ID A0A395SPP2_9HYPO Unreviewed; 898 AA.
AC A0A395SPP2;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Agc akt kinase {ECO:0000313|EMBL:RGP74306.1};
GN ORFNames=FLONG3_6085 {ECO:0000313|EMBL:RGP74306.1};
OS Fusarium longipes.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=694270 {ECO:0000313|EMBL:RGP74306.1, ECO:0000313|Proteomes:UP000266234};
RN [1] {ECO:0000313|EMBL:RGP74306.1, ECO:0000313|Proteomes:UP000266234}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 20695 {ECO:0000313|EMBL:RGP74306.1,
RC ECO:0000313|Proteomes:UP000266234};
RX PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA Busman M., Gutierrez S.;
RT "Evolution of structural diversity of trichothecenes, a family of toxins
RT produced by plant pathogenic and entomopathogenic fungi.";
RL PLoS Pathog. 14:e1006946-e1006946(2018).
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:RGP74306.1}.
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DR EMBL; PXOG01000132; RGP74306.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395SPP2; -.
DR STRING; 694270.A0A395SPP2; -.
DR Proteomes; UP000266234; 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-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd05586; STKc_Sck1_like; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24351:SF245; AGC_AKT PROTEIN KINASE SCK2; 1.
DR PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 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, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:RGP74306.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000266234};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 287..455
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 492..753
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 754..837
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT REGION 1..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 250..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 352..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 843..866
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..400
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 521
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 898 AA; 98592 MW; 58A54AFAE7443449 CRC64;
MNGVINQNVR SAADEDGADH IGLDTPRSGV ATPQPDLQDK RLPGIMSYFG QVRNHPSAPS
SNSNSNSSQS DTALDRILVQ PTPPTGLQLQ VHPEGSTRGC DSSASDRSPL QHESLDRMPS
TTQRDEHNLS NPYPTPPTSQ PSSSGGSISQ DMISADSGAH GRAAVEPKPL TQQAQFKKPT
ASPFTTTHFQ TSNDPSLPEL DSSKNAAHTK DSIQPSHPEP GAASSDASEA TAPGKWHFLN
GLKELTRMTF KSGNSTPTRA MSAARPSGSE RAPSSGRTSH DGAEVSGTQT PRSSGGAQAP
AAKGKLTIKI NEARGLRKSR DPYVVVVFQR SELISGGPHH IDEDDNLSID PPPAHGGIPI
QRSGSDSGRP LAIPMRSRQS SNTSINDHGG SLRNRPGQLS FTNPKWDAEA EFDVVDYDML
VDVSVYDHGA SGDEFLGHVD FQASKDPGAT VEGWFQLQGH ADTMAEKAPT GEIFLEAIYH
RAEKKQFGPQ DFDILKLIGK GTFGQVYQVR KKDTQRIYAM KVLQKKVIVQ KKEVAHTVGE
RNILVRTAMS DSPFIVGLKF SFQTPSELYL VTDYMSGGEL FWHLQKEGRF DEKRAKFYIA
ELILAIQHLH HNDIVYRDLK PENILLDANG HIALCDFGLS KANLTKNDTT NTFCGTTEYL
APEVLLDESG YTKMVDFWSL GVLVFEMCCG WSPFYAEDTQ QMYKNIAFGK VRFPRDTLSQ
EGRNFVKGLL NRNPKHRLGA TDDAEELKRH PFFADVDWTL LSKKLITPPF KPKLKSETDV
SYFDPEFTTA LDQNGSLNER AAALARGYAA STPLSPSVQA NFQGFTFVDE SALDDHMRDR
AGLVDEDMDD GNGHGRRHRD NDDWDNLDDI DLRKANRMSG IVKTGHDEHM VGGSHFDV
//
