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Database: UniProt
Entry: A0A2H3J6T4_WOLCO
LinkDB: A0A2H3J6T4_WOLCO
Original site: A0A2H3J6T4_WOLCO 
ID   A0A2H3J6T4_WOLCO        Unreviewed;      1249 AA.
AC   A0A2H3J6T4;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Kinase-like protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=WOLCODRAFT_135720 {ECO:0000313|EMBL:PCH34449.1};
OS   Wolfiporia cocos (strain MD-104) (Brown rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Phaeolaceae; Wolfiporia.
OX   NCBI_TaxID=742152 {ECO:0000313|EMBL:PCH34449.1, ECO:0000313|Proteomes:UP000218811};
RN   [1] {ECO:0000313|EMBL:PCH34449.1, ECO:0000313|Proteomes:UP000218811}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MD-104 {ECO:0000313|EMBL:PCH34449.1,
RC   ECO:0000313|Proteomes:UP000218811};
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).
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DR   EMBL; KB467831; PCH34449.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2H3J6T4; -.
DR   STRING; 742152.A0A2H3J6T4; -.
DR   OMA; DDWDFIE; -.
DR   OrthoDB; 1441624at2759; -.
DR   Proteomes; UP000218811; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd05123; STKc_AGC; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR045270; STKc_AGC.
DR   PANTHER; PTHR24351:SF102; AGC PROTEIN KINASE; 1.
DR   PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR   Pfam; PF00069; Pkinase; 2.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000218811};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          470..771
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          772..879
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51285"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          104..136
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          240..294
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          315..350
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          415..462
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          815..1065
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1080..1228
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        104..126
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        415..441
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        442..462
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        815..842
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        852..878
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        879..897
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        986..1005
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1012..1038
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1087..1119
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1137..1206
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1249 AA;  134410 MW;  788022E1D96E60CD CRC64;
     MKNETTPAAQ SMPSQRRIPT QDGPWTVSVA DNPHDASAYS IYIKTPTHNM TLTRSALEIV
     ELHSKLRDAA PARRLPALPI DAAAIPAPPK RKSAFLNTLS RLASPANKAR PAHTQSQSSA
     ASSPHATPVA SPAAERGDPF ASALAGAADA ARANGGAHAN GHAHGTSVGL AAYLTTLAND
     SELRQARPWR RFVRVRTDDL QSVRVERAVK RVRSDLAAHV GAAGGAENTR SIGQVVFGNG
     EGEEEAPSVN GDGAGEEDEG EGAQTGETAQ VNGVHGKKSG PNGVVPNGVP NGAENEEVEN
     FAADAAIADA IAHGASDDGT VEEMDRAPTP RSPKPALAAE PGPSASVIPN GVDVHAAASG
     ANGAVPEDNE NENDVEEDAT APATPVLADM PAHAARIPRS QSADPTSRAQ RVFFEDGTSS
     RVSASHGTET PASSSADDTS DSATAVRKKR SKSADPRRAG SSRKVRIDDF EMLRVLGKGC
     AGKVLLVRHK PSAAVYALKA ITKRHVLAHQ ELQHTLTEQA VLKRMAGDGA VNPFVVKLHF
     SFHDKENLFL VMDFHPGGDL ATQLARWGRL GRDRARFYAA EIVEGVEGLH AAGVIYRDLK
     PENILIAADG HIILTDFGLS KEFPRRTSPI TAPPTPSGFR GDFVAGSPSP AVPHWMKNDL
     PGGWVLSPND TTSTFCGTAE YLAPEVIQGQ PYSYEVDWWS FGTMLYEMLT GITPFWANNH
     SDMYYRVLQD ELQFPEDRTM DQDTKSLIRG LLQRAPALRM KEPRIKKHPY FSMIDWSHVY
     YKRYIPPYIP PIDPSNASDT QNFDDTFLDM EPVINDENEN DHTDTDQEGQ TDSERADEED
     GANTPSQSRS PSAHLDDDES VDVFDGYSFK GRHSIIMDDE EDDGDEEDED EEEGVSPSTA
     STDDIEATEE PAKPAEPSTD VVEVAEPSAA PVEEITEPKT PEARPSTALP EPTSPSSPAE
     EKAPSVARKP SVRHSEEVTV IEAPPAAPLA PEPEEIKPVK APPKVQPRPN AGRQRGRREK
     SGIPALDRDL SDAHDESEPT TEREDDEWDF VEAEATTERN GAKGTSLFAR GVVDRYKLAV
     FRKSTPRRTS AARNFLGPST ESELTSPIES PTSPDKQRRG RTPGLTFRKH PKQFLRQRSP
     HSTLTSPSLK TLSNSASNTL TASSSGLLTP TTSTQAMTPS LRSKESATSV GSPSESSDTS
     INGDAKANGD HTIKAHSSIS VDDDKQKSKV LKKYKEGAEK VLSIFQSPR
//
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