ID U1GQ33_ENDPU Unreviewed; 800 AA.
AC U1GQ33;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Tr-type G domain-containing protein {ECO:0000259|PROSITE:PS51722};
GN ORFNames=EPUS_08124 {ECO:0000313|EMBL:ERF74076.1};
OS Endocarpon pusillum (strain Z07020 / HMAS-L-300199) (Lichen-forming
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Verrucariales; Verrucariaceae; Endocarpon.
OX NCBI_TaxID=1263415 {ECO:0000313|EMBL:ERF74076.1, ECO:0000313|Proteomes:UP000019373};
RN [1] {ECO:0000313|Proteomes:UP000019373}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Z07020 / HMAS-L-300199 {ECO:0000313|Proteomes:UP000019373};
RX PubMed=24438332; DOI=10.1186/1471-2164-15-34;
RA Wang Y.-Y., Liu B., Zhang X.-Y., Zhou Q.-M., Zhang T., Li H., Yu Y.-F.,
RA Zhang X.-L., Hao X.-Y., Wang M., Wang L., Wei J.-C.;
RT "Genome characteristics reveal the impact of lichenization on lichen-
RT forming fungus Endocarpon pusillum Hedwig (Verrucariales, Ascomycota).";
RL BMC Genomics 15:34-34(2014).
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; KE720898; ERF74076.1; -; Genomic_DNA.
DR RefSeq; XP_007800276.1; XM_007802085.1.
DR AlphaFoldDB; U1GQ33; -.
DR GeneID; 19242975; -.
DR eggNOG; KOG0458; Eukaryota.
DR HOGENOM; CLU_007265_3_2_1; -.
DR OMA; FRMAISE; -.
DR OrthoDB; 5477300at2759; -.
DR Proteomes; UP000019373; 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; IPR004161; EFTu-like_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; PF03144; GTP_EFTU_D2; 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:UP000019373};
KW Translation regulation {ECO:0000256|ARBA:ARBA00022845}.
FT DOMAIN 389..610
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 181..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..196
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..231
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..268
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 800 AA; 88400 MW; D1DCFBFC78D6AA25 CRC64;
MSKHRIKSVA LEDDYADDYY DDDDQSGYVE DVGMTAEDQE RLRVGTVQVR NTLGQGFASI
TDKEIQDALW HYYYDISKSV SYLKNKHTPS QSKQEKTRPA KAGSQLAAQV HHQAVKEPNI
HHLLPSTAKD FFWDSPWLNI PLHRQAEIRV EPVFPRLGLL GGSSTGEGKM SKIAALAAKR
RLKEKENEKQ RVADTHTSGL PEDTASGLSK LRIATSHTLY PHKEHPLSSR HDLQSTSRID
QTQEPPPKGD ALPPSREQGK DKRTEDSHQP NGSQSGANVA DMRANPSMFA RTLMISCNTA
WPLSSRPPTL LPEPVISSFD FLKPSPDDIV LKAQNFKGSK TSTSSKQQKP AKAKESIINS
MENLSVVEPE TIKSKNLDVL AEYKKVERKN AANFVVIGHV DSGKSTLMGR LLFDLKAIDE
RTMEQYKEEA EKMGRGSFAF AWVLDQGTEE RARGVTIDIA SHKFQTERTS FTILDAPGHR
DFVPSMIGGA SQADFAVLVI DASPSEFEAG LRGQTKEHAL LVRSMGVARI VVAVNKMDRT
DWSKERFQDI QQQMLAFLTT AGFKSENISF VPCSGLQGDN ILTRSRAPQA AWYNGPTLVE
ELDTSEPVNH ALEKPLRMTL DDAFYDSVQN PFSVSGRIEA GSLQVGDQIV VMPSGIKTFI
RSIRVDDEPS DWAVAGQNVI LSLSITEADF DQINIGNMLC NPAFPVENVS SFTAKVLAFD
HLMPMPLDVH KGRLHIPGRI SRLAAVLNKI DDSVVKKKPQ VVHPGSVARI VVELDEPAPI
EAGRIILRAN GETVAAGHLE
//
