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Database: UniProt
Entry: U1G6S2_ENDPU
LinkDB: U1G6S2_ENDPU
Original site: U1G6S2_ENDPU 
ID   U1G6S2_ENDPU            Unreviewed;       890 AA.
AC   U1G6S2;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 53.
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=EPUS_06543 {ECO:0000313|EMBL:ERF73082.1};
OS   Endocarpon pusillum (strain Z07020 / HMAS-L-300199) (Lichen-forming
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Verrucariales; Verrucariaceae; Endocarpon.
OX   NCBI_TaxID=1263415 {ECO:0000313|EMBL:ERF73082.1, ECO:0000313|Proteomes:UP000019373};
RN   [1] {ECO:0000313|Proteomes:UP000019373}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Z07020 / HMAS-L-300199 {ECO:0000313|Proteomes:UP000019373};
RX   PubMed=24438332; DOI=10.1186/1471-2164-15-34;
RA   Wang Y.-Y., Liu B., Zhang X.-Y., Zhou Q.-M., Zhang T., Li H., Yu Y.-F.,
RA   Zhang X.-L., Hao X.-Y., Wang M., Wang L., Wei J.-C.;
RT   "Genome characteristics reveal the impact of lichenization on lichen-
RT   forming fungus Endocarpon pusillum Hedwig (Verrucariales, Ascomycota).";
RL   BMC Genomics 15:34-34(2014).
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};
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=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
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; KE720986; ERF73082.1; -; Genomic_DNA.
DR   RefSeq; XP_007801253.1; XM_007803062.1.
DR   AlphaFoldDB; U1G6S2; -.
DR   GeneID; 19241483; -.
DR   eggNOG; KOG0578; Eukaryota.
DR   HOGENOM; CLU_000288_26_2_1; -.
DR   OMA; NFTHRVH; -.
DR   OrthoDB; 460351at2759; -.
DR   Proteomes; UP000019373; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0019236; P:response to pheromone; IEA:UniProtKB-KW.
DR   CDD; cd01093; CRIB_PAK_like; 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; 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; PF15413; PH_11; 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; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Pheromone response {ECO:0000256|ARBA:ARBA00022507};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019373};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022527}.
FT   DOMAIN          85..184
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          189..202
FT                   /note="CRIB"
FT                   /evidence="ECO:0000259|PROSITE:PS50108"
FT   DOMAIN          600..869
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          259..329
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          344..521
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          533..553
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..64
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        297..326
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        344..391
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        442..470
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        491..521
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   890 AA;  99082 MW;  70B5DC529AD17BBF CRC64;
     MTSSHPPNLY APGQFMNPGP APRPPTDRPR LNLGASTGSI PQVTSFDQMS LGPNSPAPST
     TSAPYFSSNS SSLSLISSKS QSSTNVIKEG YVRCKEDKFW GGWNQRYLIL REFRLDFMKN
     EQGNLMHSIL LNTIAGVSRS EDTRMAFEIT RTASAKKGAK TITCEVRNDD EIYDWIDKIY
     VRCPKMGGVS NPTNFSHRVH VGFDPQTGGF VGLPVEWEKL LTASAITKED YKKNPQAVIE
     VLEFYSDHKM REQHPELFAG SASGQNAPEM SQNRPFGLGG VGTSIAPPRP APPSRAETFP
     TNYQEITPPR SGNNTPKPSS QRVPTDKSGY DMEADAARIK EIANQEQQRR QEEAARKEEL
     RRVREVQRRR EQDREREEKR EREEEQARRD LEAYNASIPK SRTPLAQQEI GGYGADNSPS
     RYNPARAAPQ APGRERDRQP QSSSRQPTTS QRAASSTPDG ATSTSRSPAR PHFEPSAGGD
     GRVPDGARQE SSNDAYRTDP RSQQSQTRHP PNGINGATQS SRLPAPVQQV KPLNVSNKQN
     QVPTKQAATP DARQQAEIAL TTKKPTEERS KEVRMSSMSE SEVMAKLKQV VSRDNPLESY
     SKQKKIGQGA SGSVYVARVK EGATSSIARE IYRTQGPKGQ VAIKQMDLRN QPRKELIVNE
     IIVMKDSKHP NIVNFLDSFL QEQNNELWVV MEFMEGGALT DVIDNNPVIT EDQISTICFE
     TCKGLAHLHS QDIIHRDIKS DNVLLDRVGN VKITDFGFCA KLTESKSKRA TMVGTPYWMA
     PEVVKQKEYG PKVDIWSLGI MAIEMIESEP PYLNEEPLKA LFLIATNGTP RLKNPNKLSR
     ELKAFLSVCL CVDVKSRAAA DELLQHDFMR NGCSLASLAE MLRWKNNSGK
//
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