ID A9T682_PHYPA Unreviewed; 428 AA.
AC A9T682; K9Y4B3;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 24-JAN-2024, entry version 104.
DE SubName: Full=EF1Bgamma class glutathione S-transferase {ECO:0000313|EMBL:AFZ39149.1};
GN Name=EF1Bgamma4 {ECO:0000313|EMBL:AFZ39149.1};
GN ORFNames=PHYPA_024261 {ECO:0000313|EMBL:PNR34444.1};
OS Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; Physcomitrium.
OX NCBI_TaxID=3218 {ECO:0000313|EMBL:AFZ39149.1};
RN [1] {ECO:0000313|EMBL:PNR34444.1, ECO:0000313|Proteomes:UP000006727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c19_17550V3.1,
RC ECO:0000313|Proteomes:UP000006727};
RX PubMed=18079367; DOI=10.1126/science.1150646;
RA Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H.,
RA Nishiyama T., Perroud P.-F., Lindquist E.A., Kamisugi Y., Tanahashi T.,
RA Sakakibara K., Fujita T., Oishi K., Shin-I T., Kuroki Y., Toyoda A.,
RA Suzuki Y., Hashimoto S.-I., Yamaguchi K., Sugano S., Kohara Y.,
RA Fujiyama A., Anterola A., Aoki S., Ashton N., Barbazuk W.B., Barker E.,
RA Bennetzen J.L., Blankenship R., Cho S.H., Dutcher S.K., Estelle M.,
RA Fawcett J.A., Gundlach H., Hanada K., Heyl A., Hicks K.A., Hughes J.,
RA Lohr M., Mayer K., Melkozernov A., Murata T., Nelson D.R., Pils B.,
RA Prigge M., Reiss B., Renner T., Rombauts S., Rushton P.J., Sanderfoot A.,
RA Schween G., Shiu S.-H., Stueber K., Theodoulou F.L., Tu H., Van de Peer Y.,
RA Verrier P.J., Waters E., Wood A., Yang L., Cove D., Cuming A.C., Hasebe M.,
RA Lucas S., Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S.,
RA Boore J.L.;
RT "The Physcomitrella genome reveals evolutionary insights into the conquest
RT of land by plants.";
RL Science 319:64-69(2008).
RN [2] {ECO:0000313|EMBL:AFZ39149.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23188805; DOI=10.1104/pp.112.205815;
RA Liu Y.J., Han X.M., Ren L.L., Yang H.L., Zeng Q.Y.;
RT "Functional Divergence of the GST Supergene Family in Physcomitrella patens
RT Reveals Complex Patterns of Large Gene Family Evolution in Land Plants.";
RL Plant Physiol. 0:0-0(2012).
RN [3] {ECO:0000313|EMBL:AFZ39149.1}
RP NUCLEOTIDE SEQUENCE.
RA Nishi O., Iiyama K., Yasunaga-Aoki C., Shimizu S.;
RT "The phylogenetic status and pathogenicity of a new isolate of Metarhizium
RT sp. from a fruit beetle larvae in Japan.";
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:PNR34444.1, ECO:0000313|Proteomes:UP000006727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c19_17550V3.1,
RC ECO:0000313|Proteomes:UP000006727};
RX PubMed=29237241; DOI=10.1111/tpj.13801;
RA Lang D., Ullrich K.K., Murat F., Fuchs J., Jenkins J., Haas F.B.,
RA Piednoel M., Gundlach H., Van Bel M., Meyberg R., Vives C., Morata J.,
RA Symeonidi A., Hiss M., Muchero W., Kamisugi Y., Saleh O., Blanc G.,
RA Decker E.L., van Gessel N., Grimwood J., Hayes R.D., Graham S.W.,
RA Gunter L.E., McDaniel S.F., Hoernstein S.N.W., Larsson A., Li F.W.,
RA Perroud P.F., Phillips J., Ranjan P., Rokshar D.S., Rothfels C.J.,
RA Schneider L., Shu S., Stevenson D.W., Thummler F., Tillich M.,
RA Villarreal Aguilar J.C., Widiez T., Wong G.K., Wymore A., Zhang Y.,
RA Zimmer A.D., Quatrano R.S., Mayer K.F.X., Goodstein D., Casacuberta J.M.,
RA Vandepoele K., Reski R., Cuming A.C., Tuskan G.A., Maumus F., Salse J.,
RA Schmutz J., Rensing S.A.;
RT "The Physcomitrella patens chromosome-scale assembly reveals moss genome
RT structure and evolution.";
RL Plant J. 93:515-533(2018).
