ID M2RD06_CERS8 Unreviewed; 1485 AA.
AC M2RD06;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Tr-type G domain-containing protein {ECO:0000259|PROSITE:PS51722};
GN ORFNames=CERSUDRAFT_102668 {ECO:0000313|EMBL:EMD42320.1};
OS Ceriporiopsis subvermispora (strain B) (White-rot fungus) (Gelatoporia
OS subvermispora).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Gelatoporiaceae; Gelatoporia.
OX NCBI_TaxID=914234 {ECO:0000313|EMBL:EMD42320.1, ECO:0000313|Proteomes:UP000016930};
RN [1] {ECO:0000313|EMBL:EMD42320.1, ECO:0000313|Proteomes:UP000016930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B {ECO:0000313|EMBL:EMD42320.1,
RC ECO:0000313|Proteomes:UP000016930};
RX PubMed=22434909; DOI=10.1073/pnas.1119912109;
RA Fernandez-Fueyo E., Ruiz-Duenas F.J., Ferreira P., Floudas D.,
RA Hibbett D.S., Canessa P., Larrondo L.F., James T.Y., Seelenfreund D.,
RA Lobos S., Polanco R., Tello M., Honda Y., Watanabe T., Watanabe T.,
RA Ryu J.S., Kubicek C.P., Schmoll M., Gaskell J., Hammel K.E., St John F.J.,
RA Vanden Wymelenberg A., Sabat G., Splinter BonDurant S., Syed K.,
RA Yadav J.S., Doddapaneni H., Subramanian V., Lavin J.L., Oguiza J.A.,
RA Perez G., Pisabarro A.G., Ramirez L., Santoyo F., Master E., Coutinho P.M.,
RA Henrissat B., Lombard V., Magnuson J.K., Kuees U., Hori C., Igarashi K.,
RA Samejima M., Held B.W., Barry K.W., LaButti K.M., Lapidus A.,
RA Lindquist E.A., Lucas S.M., Riley R., Salamov A.A., Hoffmeister D.,
RA Schwenk D., Hadar Y., Yarden O., de Vries R.P., Wiebenga A., Stenlid J.,
RA Eastwood D., Grigoriev I.V., Berka R.M., Blanchette R.A., Kersten P.,
RA Martinez A.T., Vicuna R., Cullen D.;
RT "Comparative genomics of Ceriporiopsis subvermispora and Phanerochaete
RT chrysosporium provide insight into selective ligninolysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:5458-5463(2012).
CC -!- SIMILARITY: Belongs to the calreticulin family.
CC {ECO:0000256|ARBA:ARBA00010983}.
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DR EMBL; KB445791; EMD42320.1; -; Genomic_DNA.
DR STRING; 914234.M2RD06; -.
DR HOGENOM; CLU_002794_10_0_1; -.
DR OrthoDB; 166721at2759; -.
DR Proteomes; UP000016930; Unassembled WGS sequence.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR CDD; cd04098; eEF2_C_snRNP; 1.
DR CDD; cd04090; EF2_II_snRNP; 1.
DR CDD; cd01683; EF2_IV_snRNP; 1.
DR CDD; cd04167; Snu114p; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.70.240; -; 1.
DR Gene3D; 2.10.250.10; Calreticulin/calnexin, P domain; 1.
DR Gene3D; 3.30.70.870; Elongation Factor G (Translational Gtpase), domain 3; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR Gene3D; 3.90.1430.10; Yeast translation eEF2 (G' domain); 1.
DR InterPro; IPR001580; Calret/calnex.
DR InterPro; IPR018124; Calret/calnex_CS.
DR InterPro; IPR009033; Calreticulin/calnexin_P_dom_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR035647; EFG_III/V.
DR InterPro; IPR000640; EFG_V-like.
DR InterPro; IPR031950; EFTUD2_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR044121; Snu114_GTP-bd.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR005517; Transl_elong_EFG/EF2_IV.
DR InterPro; IPR035655; U5-116kDa_C.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR42908:SF6; 116 KDA U5 SMALL NUCLEAR RIBONUCLEOPROTEIN COMPONENT; 1.
DR PANTHER; PTHR42908; TRANSLATION ELONGATION FACTOR-RELATED; 1.
DR Pfam; PF00262; Calreticulin; 1.
DR Pfam; PF00679; EFG_C; 1.
DR Pfam; PF03764; EFG_IV; 1.
