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Database: UniProt
Entry: G7E997_MIXOS
LinkDB: G7E997_MIXOS
Original site: G7E997_MIXOS 
ID   G7E997_MIXOS            Unreviewed;      1041 AA.
AC   G7E997;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 50.
DE   RecName: Full=Obg-like ATPase 1 {ECO:0000256|HAMAP-Rule:MF_03167};
GN   Name=Mo05909 {ECO:0000313|EMBL:GAA99216.1};
GN   ORFNames=E5Q_05909 {ECO:0000313|EMBL:GAA99216.1};
OS   Mixia osmundae (strain CBS 9802 / IAM 14324 / JCM 22182 / KY 12970).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina; Mixiomycetes;
OC   Mixiales; Mixiaceae; Mixia.
OX   NCBI_TaxID=764103 {ECO:0000313|EMBL:GAA99216.1, ECO:0000313|Proteomes:UP000009131};
RN   [1] {ECO:0000313|Proteomes:UP000009131}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 9802 / IAM 14324 / JCM 22182 / KY 12970
RC   {ECO:0000313|Proteomes:UP000009131};
RX   PubMed=21478649; DOI=10.2323/jgam.57.63;
RA   Nishida H., Nagatsuka Y., Sugiyama J.;
RT   "Draft genome sequencing of the enigmatic basidiomycete Mixia osmundae.";
RL   J. Gen. Appl. Microbiol. 57:63-67(2011).
CC   -!- FUNCTION: Hydrolyzes ATP, and can also hydrolyze GTP with lower
CC       efficiency. Has lower affinity for GTP. {ECO:0000256|HAMAP-
CC       Rule:MF_03167}.
CC   -!- FUNCTION: Is probably involved in a pathway contributing to genomic
CC       integrity. {ECO:0000256|ARBA:ARBA00037565}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_03167}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03167}.
CC       Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004115}; Single-
CC       pass type I membrane protein {ECO:0000256|ARBA:ARBA00004115}.
CC   -!- SIMILARITY: Belongs to the IRC22 family.
CC       {ECO:0000256|ARBA:ARBA00038311}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase
CC       superfamily. OBG GTPase family. YchF/OLA1 subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_03167}.
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:GAA99216.1}.
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DR   EMBL; BABT02000220; GAA99216.1; -; Genomic_DNA.
DR   AlphaFoldDB; G7E997; -.
DR   STRING; 764103.G7E997; -.
DR   eggNOG; KOG1491; Eukaryota.
DR   HOGENOM; CLU_010949_0_0_1; -.
DR   InParanoid; G7E997; -.
DR   Proteomes; UP000009131; Unassembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR   GO; GO:0043023; F:ribosomal large subunit binding; IEA:UniProtKB-UniRule.
DR   CDD; cd04867; TGS_YchF_OLA1; 1.
DR   CDD; cd01900; YchF; 1.
DR   Gene3D; 3.10.20.30; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 1.10.150.300; TGS-like domain; 1.
DR   HAMAP; MF_00944; YchF_OLA1_ATPase; 1.
DR   InterPro; IPR004396; ATPase_YchF/OLA1.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
DR   InterPro; IPR031167; G_OBG.
DR   InterPro; IPR006073; GTP-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR007568; RTA1.
DR   InterPro; IPR012676; TGS-like.
DR   InterPro; IPR023192; TGS-like_dom_sf.
DR   InterPro; IPR005595; TRAP_alpha.
DR   InterPro; IPR013029; YchF_C.
DR   InterPro; IPR041706; YchF_N.
DR   NCBIfam; TIGR00092; redox-regulated ATPase YchF; 1.
DR   PANTHER; PTHR23305; OBG GTPASE FAMILY; 1.
DR   PANTHER; PTHR23305:SF11; OBG-LIKE ATPASE 1; 1.
DR   Pfam; PF01926; MMR_HSR1; 1.
DR   Pfam; PF04479; RTA1; 1.
DR   Pfam; PF03896; TRAP_alpha; 1.
DR   Pfam; PF06071; YchF-GTPase_C; 1.
DR   PRINTS; PR00326; GTP1OBG.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF81271; TGS-like; 1.
DR   PROSITE; PS51710; G_OBG; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_03167}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03167};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_03167};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_03167}; Reference proteome {ECO:0000313|Proteomes:UP000009131};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        89..109
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        116..133
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        153..178
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        198..221
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        233..255
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        267..287
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          668..935
FT                   /note="OBG-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51710"
FT   REGION          513..591
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          621..650
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         677..682
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03167"
FT   BINDING         883
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03167"
SQ   SEQUENCE   1041 AA;  113588 MW;  617D6A96ABDC5690 CRC64;
     MALANATAIG NAAGTILDSI LKANLGVTRA NVSFFPDLTG CTYRPGIPKD YILGAPIDHA
     GGGRCYPFHL NGSVAYEGVF AHYGYNPSMT SACVFLTLFM LLTVIHVGLT IASKRAWLSV
     IAIGGFVECI GWHGRLLSAF DNGFSAASKK SFLTSTVCLT IAPVFFSAAC YATLVLIVSQ
     LSQYGHATPR YSPRSMTIFF CLADFLSLVC QAIGGALTST AKTTSARDTG THIFLAGIVF
     QLVMMLVFLA LYLEFFYTYN RHVPRKVARL ALGVLLASVA IVIRGLYRTV ELSEGWTRGP
     MIHEPYFFVF DAAMMRGRSQ AGNAASSITE QAASMRLFGL LACAVLAQAS LFGSTPDLDV
     VASFGADNPF AKVYNGQANK ITLTMTSHSK GSDLLVQSVH GSFREMSGKE RVLRNTTKAV
     YKAALPSEQP VPIVYQFHSE FKPQDLNFQI YVTYIDGDKK TYVQKVPVGI VQITEPKGSW
     LDPQLLFLYL ILMSGAAGAA YFAYNKYVSS SRKRKGKKKS ADGKAKVPGA FGSAPSTPAK
     GGKPPAVDES WLPDHHRVSQ PKQRKGQTAT SDSEGQSDAG GKRKPRKGRC MLRRALNGPV
     KLRLSSHIVR SSVQSVSVAA PYAQRKPRAH RASFSNSARE LAKKRKMPPK KAAAAERKAL
     LGRPSNNLQI GIVGLPNVGK SSLFNVIAKC DLGKAANFPY ATIDPEEARV PVPDDRFDWL
     VQLYKPKSEI PAFLTCVDIA GLTAGASTGA GLGNAFLSHV RAVDGIFQVV RAFDDAEVIH
     VEGDVDPIRD MNVIQTELRL KDIEWVEKTL ESKRKTFRGT GTASLADKAK KEEIDIIAKI
     HKTLTEDNRD VRKPLVDWNN KEIDVINHLQ LLTAKPVIYL VNLSEKDYIR KKNKWLAKIK
     AWIDENNPGD LLIPFSVALE ERLVVMNPAE QAEEEKKIGT TSAVGKIMKA GYDGLHLIRY
     FTCGPDEVRA WTIRQGTRAP QAAGVIHGDF EKNFVCGEIM LFDDLKELGS EGAVKAAGKV
     MQKGKPYEMQ DANIAYWKAG A
//
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