ID A0A1V8SJL5_9PEZI Unreviewed; 977 AA.
AC A0A1V8SJL5;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU361162};
DE EC=2.7.11.21 {ECO:0000256|RuleBase:RU361162};
GN ORFNames=B0A48_14309 {ECO:0000313|EMBL:OQN99332.1};
OS Rachicladosporium antarcticum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Cladosporiales; Cladosporiaceae; Rachicladosporium.
OX NCBI_TaxID=1507870 {ECO:0000313|EMBL:OQN99332.1, ECO:0000313|Proteomes:UP000192596};
RN [1] {ECO:0000313|Proteomes:UP000192596}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCFEE 5527 {ECO:0000313|Proteomes:UP000192596};
RA Coleine C., Masonjones S., Stajich J.E.;
RT "Genomes of endolithic fungi from Antarctica.";
RL Submitted (MAR-2017) 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 EC=2.7.11.21; Evidence={ECO:0000256|RuleBase:RU361162};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. CDC5/Polo subfamily. {ECO:0000256|RuleBase:RU361162}.
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:OQN99332.1}.
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DR EMBL; NAJO01000040; OQN99332.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V8SJL5; -.
DR STRING; 1507870.A0A1V8SJL5; -.
DR InParanoid; A0A1V8SJL5; -.
DR OrthoDB; 5471704at2759; -.
DR Proteomes; UP000192596; 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; cd13118; POLO_box_1; 1.
DR Gene3D; 3.30.1120.30; POLO box domain; 3.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR033701; POLO_box_1.
DR InterPro; IPR000959; POLO_box_dom.
DR InterPro; IPR036947; POLO_box_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24345; SERINE/THREONINE-PROTEIN KINASE PLK; 1.
DR PANTHER; PTHR24345:SF0; SERINE_THREONINE-PROTEIN KINASE PLK1; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF82615; Polo-box domain; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50078; POLO_BOX; 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:0000256|RuleBase:RU361162};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000192596};
KW Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU361162};
KW Transferase {ECO:0000256|RuleBase:RU361162}.
FT DOMAIN 23..288
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 838..894
FT /note="POLO box"
FT /evidence="ECO:0000259|PROSITE:PS50078"
FT REGION 385..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 416..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..476
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 56
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 977 AA; 106677 MW; D4DD03B38CA615F4 CRC64;
MSSSIHAEPP PPIVTEPNGG INYATGPALG KGGFAICHRA ERYEGSKPTG QLLALKIVKT
KMEPAKLAQK FVSELQIHSK LVHPNIVAFY RAFAFQTSTY VVLELCPNGS LADMLKKRKF
LTLPEIRRFV IQICGAVKYL HHRHIVHRDL KTGNLFLDKD MNVKVGDFGL AALLVTEKEM
ELKRRTTMCG TPNYLAPEIL EKGKGHNEKV DLWSIGVIAY TLAVGKAPFH ASTKEEIYKK
LKQGEYKWPE LSATNNDISN DLRVTVASLL VPEDMRPSPD EIVSQDFFKI AYVPAGIPSS
AREKAPVWME ATVPSKSVRE QGYSDSWRAL CEEAGVGSIR EGSKFKLPGG ARVRSIVYDI
EYDAQMGTTP TMPIPKDTVY VSTVSDMSKD STPEPELASR PPSRGLKEIS HNEVAARARP
AVADRDAMPP PSRPARTAEV AARPASRAAR TGTIRRTART ISEETANAEE KVKVASDPDM
AWPASRQRGQ TLAAPTALRV AESSGLTARQ QAAQVAETDA ALLKPARAAS TRTRGADPSL
ARRPGATSRR VDRSVSPPVA QPFATLEELR QVSPFKESRR RAPPAEVIEI LSDPESDAHA
PIRQTIQSAL NTNVLSLPPP PRMARTVPRP RKVTPAAVPM NPNALPSSNP ASVLTRLTLF
RDNLAAALTN STTSPPRPDP VDADSLPFVV KWVDYSHKHG VGYMLRSGTV GCVFNASNRH
SAPVTHVFSH CGRKWLAKVR KDLDNAEEIP LEILEDKGDD GLVRKIYKGL GSVKEGPLAA
EQARRKTLGV LWAKFGRYMG QSLEGEVGEE AVSKDGSMKE ANFVRFYQRV GTVGIWVFND
GCMQLHFPDH TKLVLSPSGL HLSTTLLSPE AATYLSAHST LLPHHISGRE TLASTTQSLL
HEGGRVQTRT VRANQVREKL EFLSRVVTEW VECGGLGRMR ADDGSGEKVH WEGLCAGGQG
KKVERGTVGR CGGDVSR
//
