ID A0A0G2F992_9PEZI Unreviewed; 2031 AA.
AC A0A0G2F992;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Putative gtp-binding protein {ECO:0000313|EMBL:KKY30771.1};
GN ORFNames=UCDDA912_g09292 {ECO:0000313|EMBL:KKY30771.1};
OS Diaporthe ampelina.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Diaporthaceae; Diaporthe.
OX NCBI_TaxID=1214573 {ECO:0000313|EMBL:KKY30771.1, ECO:0000313|Proteomes:UP000034680};
RN [1] {ECO:0000313|EMBL:KKY30771.1, ECO:0000313|Proteomes:UP000034680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DA912 {ECO:0000313|EMBL:KKY30771.1};
RA Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT "Distinctive expansion of gene families associated with plant cell wall
RT degradation and secondary metabolism in the genomes of grapevine trunk
RT pathogens.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KKY30771.1, ECO:0000313|Proteomes:UP000034680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DA912 {ECO:0000313|EMBL:KKY30771.1};
RA Morales-Cruz A., Amrine K.C., Cantu D.;
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Promotes mitochondrial protein synthesis. May act as a
CC fidelity factor of the translation reaction, by catalyzing a one-codon
CC backward translocation of tRNAs on improperly translocated ribosomes.
CC Binds to mitochondrial ribosomes in a GTP-dependent manner.
CC {ECO:0000256|HAMAP-Rule:MF_03137}.
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; EC=3.6.5.n1;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03137};
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_03137}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_03137}; Matrix side {ECO:0000256|HAMAP-Rule:MF_03137}.
CC -!- SIMILARITY: Belongs to the GTP-binding elongation factor family. LepA
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_03137}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. LepA subfamily.
CC {ECO:0000256|ARBA:ARBA00005454}.
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:KKY30771.1}.
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DR EMBL; LCUC01000445; KKY30771.1; -; Genomic_DNA.
DR STRING; 1214573.A0A0G2F992; -.
DR OrthoDB; 7997at2759; -.
DR Proteomes; UP000034680; Unassembled WGS sequence.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-UniRule.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043022; F:ribosome binding; IEA:UniProtKB-UniRule.
DR GO; GO:0045727; P:positive regulation of translation; IEA:UniProtKB-UniRule.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
DR CDD; cd03699; EF4_II; 1.
DR CDD; cd16260; EF4_III; 1.
DR CDD; cd01890; LepA; 1.
DR CDD; cd03709; lepA_C; 1.
DR CDD; cd02656; MIT; 1.
DR Gene3D; 3.30.70.240; -; 1.
DR Gene3D; 3.30.70.2570; Elongation factor 4, C-terminal domain; 1.
DR Gene3D; 3.30.70.870; Elongation Factor G (Translational Gtpase), domain 3; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.20.58.80; Phosphotransferase system, lactose/cellobiose-type IIA subunit; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR HAMAP; MF_00071; LepA; 1.
DR InterPro; IPR006297; EF-4.
DR InterPro; IPR041095; EFG_II.
DR InterPro; IPR035647; EFG_III/V.
DR InterPro; IPR000640; EFG_V-like.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR038363; LepA_C_sf.
DR InterPro; IPR013842; LepA_CTD.
DR InterPro; IPR035654; LepA_IV.
DR InterPro; IPR007330; MIT_dom.
DR InterPro; IPR036181; MIT_dom_sf.
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 NCBIfam; TIGR01393; lepA; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR37327; CHROMOSOME 1, WHOLE GENOME SHOTGUN SEQUENCE; 1.
DR PANTHER; PTHR37327:SF1; MIT DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00679; EFG_C; 1.
DR Pfam; PF14492; EFG_III; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF06421; LepA_C; 1.
DR Pfam; PF04212; MIT; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF54980; EF-G C-terminal domain-like; 2.
DR SUPFAM; SSF116846; MIT 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 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_03137};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_03137};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_03137};
KW Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03137};
KW Mitochondrion inner membrane {ECO:0000256|HAMAP-Rule:MF_03137};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_03137}; Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_03137};
KW Reference proteome {ECO:0000313|Proteomes:UP000034680}.
