ID A0A1R1PYJ1_ZANCU Unreviewed; 818 AA.
AC A0A1R1PYJ1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Eukaryotic peptide chain release factor GTP-binding subunit {ECO:0000256|ARBA:ARBA00015765};
DE EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
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=AX774_g424 {ECO:0000313|EMBL:OMH86005.1};
OS Zancudomyces culisetae (Gut fungus) (Smittium culisetae).
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Harpellomycetes; Harpellales; Legeriomycetaceae; Zancudomyces.
OX NCBI_TaxID=1213189 {ECO:0000313|EMBL:OMH86005.1, ECO:0000313|Proteomes:UP000188320};
RN [1] {ECO:0000313|Proteomes:UP000188320}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COL-18-3 {ECO:0000313|Proteomes:UP000188320};
RA Wang Y., White M., Kvist S., Moncalvo J.-M.;
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
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 -!- 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:OMH86005.1}.
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DR EMBL; LSSK01000024; OMH86005.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R1PYJ1; -.
DR Proteomes; UP000188320; Unassembled WGS sequence.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:0003747; F:translation release factor activity; IEA:InterPro.
DR GO; GO:0016311; P:dephosphorylation; 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; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
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 InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR PANTHER; PTHR23115:SF36; TR-TYPE G DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR23115; TRANSLATION FACTOR; 1.
DR Pfam; PF00782; DSPc; 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 SMART; SM00195; DSPc; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
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.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
PE 3: Inferred from homology;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000188320};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 1..199
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT DOMAIN 432..483
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 368..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 687..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..718
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 818 AA; 89607 MW; 687603FF77993D57 CRC64;
MEKYEREAKD AGRESWYLSW ALDTNSEERA KGKTVECGRA FFETEKRRYT ILDAPGHKNF
VPSMLGGAAQ ADVGVLVISA RRGEFETGFD RGGQTREHAI LAKTSGVRQL IVVINKMDDP
TVQWDQGRYA DILAKLTPFL RTAGYNPKTD LIFLPVSGYT GANVKDRLAA GVAPWYSGPS
LLEVLDGLTA VDRKVNAPLR MPISDKFKDM GTVVGGKIES GFVKIGQKLV IMPNKRNCEV
SAIFGEDDGE IESAICGDNV RIRLRGVEEE DVSLGNVLSD PKNPCSTAVH FDAQLFILDA
KNIIAPGYTS VLHVHNLVEE VSIVRFLHLL DKKNPNKKSR VPPTFVKRGQ SCIATLTSSA
NADAFISNST STSASAPSSA PSSNSTSANS TGVICVERFK DYPQLGRFTL RDEGKTIAIV
LNVDDLPTSD ILQYFQPASL FINQQTSTPT PTQNENGNGN GNVLIHCVAG TSRSVTIALA
HYMRTHNCSP QAAYSCLLKS NNLEPSTTTT TTTDISVSLP VSVSMPMPND GFIYQLDLFY
KMGVSLTNIN SNQMYLNYIA LLEKTPEYFT SHLLSLSLAP LSQQKDQQQQ QQHQQQQQQE
QQMICRLRCK SCRKLILSYP NPKIPNLSIH PPHPKPSSSC TSIILDQPPS WLPLSSETSG
KLLCPHCSFK LGQFSWAGSD GFPNSDSKTP LLYSSPDESA PAHYPPTHPS PPTTHCDPPA
LHSSPVQSPV NYAPSPSPNP TVGLAAPLLT DVASPLLGRR FRYCTHIVLS LVPDTNFSLC
FKLCLFNPYF SGCFFATCIL NIQLFILPIP KPQFNVSL
//
