ID A0A163J9Q8_ABSGL Unreviewed; 899 AA.
AC A0A163J9Q8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=ABSGL_04556.1 scaffold 5475 {ECO:0000313|EMBL:SAL98985.1};
OS Absidia glauca (Pin mould).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Cunninghamellaceae; Absidia.
OX NCBI_TaxID=4829 {ECO:0000313|EMBL:SAL98985.1};
RN [1] {ECO:0000313|EMBL:SAL98985.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101.48 {ECO:0000313|EMBL:SAL98985.1};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-2016) 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; LT552383; SAL98985.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A163J9Q8; -.
DR STRING; 4829.A0A163J9Q8; -.
DR InParanoid; A0A163J9Q8; -.
DR OMA; CVRLSAW; -.
DR OrthoDB; 1367900at2759; -.
DR Proteomes; UP000078561; 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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000078561}.
FT DOMAIN 65..155
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 158..171
FT /note="CRIB"
FT /evidence="ECO:0000259|PROSITE:PS50108"
FT DOMAIN 628..879
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 218..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..242
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..305
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..425
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..528
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..543
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..569
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 657
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 899 AA; 98745 MW; C9F3E6D46CA8A866 CRC64;
MESLSPASPF GDDAAGLCTL INKKALPILG GQCISWGRNH LLTPSPSPLI NQQSLGRKDS
MTLDAVKKDG FVHVKEEGLR AWIWSKRYLV LREQCLTIHR SEVAMVALKM VEAVNRSELK
SHCFELETTK KKIYIACRSD EELYSWMDEI YNLSPLGASG PTDFVHKIHV GFDPITGAFT
GLPDQWNTLL KGSKITPEDA AKNPQAVLEA LEFYTEQNRR EKQGYDSEDS DKDDDGWCHP
HDKPPLLKSS APDSVHPKPS RSTPAPRQFR DPPARPPLPK VIKDTPLKGE KLKKSSSKEK
LTGQKPKHPT TGPSPVRSAT TTDLASSGKS PTEQAVLPKK SHKYSGSTGN AHSRNPSTST
STTTRIGLTP PTPQPTLSSG SQDRHATKSN YNSSTLKPSA SLRSNSSSMK RDDRVTPENE
KHLRSKNAPT AGVPVPQLDR QKYGNDRPSP SSSSAAMGIS TSSSATELSS RHPVTAAAVA
TTTTPMTKKQ PGHHNYQPSP STSTTIVSDS TTLGKKLNTM SPSSSSTRKD TYKRLDGNNN
KKPEDKPANN NSASSLLTRK KSNGKPSLNA SPPQPAPQSS TPVPSTSSLN GKKASPKRQE
QRISTMNNAQ IMERLRSVVS NGDPSLLYRR NKRIGQGASG SVYLSTHMTA NAKVAIKQMD
LTKQSRLDLI VNEIMVMQES RHSNIVNFLD SFLVRGDLWV VMEYMEGGAL TDVIENNTMT
EHQIATVCLE TTKGLHHLHS QKIIHRDIKS DNVLLNFQGQ VKISDFGYCA KLTDQKNKRA
TMVGTPYWMA PEVVKQKEYG SKVDIWSLGI MAIEMIENEP PYLDEEPLKA LYLIATNGTP
SLKHPEKLSR ELKSFLAVCL CVDVKSRATA AELLKHEFLA KAGPVDLLPP LLRFRRNAT
//
