ID A0A0C9MHZ5_9FUNG Unreviewed; 696 AA.
AC A0A0C9MHZ5;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 49.
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=MAM1_0352d09952 {ECO:0000313|EMBL:GAN10411.1};
OS Mucor ambiguus.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX NCBI_TaxID=91626 {ECO:0000313|EMBL:GAN10411.1};
RN [1] {ECO:0000313|EMBL:GAN10411.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NBRC 6742 {ECO:0000313|EMBL:GAN10411.1};
RA Takeda I., Yamane N., Morita T., Tamano K., Machida M., Baker S., Koike H.;
RT "Draft genome sequence of an oleaginous Mucoromycotina fungus Mucor
RT ambiguus NBRC6742.";
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily.
CC {ECO:0000256|ARBA:ARBA00008874}.
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DR EMBL; DF836641; GAN10411.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C9MHZ5; -.
DR STRING; 91626.A0A0C9MHZ5; -.
DR OrthoDB; 460351at2759; -.
DR Proteomes; UP000053815; 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; cd01093; CRIB_PAK_like; 1.
DR CDD; cd13279; PH_Cla4_Ste20; 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; SERINE/THREONINE-PROTEIN KINASE TAO; 1.
DR PANTHER; PTHR48015:SF6; SERINE_THREONINE-PROTEIN KINASE CLA4-RELATED; 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}; Kinase {ECO:0000313|EMBL:GAN10411.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000053815};
KW Transferase {ECO:0000313|EMBL:GAN10411.1}.
FT DOMAIN 3..97
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 100..113
FT /note="CRIB"
FT /evidence="ECO:0000259|PROSITE:PS50108"
FT DOMAIN 422..675
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 192..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..235
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..329
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..356
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..389
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 451
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 696 AA; 78834 MW; 3C6841A044C8DE51 CRC64;
MPEIIKEGYL SLKEEGLRAW IWSKRYCVLR DQSLTFHRNE AGQCIGLLFL KEIGSVTRID
LKPYCFEISA KDKTYYVSCK SDEELYSWMD EIYNRSSVGT SGPTNFIHNV HVGFDPITGA
FTGLPDQWTR LLKGSAITAE DAAKNPQAVL DVLEFYAEQT KREEEEYGTS QLQGAVERMS
GVGWAKMMQE NSLHQPPQVP TASTSSSTLQ KKPVPNVKLP PKNIPTRPAP PPPSALAALS
ELKIQDQQQQ LKLQQKQQQQ QQQQSPSLPR PSHKTNNAIT PALPGNYALP SRDQNGSPIP
GGKSIKDLHL EKLLGSEVQE ERERQRIPVR TSSVDYYQQQ QVSREREQQQ QQQQQQLENE
KERERERERE RERLHRERER EKAAAQVSSK KKVEQRISTM SEAQIMEKLR SVVSKGDPNE
CYKKIKRVGQ GASGSVYVAN SLATNTKVAV KQMDLAHQPR KELIVNEILV MKESQHPNIV
NFLDSFLVGS SDLWVVMEFM EGGALTDVID NNSKMTEQQI STVCLETVAG LHHLHSQNII
HRDIKSDNIL LNSQGHVKIS DFGFCAKLTD QKRKRATMVG TPYWMAPEVV KQKEYGAKVD
IWSLGIMAIE MIENEPPYLD EEPLKALYLI ATNGTPTLKN PERLSSELKS FLAVCLCVDV
RSRANSMELI NHEFLKKAGP LEILAPLLKF RTKTKI
//
