQDD EGKSGVAAAA AALEKPKEKE
     KRISTMSEAQ IMDKLRSVVS ADDPKTLYSK IKKVGQGASG HVYVAKTLAT GKKVAIKEMD
     LSHQPRKELI VNEILVMKES QHPNIVNFLE SYLVKQDLWV VMEYMEGGAL TDIIENNTLE
     EDQISCICLE TCKGLGHLHS QHIIHRDIKS DNVLLDAHGR VKITDFGFCA KLTDQKSKRA
     TMVGTPYWMA PEVVKQKEYG AKVDIWSLGI MAIEMIENEP PYLDEEPLKA LYLIATNGTP
     TLKKPEDLSR ELKSFLSVCL CVDVKSRATA AELLDHEFLK KACALSGLAP LLRAKQKQGQ
//
DBGET integrated database retrieval system