ID G3J412_CORMM Unreviewed; 670 AA.
AC G3J412;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE SubName: Full=Nucleoside diphosphatase (Ynd1), putative {ECO:0000313|EMBL:EGX95787.1};
GN ORFNames=CCM_00441 {ECO:0000313|EMBL:EGX95787.1};
OS Cordyceps militaris (strain CM01) (Caterpillar fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Cordyceps.
OX NCBI_TaxID=983644 {ECO:0000313|EMBL:EGX95787.1, ECO:0000313|Proteomes:UP000001610};
RN [1] {ECO:0000313|EMBL:EGX95787.1, ECO:0000313|Proteomes:UP000001610}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CM01 {ECO:0000313|EMBL:EGX95787.1,
RC ECO:0000313|Proteomes:UP000001610};
RX PubMed=22112802; DOI=10.1186/gb-2011-12-11-r116;
RA Zheng P., Xia Y., Xiao G., Xiong C., Hu X., Zhang S., Zheng H., Huang Y.,
RA Zhou Y., Wang S., Zhao G.P., Liu X., St Leger R.J., Wang C.;
RT "Genome sequence of the insect pathogenic fungus Cordyceps militaris, a
RT valued traditional Chinese medicine.";
RL Genome Biol. 12:RESEARCH116.1-RESEARCH116.21(2011).
CC -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family.
CC {ECO:0000256|ARBA:ARBA00009283, ECO:0000256|RuleBase:RU003833}.
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DR EMBL; JH126399; EGX95787.1; -; Genomic_DNA.
DR RefSeq; XP_006665664.1; XM_006665601.1.
DR AlphaFoldDB; G3J412; -.
DR STRING; 983644.G3J412; -.
DR GeneID; 18162476; -.
DR KEGG; cmt:CCM_00441; -.
DR VEuPathDB; FungiDB:CCM_00441; -.
DR eggNOG; KOG1386; Eukaryota.
DR HOGENOM; CLU_010246_3_0_1; -.
DR InParanoid; G3J412; -.
DR OMA; WHDALFD; -.
DR OrthoDB; 180318at2759; -.
DR Proteomes; UP000001610; Unassembled WGS sequence.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProt.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0017110; F:nucleoside diphosphate phosphatase activity; IEA:UniProt.
DR CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR Gene3D; 3.30.420.40; -; 1.
DR Gene3D; 3.30.420.150; Exopolyphosphatase. Domain 2; 1.
DR InterPro; IPR000407; GDA1_CD39_NTPase.
DR PANTHER; PTHR11782; ADENOSINE/GUANOSINE DIPHOSPHATASE; 1.
DR PANTHER; PTHR11782:SF121; NUCLEOSIDE-DIPHOSPHATASE MIG-23; 1.
DR Pfam; PF01150; GDA1_CD39; 1.
DR PROSITE; PS01238; GDA1_CD39_NTPASE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PIRSR:PIRSR600407-2};
KW Hydrolase {ECO:0000256|RuleBase:RU003833};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR600407-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000001610};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 515..532
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 482..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 584..613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 645..670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 149
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-1"
FT BINDING 186..190
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-2"
SQ SEQUENCE 670 AA; 73912 MW; 0F01230228D0CCFF CRC64;
MGNHKNSQYG VVLDAGSSGT RVYVYKWRNP SAPPKHKYDN DDDEVRSLPK IELKKNHKIH
PGISTFADAV DSVGHDHLQE LVDVAISKVP SHKIPETPIF LMATAGVRFL PEHKQKALLG
AVCSYFKTNT KFQLPDCDAH VQVIPGETEG LYGWIAANYL LGGFERPDEH KHSKGHHTYG
FLDMGGASAQ IAFAPNATET KKHADDLKLV RMRKLDGSSV EYKVFTSTWL GYGANKARER
FVEKLTDEYE TNVHEIPDPC LPKGLRTTLR GAVVESAASD EQQLLLGTGK FDECVRRTYP
LLGKEKPCED SPCLLNGQHA PAIDFDINHF VGVSEYWHTT HGVFGKEDVA YDLATYQKKV
LEYCARNWSA IKSDVVGRKK TAEEKMADAQ QACFKASWLI NMLHDGIGIP RIGIEGSVNG
SRSGADEKGF RDPFQPVDTI HDMEVSWTLG KMVLYATGQI PARDSKLPVG FGSNIASGVP
SDFEHAGSVP IPTGPKLGGS DDDDDDDVHR SSGSFIPFLT LLVLVLVVGY WLRKPERRHK
FLAFGRRSRK NGKGSRGIIN MLLGRSNGSY ERVLEEGDAA EFELGGIDSD ENDHSDSTEG
SKGGRSSGLG TPKLNLERFE DFRIPSAMDR TGLVVRTESR EHLGPSLQML NAGRRSRNVS
PTRMKSPLAV
//