ID M7PB55_PNEMU Unreviewed; 822 AA.
AC M7PB55;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=mitogen-activated protein kinase kinase kinase {ECO:0000256|ARBA:ARBA00012406};
DE EC=2.7.11.25 {ECO:0000256|ARBA:ARBA00012406};
GN ORFNames=PNEG_00717 {ECO:0000313|EMBL:EMR11120.1};
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:EMR11120.1, 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 -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. MAP kinase kinase kinase subfamily.
CC {ECO:0000256|ARBA:ARBA00006529}.
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:EMR11120.1}.
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DR EMBL; AFWA02000002; EMR11120.1; -; Genomic_DNA.
DR RefSeq; XP_007872617.1; XM_007874426.2.
DR AlphaFoldDB; M7PB55; -.
DR STRING; 1069680.M7PB55; -.
DR GeneID; 19894415; -.
DR VEuPathDB; FungiDB:PNEG_00717; -.
DR eggNOG; KOG0198; Eukaryota.
DR HOGENOM; CLU_003051_1_2_1; -.
DR OMA; TINARWQ; -.
DR OrthoDB; 145974at2759; -.
DR Proteomes; UP000011958; 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 GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd09534; SAM_Ste11_fungal; 1.
DR CDD; cd06628; STKc_Byr2_like; 1.
DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR000159; RA_dom.
DR InterPro; IPR029458; Ras-bd_By2.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR11584:SF369; APOPTOTIC SIGNAL-REGULATING KINASE 1, ISOFORM C; 1.
DR PANTHER; PTHR11584; SERINE/THREONINE PROTEIN KINASE; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF14847; Ras_bdg_2; 1.
DR Pfam; PF07647; SAM_2; 1.
DR SMART; SM01304; Ras_bdg_2; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50200; RA; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022527};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000011958};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022527}.
FT DOMAIN 10..73
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 183..268
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 545..809
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 574
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 822 AA; 93068 MW; EC32F3FB16C5800B CRC64;
MNYLNEVKLW SEEKVGEWLK SNNFGDYVDI FKENNVNGDI LLECNAALLK ELGIKKLGDR
IKLSVCIKKL REKCIESARK AKMSFLMIDN RISEFPFTSQ SPTDPLIPVK SGDLISPTSN
FQLDNPYNDA CCFDSLNNSH SFLSNASHST KSLSKDSFTS TQRVFEKSPI FSEINIMQSN
SIKKNCLKFI GEKGQTRIVN ISRCHTAEAI LSKALKKFNI IEDPSEWRVF ITNEDGSFEC
ISNDTLLTIS RQLSRPERER LILKRKSDPL TLEEFRKSQT IAREQQDAIY HTAVMAKTSG
NLRKLETFFG EKLTPTFTSS FTTPLPSPLP KDNKYGNIKH IRNFFGQRPP SELINSNLAE
YFPGHEKKVL EQTIKNSIKS THLNSFRGPN FSTSSSTLAY DISSIPTVGE AWIQFEGQRL
SEIGRTFSLS RFISTRFPTL LESSILKENS SHHTLSLSKS NTEDNTQDIK PIFCKKSEEK
AFPNETFKSE SPNVLGEPLI LSDIYNTSLE TARDVLDDNI FENNENKDFN FEKEVENNNT
GPTRWIKGAL IGSGSFGSVF LGMNALSGEL MAVKQVEIPS FDIQGCKRKK AMLDALQREI
SLLKELHHEN IVQYLGSSMD ETHLTFFLEY VPGGSVTALL NNYGAFEEPL IRNFVRQILK
GLNYLHNKKI IHRDIKGANI LVDNKGGIKI SDFGISKKVE ANLLSMTRNQ RPSLQGSVYW
MAPEVVKQTL YTRKADIWSL GCLIVEMFTG EHPFPKMNQL QAIFKIGQYV SPEIPEHCTS
EARHFLEKIF EPDYHARPTA ADLLKYSFLG PMVSSPLTDA KK
//
