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Database: UniProt
Entry: A0A165DH63_9APHY
LinkDB: A0A165DH63_9APHY
Original site: A0A165DH63_9APHY 
ID   A0A165DH63_9APHY        Unreviewed;       534 AA.
AC   A0A165DH63;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   28-JUN-2023, entry version 24.
DE   SubName: Full=GTPase {ECO:0000313|EMBL:KZT04870.1};
GN   ORFNames=LAESUDRAFT_657005 {ECO:0000313|EMBL:KZT04870.1};
OS   Laetiporus sulphureus 93-53.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Laetiporus.
OX   NCBI_TaxID=1314785 {ECO:0000313|EMBL:KZT04870.1, ECO:0000313|Proteomes:UP000076871};
RN   [1] {ECO:0000313|EMBL:KZT04870.1, ECO:0000313|Proteomes:UP000076871}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-53 {ECO:0000313|EMBL:KZT04870.1,
RC   ECO:0000313|Proteomes:UP000076871};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
CC   -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase
CC       superfamily. OBG GTPase family. {ECO:0000256|ARBA:ARBA00007699}.
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DR   EMBL; KV427633; KZT04870.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165DH63; -.
DR   STRING; 1314785.A0A165DH63; -.
DR   InParanoid; A0A165DH63; -.
DR   OrthoDB; 232786at2759; -.
DR   Proteomes; UP000076871; 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:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-UniRule.
DR   CDD; cd01898; Obg; 1.
DR   Gene3D; 2.70.210.12; GTP1/OBG domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR031167; G_OBG.
DR   InterPro; IPR006073; GTP-bd.
DR   InterPro; IPR014100; GTP-bd_Obg/CgtA.
DR   InterPro; IPR006169; GTP1_OBG_dom.
DR   InterPro; IPR036726; GTP1_OBG_dom_sf.
DR   InterPro; IPR045086; OBG_GTPase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR11702; DEVELOPMENTALLY REGULATED GTP-BINDING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR11702:SF31; MITOCHONDRIAL RIBOSOME-ASSOCIATED GTPASE 2; 1.
DR   Pfam; PF01018; GTP1_OBG; 2.
DR   Pfam; PF01926; MMR_HSR1; 1.
DR   PIRSF; PIRSF002401; GTP_bd_Obg/CgtA; 2.
DR   SUPFAM; SSF82051; Obg GTP-binding protein N-terminal domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51710; G_OBG; 1.
DR   PROSITE; PS51883; OBG; 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:UP000076871}.
FT   DOMAIN          16..264
FT                   /note="Obg"
FT                   /evidence="ECO:0000259|PROSITE:PS51883"
FT   DOMAIN          265..516
FT                   /note="OBG-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51710"
SQ   SEQUENCE   534 AA;  58789 MW;  4B0555E3545C6E4C CRC64;
     MRRKRRTEWK RRQGGQAFLD HAVVHICAGK GGDGCVAFHR EKFVPYGPPS GGSGGRGGDV
     YIMATPHLTT LSSVPTRVHA PNGGTGQGSW QNGKNAPPFV IKVPVGTIVR QLPRDDPRSS
     KDEIDMEAEM LDALDPDERR TKLRELRWVH YPRAEDDNVE RQDFKDAERL VYREERERRL
     MQQRRLLQTI YLDLDKPDSS LEERDPNSPL GLRRPDSLGH LIASGGSGGV GNTHFLTLTN
     RSPKWATRGW EGERVTLSLE LKLLADVALV GMPNAGKSTL LRALSGGRAK TEIAGYAFTT
     LNPVVAVIRV ADDGSFEGSN GLVHEETWLE EQREQALIKQ GLLADARTRN QRDDAGADPL
     DTLESFRFTV ADNPGLIAEA SADIGLGHSF LRSIERSNAL AYVVDLSAPA PWDDLSVLRD
     EIEKYKPGLS PKARIVLANK ADLLGGQAGQ EDAEAVREAK EKLRKLEEFV EKEMRTPVQD
     GEGSVLDKRT LDVVPISAKY SMNLQKVVNL MRSYVEDARA GGIQPSSGPQ ASSS
//
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