ID A0A135TMM3_9PEZI Unreviewed; 1355 AA.
AC A0A135TMM3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=MAP kinase kinase kinase {ECO:0000256|PIRNR:PIRNR037579};
DE EC=2.7.11.- {ECO:0000256|PIRNR:PIRNR037579};
GN ORFNames=CSAL01_11415 {ECO:0000313|EMBL:KXH49385.1};
OS Colletotrichum salicis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=1209931 {ECO:0000313|EMBL:KXH49385.1, ECO:0000313|Proteomes:UP000070121};
RN [1] {ECO:0000313|EMBL:KXH49385.1, ECO:0000313|Proteomes:UP000070121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 607.94 {ECO:0000313|EMBL:KXH49385.1,
RC ECO:0000313|Proteomes:UP000070121};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum salicis CBS 607.94.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
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 Evidence={ECO:0000256|PIRNR:PIRNR037579};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. MAP kinase kinase kinase subfamily.
CC {ECO:0000256|PIRNR:PIRNR037579}.
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:KXH49385.1}.
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DR EMBL; JFFI01001930; KXH49385.1; -; Genomic_DNA.
DR STRING; 1209931.A0A135TMM3; -.
DR OrthoDB; 1440978at2759; -.
DR Proteomes; UP000070121; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004709; F:MAP kinase kinase kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0051403; P:stress-activated MAPK cascade; IEA:UniProtKB-UniRule.
DR CDD; cd06626; STKc_MEKK4; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017240; MAPKKK_Ssk2/Ssk22.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR48016; MAP KINASE KINASE KINASE SSK2-RELATED-RELATED; 1.
DR PANTHER; PTHR48016:SF32; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 4; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PIRSF; PIRSF037579; MAPKKK_SSK22; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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|PIRNR:PIRNR037579};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR037579};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR037579};
KW Reference proteome {ECO:0000313|Proteomes:UP000070121};
KW Serine/threonine-protein kinase {ECO:0000256|PIRNR:PIRNR037579};
KW Transferase {ECO:0000256|PIRNR:PIRNR037579}.
FT DOMAIN 1051..1320
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 89..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 168..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1329..1355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1080
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1355 AA; 153037 MW; 8E2E5A492C98C269 CRC64;
MSTELSPRAV RFSNGDDDLR SDKIMPQRPV VIPVDSDNSA SSGEFQPDDP HAVERQDELG
SLARYSEGHI AGSMSNLVQA AVANGTTRSL RSNASDGDAS YTNGASKVQR PSAPARTPSN
TYAPATHRRP QPAPSFVESV RASSRGRPRP SERFRQQERA YVQRLRQDHN DGYPFDGGYV
NGITGIGQGA DSDSEGETPS SEGPFDDRYD QETIMFYGND DLQPTDEDLK DPTNRERLEW
HGMLEAVLTG DVVKQEKKRL IGSNEQAVGK SGQKAELWLG IRSKACGRHL PVQRRMVEEA
RAALDRTLDE IINFSVKGES EAGKPPYEQV KDVVKKMDKA ENLYPSWTSL AAEHQSANSP
LFHEASESII AWYNTNEMIN TELAILKKWV GNEELDFTRT RQRSPVGNGI SDESSFLDRL
MKEDGLKSLY DEEFDEKNKD AHKGMLPGIS TVITKSKQTL IRNFAAFQKR HLPPYIEELL
TLISFPSRLI EEIIKMRLAY AKKVKESAQQ NPMMQDQMIN QFQLLLKLAI RIKLECLAVT
QPEPGWELPP CIDESFDQVV LDALRYYFKM LNWKLSGNKN TFKEAELLFA EWDFANEIGS
HLLGGDVEVA EQFSSLTFKA INRLSVTFEK ELQVKPKEST AEMSKRYKQC LDSVRVRQRM
LQRFSRMLSE NYENASDFSI SFTPEKLQEF YDRLIASGHF QIFTDLYEQE GIFIIASPSL
MDRHDAIHSI LGLSSPEQFA EDPSDPYLLI LRPESSPHWF GDIVQLSVRE RNVDLKKGHM
RLVAAAAQAR LVNARKAFID AVDMHVDLVV EQRSNLHKVN TRLMETRRVA YKLSNNFMGS
VEIIRKQTQG REVQELIQTC FVFATEFGQR SLLVMDSNRK QMNNLKLTKL ALDWVSFICD
DCIASDRKTF RWAVLALEFA MGMTRGRHIL ALGEEEYARL RAKVAGCMAL LISHFDIMGA
RSNLAAQAEK ERIEALVGQF KRLDKNRMLD DHEASKYITE QRLEEIDKVD DIRRAKEAER
QALGRVLEGN NEVDRCLAYL SSSATNITMR WQQGHFVGGG TFGNVYAAMN LDSGHLMAVK
EIRLQDPKLI PTIAEQIKDE MGVLEVLDHP NVVSYYGIEV HRDRVYIFME FCQGGSLANL
LEHGRIEDEQ VIMVYALQLL EGLAYLHESG IAHRDIKPEN ILLDHNGIIK YVDFGAAKVI
ARQGKTLVQD LSSSKPNKSM TGTPMYMSPE VIKGENPGRA GSVDIWSLGC VILEMATGRR
PWANLDNEWA IMYNIAQGNP PQMPSVDQLS PQGLDFLKRC FTRDPKHRAS AVELLQHDWI
MTIRSQVVEP PTPSDASSSA QSTPSSRSNT NDGFY
//
