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Database: UniProt
Entry: M7NM13_PNEMU
LinkDB: M7NM13_PNEMU
Original site: M7NM13_PNEMU 
ID   M7NM13_PNEMU            Unreviewed;       785 AA.
AC   M7NM13;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=Tr-type G domain-containing protein {ECO:0000259|PROSITE:PS51722};
GN   ORFNames=PNEG_03405 {ECO:0000313|EMBL:EMR08237.1};
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:EMR08237.1, 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=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC         Evidence={ECO:0000256|ARBA:ARBA00001702};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC         Evidence={ECO:0000256|ARBA:ARBA00001702};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC       subfamily. {ECO:0000256|ARBA:ARBA00007249}.
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:EMR08237.1}.
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DR   EMBL; AFWA02000017; EMR08237.1; -; Genomic_DNA.
DR   RefSeq; XP_007875490.1; XM_007877299.1.
DR   AlphaFoldDB; M7NM13; -.
DR   STRING; 1069680.M7NM13; -.
DR   GeneID; 19897092; -.
DR   VEuPathDB; FungiDB:PNEG_03405; -.
DR   eggNOG; KOG0458; Eukaryota.
DR   HOGENOM; CLU_007265_3_2_1; -.
DR   OrthoDB; 5477300at2759; -.
DR   Proteomes; UP000011958; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0002181; P:cytoplasmic translation; IEA:UniProt.
DR   GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR   CDD; cd01883; EF1_alpha; 1.
DR   CDD; cd16267; HBS1-like_II; 1.
DR   CDD; cd04093; HBS1_C_III; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 2.
DR   InterPro; IPR004161; EFTu-like_2.
DR   InterPro; IPR015033; HBS1-like_N.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR   InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR   PANTHER; PTHR23115:SF188; HBS1-LIKE PROTEIN; 1.
DR   PANTHER; PTHR23115; TRANSLATION FACTOR; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   Pfam; PF03143; GTP_EFTU_D3; 1.
DR   Pfam; PF08938; HBS1_N; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SUPFAM; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50447; Translation proteins; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011958};
KW   Translation regulation {ECO:0000256|ARBA:ARBA00022845}.
FT   DOMAIN          359..573
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   785 AA;  89056 MW;  C7507886FFDFF025 CRC64;
     MSWRSYFGQE LDDFSADNLE DFSQEELEKL TWTSAKVRER LKDVLHVKQK DIQEALKYCC
     FDIDKACSRI IEKKHLKEGL NINKTPSKKG FISFNNSSLN KEDLKSHFNL EVSSEENASE
     TKEVSGPKQS KLIALASSKH KLSSNNPISS SLKSVSLLSH LTREKFKATN NRENNNNSSK
     IILDIQTNFA KPDVEKDLNL LKTTSEEDQK EEVIDDSLNV FFKKNCEYNI EVKPSKFALT
     IFGEKLELPD YFYKFANQRF SLFTGVLEDD LKISLNETFN NSLKSQKKKE KKLKTPSIVK
     SPIYSEIISN KDDLHHILNT LNISSEQGDK DETNYDKFYK LSESKNKISN LKTANIKNKP
     NVNIVIIGHV DAGKSTLIGR LLYDLKVVDT ETIEKLKRET NKLGKPSFHF AWVLDQTSEE
     RDRGVTMDLG INYFETSLRR YTILDTPGHK DFIPNMIAGA SQADVALLVI DASYGSFESG
     FTAHGQTREH VILARSLGIQ KIVVAINKLE TTNWSQERYE DIMAQMLQFF IYKGFQKSNI
     SFIPCSGLTG ENLTNTIPLN PQLKLWYSNF TLLDTLENIS INRQQLDTFL RLSIMDVYKS
     SNTLISVVGR IETGIINVGK EVIIMPSRKN GIIESIYIHD NLQDLAFSGD EVLINLLNID
     LSYLKPGDII CDLENPVQIV SKFRAKIITF DLSRPLIIGT PLIIYRGRLN VDGNIKKLIS
     IIDKSTGQVK KKDPKFIGSF DAAIVEIEFC KQAEAMESFK HCKELGRFIA RSQGETVAAG
     IIEDE
//
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