ID A0A2N3NGH2_9PEZI Unreviewed; 874 AA.
AC A0A2N3NGH2;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Tr-type G domain-containing protein {ECO:0000259|PROSITE:PS51722};
GN ORFNames=jhhlp_003266 {ECO:0000313|EMBL:PKS11501.1};
OS Lomentospora prolificans.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Microascales; Microascaceae; Lomentospora.
OX NCBI_TaxID=41688 {ECO:0000313|EMBL:PKS11501.1, ECO:0000313|Proteomes:UP000233524};
RN [1] {ECO:0000313|EMBL:PKS11501.1, ECO:0000313|Proteomes:UP000233524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JHH-5317 {ECO:0000313|EMBL:PKS11501.1,
RC ECO:0000313|Proteomes:UP000233524};
RX PubMed=28963165; DOI=10.1534/g3.117.300107;
RA Luo R., Zimin A., Workman R., Fan Y., Pertea G., Grossman N., Wear M.P.,
RA Jia B., Miller H., Casadevall A., Timp W., Zhang S.X., Salzberg S.L.;
RT "First Draft Genome Sequence of the Pathogenic Fungus Lomentospora
RT prolificans (Formerly Scedosporium prolificans).";
RL G3 (Bethesda) 7:3831-3836(2017).
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 -!- 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:PKS11501.1}.
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DR EMBL; NLAX01000008; PKS11501.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N3NGH2; -.
DR STRING; 41688.A0A2N3NGH2; -.
DR VEuPathDB; FungiDB:jhhlp_003266; -.
DR InParanoid; A0A2N3NGH2; -.
DR OrthoDB; 5477300at2759; -.
DR Proteomes; UP000233524; 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:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR CDD; cd01883; EF1_alpha; 1.
DR CDD; cd16267; HBS1-like_II; 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; IPR031157; G_TR_CS.
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:SF309; ELONGATION FACTOR EF-1 SUBUNIT, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G04630)-RELATED; 1.
DR PANTHER; PTHR23115; TRANSLATION FACTOR; 1.
DR Pfam; PF00009; GTP_EFTU; 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; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 4: Predicted;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000233524};
KW Translation regulation {ECO:0000256|ARBA:ARBA00022845}.
FT DOMAIN 465..688
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 246..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..335
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 874 AA; 96328 MW; 53855F0F5B120E82 CRC64;
MSRHRVMAGL DYREELSDAD PDDEVPFDDE VDQVAMREGK EKVTKALGDI ADLIPPAEVE
QALWDNYYDV EKSVAILSEI YEKEVHKLGE ATIEVLARLG ESSEKVTPKQ IKDALWHYYF
DIDKTVAYID RTYINPVEKP KPKAKAPAER KCSSHCMPLR HYTHVEASRR DKKRRTSDNM
PDGMALAEGY SEEFSLVPRI KVPAEWHFYG VPWTNGLCGQ STTTFIEPPR YAGLLGGSSK
PSKLQALAAA RKNKKAGEKP PPEPVPEKPR PSTSGPPAAP SSSKENIKLD IRLLSKRRRE
EAKEEPAAPA DTRPLHENEP DAPEQLHKRR DSNLDEGLIP EVQVYVKPPQ PSAFASTLFG
SSTNVPAPRV EAYPFPYTTS TSYSAKAFLE PSPDDVVMAA QAKAGKKIAV PTQKKGPKGS
TATPSNNNVE AVAEQMGKLT TKHEPRPKSK QLDVVKEYEN MKKDKKSASF VVVGHVDAGK
STLMGRLLLE LKFVDKALVD KYRRQAEKIG KQSFALAWVM DQREEERDRG VTIDIATNHF
ETDKGRYTIL DAPGHKDFIP NMIAGASQAD FAILVVDAST GAFEKGLKGQ TREHVLLLRA
LGVHKLIVAV NKMDMVDWSK ARFDEISDQI MGFLSAKGFL PKNVTFIPMS GFNGDNLTRR
SEASASSWYT GTTLIESLDN ADPISRPLRK AFRMAISEIW KSPLGHVTVS GRIDTGTTQI
GDVLVVQPSG EEAYVKTIMV DADLRDWAVA GESVSIFLTG IDPAHLRVGD IMCAASSPVG
TSDTFRMKAM AFEHVMPMPI DLHRGRLHSA GQVLEMEAIL DKATGEVLKK RPKVIQPGEV
ARVTVKLASK IPLEAGQRVV IRSSGETVAA GLVE
//
