ID A0A423WJG3_9PEZI Unreviewed; 1022 AA.
AC A0A423WJG3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Eukaryotic peptide chain release factor GTP-binding subunit {ECO:0000256|ARBA:ARBA00015765};
DE AltName: Full=ERF-3 {ECO:0000256|ARBA:ARBA00031881};
DE AltName: Full=ERF2 {ECO:0000256|ARBA:ARBA00030845};
DE AltName: Full=Polypeptide release factor 3 {ECO:0000256|ARBA:ARBA00029585};
DE AltName: Full=Translation release factor 3 {ECO:0000256|ARBA:ARBA00030210};
GN ORFNames=VSDG_01404 {ECO:0000313|EMBL:ROW03562.1};
OS Valsa sordida.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX NCBI_TaxID=252740 {ECO:0000313|EMBL:ROW03562.1, ECO:0000313|Proteomes:UP000284375};
RN [1] {ECO:0000313|EMBL:ROW03562.1, ECO:0000313|Proteomes:UP000284375}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YSFL {ECO:0000313|EMBL:ROW03562.1,
RC ECO:0000313|Proteomes:UP000284375};
RA Yin Z., Huang L.;
RT "Host preference determinants of Valsa canker pathogens revealed by
RT comparative genomics.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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 -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000256|ARBA:ARBA00006375}.
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:ROW03562.1}.
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DR EMBL; LJZO01000003; ROW03562.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A423WJG3; -.
DR STRING; 252740.A0A423WJG3; -.
DR Proteomes; UP000284375; Unassembled WGS sequence.
DR GO; GO:0005743; C:mitochondrial inner membrane; 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:0003747; F:translation release factor activity; IEA:InterPro.
DR GO; GO:0000288; P:nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IEA:InterPro.
DR CDD; cd01883; EF1_alpha; 1.
DR CDD; cd03704; eRF3_C_III; 1.
DR CDD; cd04089; eRF3_II; 1.
DR Gene3D; 1.50.40.10; Mitochondrial carrier domain; 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; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003285; Sup35.
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:SF36; TR-TYPE G DOMAIN-CONTAINING 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; PF00153; Mito_carr; 3.
DR PRINTS; PR00315; ELONGATNFCT.
DR PRINTS; PR01343; YEASTERF.
DR SUPFAM; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1.
DR SUPFAM; SSF103506; Mitochondrial carrier; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS51722; G_TR_2; 1.
DR PROSITE; PS50920; SOLCAR; 3.
PE 3: Inferred from homology;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE-
KW ProRule:PRU00282}; Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000284375};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|PROSITE-
KW ProRule:PRU00282}; Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 280..507
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REPEAT 730..820
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REPEAT 830..916
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REPEAT 925..1015
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..206
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1022 AA; 111030 MW; 1A4DC57AE3498229 CRC64;
MSNLNSWEDD PAAQEENLAQ QAQQMNLGNQ GRVPPTFHPG AAAFSPGAAA FQPGQSYGAG
YGMPQYQQGY YGGQQQAYGQ YSQYGGQQAY GQYGQTGYGN IYGQGQYNPI GGQYQGYQQG
QQLGQQQQAP AQAPKQTPTI AKRPTDATAA SSESGPKATV AKEGGTKVLS IGGDTAPKPK
AKVLSIGGTV PPKEPKKEEA DEEAAPEAGA KVAAAKAIEK TGEKTGSDKS ASGKTSPTPS
SGRSSPSRTA AKAAARDAAA VEQEQSADVD EETLKEMYGK EHVNIIFIGH VDAGKSTLGG
AILVVTGMVD QRTLDKYKRE AREMGRETWY LSWALDLTNE ERSKGKTVEV GRGYFETEKR
KYSILDAPGH KTYVPNMIGG ASQADVGILV ISARKGEYET GFEKGGQTRE HAMLAKTQGV
NKLVVAINKM DDPTVEWSQE RYKECTTKLS TFLKGTGYNL KTDVFFMPIA AQSLLNIKER
LPEGVAPWYN GPSLLEYLDG MTALERKVNA PFMMAIAGKY RDMGTMVEGR VEAGVVKKGM
KLTMMPNKAQ IDIAAVYGEQ EDEIPHAQCG DQVRMRLRGV EEDDILPGFV ICSPKRLVHC
VKQFDAQIRI LDLKSILSAG FNCVLHVHAA IEEVTFSALL HTLQKGTGRK SKRPPTHAKK
GDNIIARMEV TSTSGAVCIE RFEDYPQMGR FTLSIYACLS QSKHFSSVLP HQSISPTFKA
AVKMSQEKPL PFIYQFAAGA VAGVSEILVM YPLDVVKTRV QLQTGKGTGA DHYNGMLDCF
RKIVKNEGFS RLYRGITAPI LMEAPKRATK FAANDEWGKV YRKAFGADKM NQSLSILTGA
TAGATESFVV VPFELVKIRL QDKASAGKYN GMIDVVTKTV KQEGILAMYN GLESTLWRHI
LWNAGYFGCI FQVRQLLPQA KDKSGQMVND IMAGTIGGTV GTIVNTPMDV VKSRIQNSVK
VAGVVPKYNW AWPAVATVMK EEGFGALYKG FLPKVLRLGP GGGILLVVFQ GVMDFFRNMK
QD
//