ID Q9HGI5_YARLL Unreviewed; 742 AA.
AC Q9HGI5;
DT 01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2001, sequence version 1.
DT 24-JAN-2024, entry version 80.
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 Name=sup35 {ECO:0000313|EMBL:BAB12683.1};
OS Yarrowia lipolytica (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=4952 {ECO:0000313|EMBL:BAB12683.1};
RN [1] {ECO:0000313|EMBL:BAB12683.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=11430816; DOI=10.1016/S1097-2765(01)00259-3;
RA Nakayashiki T., Ebihara K., Bannai H., Nakamura Y.;
RT "Yeast [PSI+] 'prions' that are crosstransmissible and susceptible beyond a
RT species barrier through a quasi-prion state.";
RL Mol. Cell 7:1121-1130(2001).
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}.
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DR EMBL; AB039752; BAB12683.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9HGI5; -.
DR VEuPathDB; FungiDB:YALI0_B08250g; -.
DR VEuPathDB; FungiDB:YALI1_B11083g; -.
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; 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; 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 PRINTS; PR00315; ELONGATNFCT.
DR PRINTS; PR01343; YEASTERF.
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; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 317..544
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 1..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 180..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..255
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..275
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 742 AA; 80125 MW; 3C8D3F5738206C0A CRC64;
MSDQFNQDFA NKANINEQGQ GQGQGQQGQG YGQYQAPQQF VPGQSFVPGQ SFVPGQSFAP
QGGYDQYQGQ GGYQGGYQGG YQGGYQGNNR GGYSGRGRGG YRGGYQGGYN NQYGNQGGYQ
GGYQGGYDNQ YGNQGGYQGG YDNQYGYDQP EEPQEKTLTL EEYQKQKQEA LNKLKKPKVG
GALKIGGDKP KAGGALKIGG DKPASTGGAL KIGGDKPKTS GGALKIGGDK PKSGGVLKIG
GDKESEKKEA VSKEASPAPK ESTPKESTPA PASKESTPSA AEKKEAAENA ASADALIAAQ
NAEIDQETIK EMFGETKDHM SIIFMGHVDV GKSTLGGQIL YLTGTVNKRT IEKMEKEAAD
AGRPGWYLSW VMDINKEERA EGKTVEVGRS YFETEKRRYT LLDAPGHKMY VPSMIGGAAQ
ADAGILVISA RKGEYETGFE RDGQTREHAM LAKTQGINKL VIAINKMDDS TVNWSKERYD
ECINKLKLYL KGLGYSDKTE ITFMPVSGFT GANVKERVSK EVCPWYDGPS LLELLDSFEL
ERNLTGPFML PISNKEKNLG TIVEGKIEVG QVKKGDNLVV MPSKVPVEVT TLYKETEQEV
GGASVGEQIR LKVKGIEEEE VQIGQVLCSA AQPVAAVTVF EAQIAITELK SILSTGFSCV
MHIHTAAEEV TFTALLHKLE KGTNRKSKKP PAFAKKGMKI IARLETQNPV CMDEFSKTPQ
LGRFTLRDQG QSIAIGRVTK LC
//