FT DOMAIN 1427..1613
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 37..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 155..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 495..690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 798..1014
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1083..1105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1396..1415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 733..774
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 37..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..86
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..204
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..380
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..400
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..424
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..525
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..591
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 625..652
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 659..675
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 824..863
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 864..878
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 971..988
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1396..1411
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1436..1443
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03137"
FT BINDING 1501..1505
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03137"
FT BINDING 1555..1558
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03137"
SQ SEQUENCE 2031 AA; 221642 MW; 88AF0FBF489D860D CRC64;
MPSPHANAHA HHTGSVSAAS NTSLPQSAFN FHLNSASFSN STFNSVPDPT SRATTPASQV
TVGPRKPHYH QHNQPLPPPP PQQQQNQHHP HPQQQQQHHQ YHDSSAHISR PIYGSAQYNP
TRPLHIANSA THISSAVNLT PSFSSASLPR TSSLLPPPSL TVDQSSWNQP ALHDPFSNAP
TAVPTPADPV NDREFDDSVS PKNTRRQHSK SHSRSSSLGG LSDGFRNLNR WSISTASSRA
SNPASAKRFS RRMSIDSTAL FSQSSSASPR RLHKSRPSTA GGSPEDLHNH QQQPAVPPLT
TLPPIVQLPS LSQDDLVGAA LSGRDPRPER ATYFPGPGAE SESGAFWDDS SRVGETPYLS
TSTRATPDPS LPTSAFSRDA NMPHTEDGAA YREKGHSRSR SQGLKSSTDS TSSQRNPNRS
KQPSQKAMLS KALQKANIAV QLDNAQNFQG ARSAYREACD LLHQVLLRTA GDEDKKKLEA
IRKTYASRIE ELDQMLPDDE QDSKALPQRP TSNSTTSTSQ VAGRARNGSV AAADDQPQRL
RSDSERSQPS QRPVPNYARP TSAAWRPQHS PKPSLDGSRY VTPTPTNFNT FLARPMEDEY
KPPPLSPRRP ISPTAKLGPD VSIRADFSSD TNRLAPAPSS QRGHQRGNSH ESISWLDPID
ESAGSSASSV HSRSSSMGIR RKHIRSASGD TEAEFDAALD DAIEAAYDDG YESTDPAQRV
LNLDHVIDED DVIAQALKKV QLAKERVRQS ELEMQRLAND RDRRMKALQE EEQTLPGGFY
DGDDSDDEER MLEEMTTGYA IENFTLGDQS RNRMPRESDS SELTSRTWHS STVSNPPTAN
TVLSPVTEST TLPSLSKSQG PIAPPPSQSL PKLPPGRPPS SAGRDSVRDR RLSGTNAKQL
KIETQKLGPK VQEPATAGPM MQSKESLGGQ HPKTAGFVGQ QRQTLAAAPG SGPGPARSAS
QLRGPSPIPP GLAAQGAPPT PPVPAGFEGP PEGRAESPAV SRPPALRKNF SSNSLKTMKT
RNLSITNIDE YSDVSPGTPL SNQFGSAPAA RLPALPSLPT PVAAAFRDRV TSGSAAGGFH
LFDNDIHSPA SPGDTNAPSE DAPLPLEPCP TDVMLRPFWL MRALYQTLAH PKGGYISNKL
FVPRDAWRVK GVKIKGMEEK ASQCDLLTAA LQKLARVDSE DADALLEEMQ SFENVLEQAQ
VFLTRRLGNE VGVQGAGTMF KDADGVVESD GKPVPRNNSV SAKGAFSWRR LRSKTSSTGL
GSAYERGGSK KEVPIAGGVE AMSLATLPMT NHPSSKPGKR DAMGVQFSGP NAHYMAALAR
LFDAAQTIDQ IARQVEDPGL RHADKTQVGL ELCTRHAAEF FAFYICRFVL QDLTLLLDKF
IKRGIYLRPG TLRSYATASS PSTSTPASAS RKGPTDLERR IAAIPLDRFR NFCVIAHIDH
GKSTLSDRLL ELTGTISKDD ENKQILDKLD VERERGITVK AQTCTMMYKY RGQDYLLHLV
DTPGHVDFRA EVTRSYASCG GALLLVDASQ GIQAQTVANF YTAFAQELVM VPVVNKIDLP
TADVERAVSQ LKDTFEIGAE DHEGGAPVLV SAKSGKNVEA ILPAVVERIP PPDGDCSRPL
RLLLVDSWYD TFRGVNLLVR LFDGTIRAGD QVVSLATGKK YTVGEVGIHY PHQVPQTILR
AGQVGYILFN PGMKRIQDAK IGDTFTTLGN EDKVEMYPGF EEPKPMVFVG AFPTDQSDYT
KMSESINQLV LNDRSITLQK DHSEALGAGW RLGFLGSLHC SVFQDRLRQE YGASVIITEP
SVPSRIVYAD GKEVIITNPA EFPSDDDHRA RAATFYEPFV HAMITLPEEY LGRVIELCEG
SRGEQVSIEF FHATQVILKY DLPASALVDD LFGKLKGATK GYATLDYEDA GWRESRLQKL
QLLVNKKPVD AICRVVHASQ VDRLGKYWTA RFKEHVDRQM FEVVIQAAVG RRIIARETLK
PFRKDVLAKL HASDISRRKK LLDKQKDGRK KLNAIGNVTI AQESFQKFLT K
//
