ID A0A446BIC0_9PEZI Unreviewed; 722 AA.
AC A0A446BIC0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=0a0154c1-d448-46dc-93f5-c7a7e537e610 {ECO:0000313|EMBL:SPQ22257.1};
GN ORFNames=TT172_LOCUS4676 {ECO:0000313|EMBL:SPQ22257.1};
OS Thermothielavioides terrestris.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Thermothielavioides.
OX NCBI_TaxID=2587410 {ECO:0000313|EMBL:SPQ22257.1, ECO:0000313|Proteomes:UP000289323};
RN [1] {ECO:0000313|EMBL:SPQ22257.1, ECO:0000313|Proteomes:UP000289323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Huttner S., Dainat J.;
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001433};
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DR EMBL; OUUZ01000008; SPQ22257.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A446BIC0; -.
DR Proteomes; UP000289323; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR CDD; cd12122; AMPKA_C; 1.
DR CDD; cd14079; STKc_AMPK_alpha; 1.
DR CDD; cd14334; UBA_SNF1_fungi; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR Gene3D; 3.30.310.80; Kinase associated domain 1, KA1; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR032270; AMPK_C.
DR InterPro; IPR028375; KA1/Ssp2_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR013896; SNF1_UBA.
DR PANTHER; PTHR24346; MAP/MICROTUBULE AFFINITY-REGULATING KINASE; 1.
DR PANTHER; PTHR24346:SF82; SERINE_THREONINE-PROTEIN KINASE MARK-A-RELATED; 1.
DR Pfam; PF16579; AdenylateSensor; 2.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF08587; UBA_2; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF103243; KA1-like; 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 4: Predicted;
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}.
FT DOMAIN 80..331
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 583..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..520
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 109
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 722 AA; 80184 MW; 136938FA69141978 CRC64;
MAPAYDDEEL SISLSPSQIR RNRRPGEGQR QSTTTTTATT ATTGATETAT TRSPAAMSDP
PPSNVPLREK MRTEQRIGAY NIVKTLGEGS FGKVKLAVHR GTGQQVALKI ISRKNLISRD
MQGRVEREIE YLQLLRHPHI IKLYTVIKTP TEIIMVLEYA GGELFDYIVQ HGKMHEDEAR
RFFQQMLCAV EYCHRHKIVH RDLKPENLLL DDNLNVKIAD FGLSNIMTDG NFLKTSCGSP
NYAAPEVIGG KLYAGPEVDV WSCGVILYVL LVGRLPFDHE HIPTLFAKIA KGSYMVPTWM
SPGAANLIKK MLVVNPVQRA TIEEIRLDPW FLKDLPPYLH PPVEEFLNTG VDPNKAIKVS
DIAPHAPPQE QEKLHNEVTD KISKTMGYGK RDVEEALEAD EPSAIKDAYM IVRENKLMQS
SQLAGLGAED GTLSSARSVA SASTGASARP PYVSKVGILP SSLPVYHQAY MEREKARAEG
REVPDAPLTV PEPAPQPRSQ AEQAETLRRL KPHSRSFLRL DDASRPQGLT PVNPPKKTKP
VRWQFGIRSR NAPWEALLCI YKALHKLGAT WIVDEDYDPA QHGDDAGDDR YSRGRHSRSH
STASGAGPTE AYRLPADPWH MKIRWNTNKL QKHSAASGLC DAGASATHVS SCRDGTAGDE
QVVAMHMEIQ IYEMERGVYL VDFKVDGYET PDGKLLEDKE VASPFPFLDM AARLIMQLAD
AD
//
