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Database: UniProt
Entry: A0A423WJG3_9PEZI
LinkDB: A0A423WJG3_9PEZI
Original site: A0A423WJG3_9PEZI 
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
//
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