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Database: UniProt
Entry: M7PGS8_PNEMU
LinkDB: M7PGS8_PNEMU
Original site: M7PGS8_PNEMU 
ID   M7PGS8_PNEMU            Unreviewed;       673 AA.
AC   M7PGS8;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN   ORFNames=PNEG_01854 {ECO:0000313|EMBL:EMR09664.1};
OS   Pneumocystis murina (strain B123) (Mouse pneumocystis pneumonia agent)
OS   (Pneumocystis carinii f. sp. muris).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Pneumocystomycetes; Pneumocystaceae; Pneumocystis.
OX   NCBI_TaxID=1069680 {ECO:0000313|EMBL:EMR09664.1, ECO:0000313|Proteomes:UP000011958};
RN   [1] {ECO:0000313|Proteomes:UP000011958}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B123 {ECO:0000313|Proteomes:UP000011958};
RX   PubMed=26899007; DOI=10.1038/ncomms10740;
RA   Ma L., Chen Z., Huang D.W., Kutty G., Ishihara M., Wang H., Abouelleil A.,
RA   Bishop L., Davey E., Deng R., Deng X., Fan L., Fantoni G., Fitzgerald M.,
RA   Gogineni E., Goldberg J.M., Handley G., Hu X., Huber C., Jiao X., Jones K.,
RA   Levin J.Z., Liu Y., Macdonald P., Melnikov A., Raley C., Sassi M.,
RA   Sherman B.T., Song X., Sykes S., Tran B., Walsh L., Xia Y., Yang J.,
RA   Young S., Zeng Q., Zheng X., Stephens R., Nusbaum C., Birren B.W.,
RA   Azadi P., Lempicki R.A., Cuomo C.A., Kovacs J.A.;
RT   "Genome analysis of three Pneumocystis species reveals adaptation
RT   mechanisms to life exclusively in mammalian hosts.";
RL   Nat. Commun. 7:10740-10740(2016).
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   -!- 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:EMR09664.1}.
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DR   EMBL; AFWA02000009; EMR09664.1; -; Genomic_DNA.
DR   RefSeq; XP_007873825.1; XM_007875634.1.
DR   AlphaFoldDB; M7PGS8; -.
DR   STRING; 1069680.M7PGS8; -.
DR   GeneID; 19895548; -.
DR   VEuPathDB; FungiDB:PNEG_01854; -.
DR   eggNOG; KOG0583; Eukaryota.
DR   HOGENOM; CLU_000288_59_3_1; -.
DR   OMA; SKTKWHF; -.
DR   OrthoDB; 5475340at2759; -.
DR   Proteomes; UP000011958; 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}; Reference proteome {ECO:0000313|Proteomes:UP000011958}.
FT   DOMAIN          31..282
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         60
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   673 AA;  76669 MW;  58244BF96E3141D5 CRC64;
     MNDKNTNANT IFDNDPQELL NISEKPRLGH YAILKTLGEG SFGKVKLAVH SITGHKVALK
     IISRKSLLNL DMSSRVDREI SYLKLLRHPH IIKLYEVIAT PTDIIMVIEY AGGELFDYIV
     SRGKMSEDEA RRFFQQIITA VEYCHRHKIV HRDLKPENLL LDDFLNVKIA DFGLSNLMTD
     GNFLKTSCGS PNYAAPEVIS GKLYAGPEVD VWSCGVILYV MLVGRLPFDD EFIPTLFKKI
     NGGIYTIPSF LSSDAKELLS QMLVVDPIQR ITLQEIRESK WFNLNLPDYL HPLDKYEEKN
     EVDDKIVGKL GQAMGYNKDH VYEALARSDC NEIKDAYRLV AENQMRYKDF RIIMAKNIQS
     FLAQSPPSWD TEQIKFPRNI SSSSLGHPSP TNINTYSISK GVYSTLLPSV GGSYTRIEDQ
     TPFHISILPS SLHNYHIMYM NKRISLDSLN RNIKDKKLQS NISKSVLVPM SINTEKKKRA
     IRWHFGIRSR SSPLEIMIEI YRALKDLGAE WVDIESQNIN LHEKINKFKE KNLSENNDAN
     EAILDSNKAK DPYVIKCRLT KSSDNEKKII VTIVIQLYHL ESNNFLVDFK CGGYENVYSI
     ISELPSNNIN SETEKIICGM SKLIKNDIMK TSSQDLNTSQ YSLDSSGKNL SEKQVTSPFP
     FLDMASQLIL HLM
//
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