RN [5] {ECO:0000313|EnsemblPlants:Pp3c19_17550V3.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (DEC-2020) to UniProtKB.
CC -!- FUNCTION: Probably plays a role in anchoring the complex to other
CC cellular components. {ECO:0000256|ARBA:ARBA00003468}.
CC -!- SUBUNIT: EF-1 is composed of four subunits: alpha, beta, delta, and
CC gamma. {ECO:0000256|ARBA:ARBA00011237}.
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DR EMBL; KC119484; AFZ39149.1; -; mRNA.
DR EMBL; ABEU02000019; PNR34444.1; -; Genomic_DNA.
DR RefSeq; XP_001774148.1; XM_001774096.1.
DR AlphaFoldDB; A9T682; -.
DR STRING; 3218.A9T682; -.
DR PaxDb; 3218-PP1S172_22V6-1; -.
DR EnsemblPlants; Pp3c19_17550V3.1; Pp3c19_17550V3.1; Pp3c19_17550.
DR EnsemblPlants; Pp3c19_17550V3.2; Pp3c19_17550V3.2; Pp3c19_17550.
DR Gramene; Pp3c19_17550V3.1; Pp3c19_17550V3.1; Pp3c19_17550.
DR Gramene; Pp3c19_17550V3.2; Pp3c19_17550V3.2; Pp3c19_17550.
DR eggNOG; KOG0867; Eukaryota.
DR eggNOG; KOG1627; Eukaryota.
DR HOGENOM; CLU_011226_3_0_1; -.
DR InParanoid; A9T682; -.
DR OMA; GYESYTW; -.
DR OrthoDB; 159792at2759; -.
DR Proteomes; UP000006727; Chromosome 19.
DR GO; GO:0004364; F:glutathione transferase activity; IEA:InterPro.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042221; P:response to chemical; IEA:UniProt.
DR CDD; cd03181; GST_C_EF1Bgamma_like; 1.
DR CDD; cd03044; GST_N_EF1Bgamma; 1.
DR Gene3D; 1.20.1050.10; -; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR Gene3D; 3.30.70.1010; Translation elongation factor EF1B, gamma chain, conserved domain; 1.
DR InterPro; IPR044628; EF-1-gamma_plant.
DR InterPro; IPR001662; EF1B_G_C.
DR InterPro; IPR036433; EF1B_G_C_sf.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR040079; Glutathione_S-Trfase.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR44372; ELONGATION FACTOR 1-GAMMA 1-RELATED; 1.
DR PANTHER; PTHR44372:SF1; ELONGATION FACTOR 1-GAMMA 1-RELATED; 1.
DR Pfam; PF00647; EF1G; 1.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF02798; GST_N; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SFLD; SFLDG00358; Main_(cytGST); 1.
DR SMART; SM01183; EF1G; 1.
DR SUPFAM; SSF89942; eEF1-gamma domain; 1.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS50040; EF1G_C; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 2: Evidence at transcript level;
KW Elongation factor {ECO:0000256|ARBA:ARBA00022768, ECO:0000256|PROSITE-
KW ProRule:PRU00519};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|PROSITE-
KW ProRule:PRU00519}; Reference proteome {ECO:0000313|Proteomes:UP000006727};
KW Transferase {ECO:0000313|EMBL:AFZ39149.1}.
FT DOMAIN 2..82
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT DOMAIN 86..212
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
FT DOMAIN 268..428
FT /note="EF-1-gamma C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50040"
FT REGION 209..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..263
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 428 AA; 48412 MW; 356519DAF9C3553C CRC64;
MAGLKLYANP VNKNAYKALI AAEYVGVKIE FTEITDWSTT KSPQYLAMNP MGKVPVLETP
EGSIFESNAI ARYVAGLKDV GLLGVPGYNK AQIDQWIDFA ALEIDINARA WVLPHLGLGF
FNEEVEAFII NNLKRALTTL NSYLASRTYL VGESVTLADI VLICNLSFIW RRAATKEFTA
EYPHVERYFW TLINQPNFKK VFGEFTQADK PLGPPPSKGE TVAPPAAEKK STPEKEKVKK
EKPAPAPKPV PEPEAALDDE EAAPVKKTKN ALDLLPPTPM VLDNWKRLYS NTKAKDFHLA
ISGFWEMFDA EGWSLWFCDY KYNDENQVTF VTMNKVGGFL QRMDLARKYS FGKMCILGEN
PPYKIKGVWL FRGLDVPQMV LDEVYDAELY EWTKVDITNE EQKALVNAYF EEPDTIQGEK
LLEAKCFK
//
