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Database: UniProt
Entry: F2TH60_AJEDA
LinkDB: F2TH60_AJEDA
Original site: F2TH60_AJEDA 
ID   F2TH60_AJEDA            Unreviewed;       391 AA.
AC   F2TH60;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 2.
DT   27-MAR-2024, entry version 39.
DE   SubName: Full=CobW domain-containing protein {ECO:0000313|EMBL:EGE82573.2};
GN   ORFNames=BDDG_05517 {ECO:0000313|EMBL:EGE82573.2};
OS   Ajellomyces dermatitidis (strain ATCC 18188 / CBS 674.68) (Blastomyces
OS   dermatitidis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX   NCBI_TaxID=653446 {ECO:0000313|EMBL:EGE82573.2};
RN   [1] {ECO:0000313|EMBL:EGE82573.2}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18188 {ECO:0000313|EMBL:EGE82573.2};
RG   The Broad Institute Genome Sequencing Platform;
RG   Broad Institute Genome Sequencing Center for Infectious Disease.;
RA   Cuomo C., Klein B., Sullivan T., Heitman J., Young S., Zeng Q., Gargeya S.,
RA   Alvarado L., Berlin A.M., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA   Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA   Birren B.;
RT   "Annotation of Blastomyces dermatitidis strain ATCC 18188.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC         Evidence={ECO:0000256|ARBA:ARBA00001702};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC         Evidence={ECO:0000256|ARBA:ARBA00001702};
CC   -!- SIMILARITY: Belongs to the SIMIBI class G3E GTPase family. ZNG1
CC       subfamily. {ECO:0000256|ARBA:ARBA00034320}.
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DR   EMBL; GG749435; EGE82573.2; -; Genomic_DNA.
DR   AlphaFoldDB; F2TH60; -.
DR   HOGENOM; CLU_017452_0_1_1; -.
DR   Proteomes; UP000007802; Unassembled WGS sequence.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   CDD; cd03112; CobW-like; 1.
DR   Gene3D; 3.30.1220.10; CobW-like, C-terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR036627; CobW-likC_sf.
DR   InterPro; IPR011629; CobW-like_C.
DR   InterPro; IPR003495; CobW/HypB/UreG_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR13748:SF31; COBW DOMAIN-CONTAINING PROTEIN 1-RELATED; 1.
DR   PANTHER; PTHR13748; COBW-RELATED; 1.
DR   Pfam; PF02492; cobW; 1.
DR   Pfam; PF07683; CobW_C; 1.
DR   SUPFAM; SSF90002; Hypothetical protein YjiA, C-terminal domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT   DOMAIN          38..233
FT                   /note="CobW/HypB/UreG nucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02492"
FT   DOMAIN          320..385
FT                   /note="CobW C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF07683"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   391 AA;  42753 MW;  321434D2FF6AD558 CRC64;
     MNFRDGDEEG PPELVDVDAL EEETAAKSPT ERKFKKVPIT IVTGYLGAGK TTLLNYILGE
     EHGKKIAVIL NEFGDSIDIE KSLTVNKDGQ QVEEWLELAN GCICCSVRDT GVVAIESLME
     RQGTFDYILL ETTGLADPGN IAPLFWVDDG IGSTIYLDGI VTLVDGKNIL RLLDEPAPAE
     VQGTHHGAVL TTAHLQISHA DVIILNKSDL LTAAELDKVK ERVISINGLA KIIVTDHSKV
     PNLDGTVLEL HAYDNVTDVD FSEKGHSHLD PSISTLSFTI DKITPECVPK VDAWLRSLLW
     ERQLPHPQPT NQGQQKIEDF EIHRLKGLLC LTDGSTQVIQ GVQEVFDITE TDSRHPSASG
     NHCKMVLIGR GLGMDSSPWR ESLQASLGRA S
//
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