DR Pfam; PF16004; EFTUD2; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR PRINTS; PR00626; CALRETICULIN.
DR SMART; SM00838; EFG_C; 1.
DR SMART; SM00889; EFG_IV; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF54980; EF-G C-terminal domain-like; 2.
DR SUPFAM; SSF63887; P-domain of calnexin/calreticulin; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS00803; CALRETICULIN_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Membrane {ECO:0000256|SAM:Phobius};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW mRNA splicing {ECO:0000256|ARBA:ARBA00023187};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000016930};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1418..1441
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 137..344
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1171..1261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1445..1485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..29
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1187..1208
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1209..1252
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1485 AA; 166505 MW; E97991F2D82600E4 CRC64;
MASFEDYDEF GNYIGADLDS DDEEIQQEEF APQPEARPLE GFDEEPMEEV HEDTALMQID
EPSHNAVILH EDKQYYPSAE EVYGADVETL VQEEDAQPLT EPIIAPVKLR KWTVEEKNMP
ETRFDKGFLL NMTAFPEFIR NVAVVGHLHH GKTALMDMLV FETHKLVWDS DHQTRYTDTH
ILSRERGISI KSSPMSLVLT SSSGKSHLVH FIDTPGHVNF VDEVASSIRL ADGIVLVVDV
VEGVMVNTEH IIRHAIQEGL KVTLVVNKID RLILELRIKP ADAYYKIKHT IEEVNTIISG
IDPNPELRLS PEKGNVAFAS ADMHWCFTLR SFAQMYADTY GSMDVSAFAD RLWGNIYFNN
DDRKFTRKPA DPESNRTFVH FILEPLYKLY SQVLSEDTDS LKETLQNLGI ELHPVMYKMD
VRPLLKAVLD QFFGPSVGLV DMIVEHIPSP LQGTDDKVER TYTGPMSSEL VQRMKACDPE
GPVMVQITKL YHTTDAQAFR AFGRVISGTV RKGMDIKVLG EGYSPEDEED MVKVAVEDIW
ISEARYFIPA GEVPAGNLVL LGGVDASITK TATLASVDIE DDLYIFRPIK HMTQSVLKIA
IEPIAPSELP KMLSGLRSIN KSYPLVSTKV EESGEHVLIG TGELYLDCVM HDLRRLFSEI
EIKVSDPVTK FCETVLETSA LKCYADTPNK KNRITMIAEP LERGIAEDIE TGRVTMRMTP
KERGKFFEEK YQWDLLASRS IWAFGPDDSG PNILLDDTLP SQVDKKLLGT VKEHIKQGFQ
WGAREGPLCD EPMRNVKFRI LDASLAQEPI FRGGGQIVPT ARRVCYSSFL MATPRLMEPI
YYVEVQAPAD CISAVYTVLA RRRGHVTQDI PKAGSPLYTV KALIPVIDAN GFETDLRTAT
QGQAFCLQVF DHWSIVPGDP TDTSIKLRPL EPASGQALAR DLVLKTRRRK GLGDQIAVSK
YLDDEFISTG IKAPFLEQFT DDYSDRWTPS EATKKTPVGG ETFSYVGKWE VEEPIDLVIE
GDKGLVAKTK AAHHAISAPF AKSVEFADEP LVVQYEVKYQ KGGNCGGGYL KLLEDGFQTE
GKEFSDKTPW TIMFGPDLTC PGTKAHFIFR HKNPITGEYE EKHLKTPPKP AIADKFSHLY
TLIVYPNNTY DVQFDGESHN LGSLLEDFVP SVNPDAEIDD PEDEKPEDWV DQKRIPDPEA
TKPEDWDEDA PYEIPDEEAE KPEGWLDDEP DTVPDPDAEK PEEWDDEEDG DWIAPMVSNP
KCDEAPGCGE WKRPMKANPA YKGKWYAPMI DNPAYIGEWA PRKIPNPEFF EDLTPFKSLK
AIGGVGIELW TMSEDILFDN IYIGHSVEDA KKFAEETFNV KKPLEKAKST PKVEDVVEQE
VFFKEDPIEY IRAKVFTFIE LARIDPLLAF KTQPETGAAL ALSVVTLFGM LGVMFGVIGS
AQKPITKSAK KTDAPSPDDK SKKESAPVTP AGGEKAADST VKKRK
//
