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Database: UniProt
Entry: M2QLM6_CERS8
LinkDB: M2QLM6_CERS8
Original site: M2QLM6_CERS8 
ID   M2QLM6_CERS8            Unreviewed;       618 AA.
AC   M2QLM6;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=Tr-type G domain-containing protein {ECO:0000259|PROSITE:PS51722};
GN   ORFNames=CERSUDRAFT_114562 {ECO:0000313|EMBL:EMD37913.1};
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:EMD37913.1, ECO:0000313|Proteomes:UP000016930};
RN   [1] {ECO:0000313|EMBL:EMD37913.1, ECO:0000313|Proteomes:UP000016930}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B {ECO:0000313|EMBL:EMD37913.1,
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 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; KB445796; EMD37913.1; -; Genomic_DNA.
DR   AlphaFoldDB; M2QLM6; -.
DR   HOGENOM; CLU_012821_0_1_1; -.
DR   OrthoDB; 129286at2759; -.
DR   Proteomes; UP000016930; Unassembled WGS sequence.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   CDD; cd04165; GTPBP1_like; 1.
DR   CDD; cd03694; GTPBP_II; 1.
DR   CDD; cd03708; GTPBP_III; 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; IPR035531; GTPBP1-like.
DR   InterPro; IPR027417; P-loop_NTPase.
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; PTHR43721; ELONGATION FACTOR TU-RELATED; 1.
DR   PANTHER; PTHR43721:SF9; GTP-BINDING PROTEIN 1; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   Pfam; PF03143; GTP_EFTU_D3; 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; 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   Reference proteome {ECO:0000313|Proteomes:UP000016930}.
FT   DOMAIN          187..428
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   REGION          31..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..46
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   618 AA;  67597 MW;  A34B7BC62ED3770D CRC64;
     MTSLRTFQHE IDEIQHREIS KQRVLGAAEL QRAKEKEHKK AAPAKASEAK NETAANQTPV
     PIPAEDDGDA PDLDVRIQTL LLSKTPSDHD KARDLILSQL TRRRGEYIIR IGARPAHAKL
     FAGEAATDDD QWHGTPCTED ELNTLVIDVT HIVEESGGKA SVLFEARAEH PRAALLLRLP
     PANVSLTPEV RCAVVGNVDS GKSTTLGVLT RGGLDDGRGR ARVSLFRHKH EIESGRTSSV
     GMEILGFDLT GIPILPSTSF SNDLDVIRRE KMSWEEISTR AAKIISFSDL AGHERYLKTT
     LYGLTSGAPS CVILIVGGNA GLIGMSKEHL AIALALSVPV VVCITKIDMT PPNVLTKTIE
     QVTKIMKSPG CRKTPIFVKS LETAVEVSQV FAKERLCPIF QLSNVTGQGH DFLRTFLNLL
     PASEGDSEKF MKDQPLEYSV TEVWSVPYVG TVVDGILNSG TIKAGDAVLL GPDSNGHFQS
     TVVKSIQRKR APVNSAEAGQ CVSLALKRVR RAAVRKGMVL VHKSEVPPRA VRQFEGQVLI
     LYHNTTLQQN YQAMLHCGAV RQTVRIISMD HPQGILRTGD RATVTFEFIS HPEFIKEGMK
     LLFREGKTKG LGVITKLL
//
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