ID A0A061H3W6_9BASI Unreviewed; 483 AA.
AC A0A061H3W6;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=GPN-loop GTPase 2 {ECO:0008006|Google:ProtNLM};
GN ORFNames=PFL1_05050 {ECO:0000313|EMBL:EPQ27512.1};
OS Pseudozyma flocculosa PF-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Pseudozyma.
OX NCBI_TaxID=1277687 {ECO:0000313|EMBL:EPQ27512.1, ECO:0000313|Proteomes:UP000053664};
RN [1] {ECO:0000313|EMBL:EPQ27512.1, ECO:0000313|Proteomes:UP000053664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PF-1 {ECO:0000313|EMBL:EPQ27512.1,
RC ECO:0000313|Proteomes:UP000053664};
RX PubMed=23800965; DOI=10.1105/tpc.113.113969;
RA Lefebvre F., Joly D.L., Labbe C., Teichmann B., Linning R., Belzile F.,
RA Bakkeren G., Belanger R.R.;
RT "The transition from a phytopathogenic smut ancestor to an anamorphic
RT biocontrol agent deciphered by comparative whole-genome analysis.";
RL Plant Cell 25:1946-1959(2013).
CC -!- SIMILARITY: Belongs to the GPN-loop GTPase family.
CC {ECO:0000256|ARBA:ARBA00005290}.
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DR EMBL; KE361639; EPQ27512.1; -; Genomic_DNA.
DR RefSeq; XP_007880770.1; XM_007882579.1.
DR AlphaFoldDB; A0A061H3W6; -.
DR GeneID; 19319149; -.
DR KEGG; pfp:PFL1_05050; -.
DR eggNOG; KOG1533; Eukaryota.
DR HOGENOM; CLU_037460_0_1_1; -.
DR OrthoDB; 168004at2759; -.
DR Proteomes; UP000053664; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR CDD; cd17871; GPN2; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR004130; Gpn.
DR InterPro; IPR030231; Gpn2.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR21231:SF3; GPN-LOOP GTPASE 2; 1.
DR PANTHER; PTHR21231; XPA-BINDING PROTEIN 1-RELATED; 1.
DR Pfam; PF03029; ATP_bind_1; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000053664}.
FT REGION 104..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 225..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 283..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 364..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 483 AA; 53584 MW; 7A28A7743FC50230 CRC64;
MPFAQLVIGS PGSGKSTYCN GLSHFLPLLS RPCSIINLDP ANDSLPYPCA IDINHLISVR
DVMAELHLGP NAAMLYCIEY LETNLDWLID RLGDVMSHQR QGRLVHTEPT SHDTATTTTT
TTTTTTHTTI DPVPAGSEYL VFDLPGQVEL STNHPSLRRI LGVLEKQLQL RFVAVHMTDA
THITDPSRYV SLLLLALRAM LALELPHVNV LSKVDLLGQH SRSIGGLDPV ARRPGQEGDD
DDGSDAGTTG MQGGLSGDLA FNLDFYTQVQ DLSYLYDLLL RPSSSGSRRR RGPSSDDNDD
DDDEEEEPPL RRDARFAELN RTICELVEDF GLVQFETLAV EDRRSMFRLL QVLDKAVGYV
YVGQGEEPFP DDDDDDGGEG DEERGGRYES GSAAATAGLA LWKQGASARA LFSTADRGDP
LGWGDALEVQ ERYVDHRHLY DAHERKRDDE ARDKLWERRV WDEVNKVSRQ SSSSHDNKGQ
QPQ
//
