ID A0A165TU87_9AGAM Unreviewed; 812 AA.
AC A0A165TU87;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Fungal-type protein kinase domain-containing protein {ECO:0000259|Pfam:PF17667};
GN ORFNames=NEOLEDRAFT_161770 {ECO:0000313|EMBL:KZT27186.1};
OS Neolentinus lepideus HHB14362 ss-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Gloeophyllales; Gloeophyllaceae; Neolentinus.
OX NCBI_TaxID=1314782 {ECO:0000313|EMBL:KZT27186.1, ECO:0000313|Proteomes:UP000076761};
RN [1] {ECO:0000313|EMBL:KZT27186.1, ECO:0000313|Proteomes:UP000076761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB14362 ss-1 {ECO:0000313|EMBL:KZT27186.1,
RC ECO:0000313|Proteomes:UP000076761};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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; KV425563; KZT27186.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165TU87; -.
DR STRING; 1314782.A0A165TU87; -.
DR InParanoid; A0A165TU87; -.
DR OrthoDB; 1609880at2759; -.
DR Proteomes; UP000076761; Unassembled WGS sequence.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR040976; Pkinase_fungal.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR PANTHER; PTHR38248:SF2; FUNK1 11; 1.
DR PANTHER; PTHR38248; FUNK1 6; 1.
DR Pfam; PF17667; Pkinase_fungal; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000076761}.
FT DOMAIN 141..222
FT /note="Fungal-type protein kinase"
FT /evidence="ECO:0000259|Pfam:PF17667"
FT DOMAIN 298..585
FT /note="Fungal-type protein kinase"
FT /evidence="ECO:0000259|Pfam:PF17667"
FT REGION 676..696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 759..812
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 768..791
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 812 AA; 92426 MW; 7936B4B41584AF72 CRC64;
MDMRGKFLSI DPQAFLDTFL PINEGSGVPP SIDLKAFEPM KEIDGEREMY LPWINCEENN
NFCPGYKFVA TPDKGDRNDS RTKGRQVPDV GLYLKKDAPV DTPRWSKMAL YVEFKSRKEG
LKQDPFCDDP RKPFESDAEE RESVRGQIIG YTEAMFSHQH RTHVFSLLVL GEHVRFIRWD
RSGAIVSQLV HYVEDPEILA HFLWRFSNLA PSQAGFDLTA EEIVKESPEW RLMTSGPDDE
KLTTQQRQYW QDSLKESWSW WKLKVGGCDC SSRTSRAQVP RQNMDPNCED RNHVAGTERP
RYFLVGKPHF TAPGVDGRGT RGYIAMDPET KKLHYLKDCW RVSLPGIQKE GDVLRALRDA
KVRYVPTLTC DGDVCNHCRG YPEDSLQFVH TDSSSDATSV VGTEFTSKGD GVDAKNSILY
TGYTANDCAN VLDHRQSTFT DKQWKGANPN PMKSHLHYRM VVEEIGQPLD DLKDARQLVA
TIFYTIIAHH EAYEKAGILH RDISRGNILI HVTRKKQADG SWKRYPAALL NDWDLSRNVR
ADGANPRQPD RTGTWQFMSA ALLISPRKIH EVSDDLESFV HVLVYESLRF LKHNCQSVSS
VMKEFFDTYN YQTNGVVTGG YPKLAAFQAG HLIDGQQQIV FANHHVDEII QTTFQWFDAY
YHDVLRRLHE RNTAQNYPAE DANLPQETED DEEEEDFNRL DAEIADALEH HVPDLNPVLV
VRDSSTRLQV ETHSPMRHLF AAHLQDLVWS DGDKVGDQLK KPATPSISVA IPPSSNTSLG
KRPASEYQAD QPGTSEERKQ KALKSNTGRS PS
//