ID A6RA16_AJECN Unreviewed; 957 AA.
AC A6RA16;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=Tr-type G domain-containing protein {ECO:0000259|PROSITE:PS51722};
GN ORFNames=HCAG_05804 {ECO:0000313|EMBL:EDN10001.1};
OS Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=2059318 {ECO:0000313|EMBL:EDN10001.1, ECO:0000313|Proteomes:UP000009297};
RN [1] {ECO:0000313|Proteomes:UP000009297}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NAm1 / WU24 {ECO:0000313|Proteomes:UP000009297};
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
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};
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DR EMBL; CH476661; EDN10001.1; -; Genomic_DNA.
DR AlphaFoldDB; A6RA16; -.
DR STRING; 339724.A6RA16; -.
DR VEuPathDB; FungiDB:HCAG_05804; -.
DR HOGENOM; CLU_007265_3_2_1; -.
DR OMA; FRMAISE; -.
DR OrthoDB; 5477300at2759; -.
DR Proteomes; UP000009297; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
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; IPR005225; Small_GTP-bd_dom.
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 NCBIfam; TIGR00231; small_GTP; 1.
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; 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 Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000009297};
KW Translation regulation {ECO:0000256|ARBA:ARBA00022845}.
FT DOMAIN 421..648
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 83..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 177..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 896..957
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 31..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 917..947
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 957 AA; 104230 MW; F7EFE6CAF3A6B64B CRC64;
MSRNRVKNIA YDHDDFPSDD DNDSNDMTPE DREQMQQGSA QVRQLLDTDT PPVPASDEEI
WEALWYYYYD VDKAVGFLRK KYTTKTPKKQ QQQQVKVKGA APSSSPYPVP MCPEPFSAAD
FFKDSPWLNI PTRRRADILI EPLYPRLGLL GGAQESSGKV SKLAALAARK RKESERKAAA
EALSGGVVTG SETSDGTQNQ QRKSHVSLLD RLAVDGKAQG ALPARSIHLP LRSGKNALNW
SSLKKPLQAS PDVAGTPEST TTVPGVPPNE KRKATAALSG ESTAQEVERP SKLPNLRAEP
SAFALVLVGA GGAEDGGDRD GGFISNPISH NIDVMRFFGQ DLTEAFDFAE PSPDDIVIKA
RESAKGNSNK NKTKRTTANK SSPGKNDDVV EGVGELSIQE TVKVKSKNID VLAEYRKTER
KKAANFVVIG HVDAGKSTLM GRLLYELKAV DQRTIDRYQK EADRIGKGSF ALAWVLDQGS
EERARGVTID IATNRFATEN TNFTILDAPG HRDFVPNMIA GASQADFAVL VLDATTGNFE
SGLRGQTKEH ALLVRSMGVQ RIVVAVNKMD AAGWSHDRFD EIQQQTASFL TTAGFQAKNI
SFVPCSGLRG DNVAQRAHDT NASWYTGRTL VEELDTSEPY TYALDKPLRM TITDVFRGGV
QNPLSISGRL DAGHLQVGDQ LTTMPSGETC TVRSLVVDET PSEWSVAGQN VTLHLTDIDP
AHVRIGDILC SPSAPVKNVT SFTAKVLAFD HLTPMHIEVH RGRLQVPGRI SRLVALLDKG
SGVAVKKRPK IVGPGGVARI VVELEEAIPL EAPGRVVLRA AVLCKFTKNT ADYKSTATKA
ARVAVAVTVT VSSPALLSHT QVEKCPFNHR ACIDPLQPFH RASIATPERG LLPRWKAPEP
LRQPRHRGTV LSHGRPANQR RRNRPQRPAR NCHSRTGRGR GRGARARSRL ARAVGSV
//
