ID A0A2G8RS74_9APHY Unreviewed; 771 AA.
AC A0A2G8RS74;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Transporter {ECO:0008006|Google:ProtNLM};
GN ORFNames=GSI_14094 {ECO:0000313|EMBL:PIL24341.1};
OS Ganoderma sinense ZZ0214-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Ganoderma.
OX NCBI_TaxID=1077348 {ECO:0000313|EMBL:PIL24341.1, ECO:0000313|Proteomes:UP000230002};
RN [1] {ECO:0000313|EMBL:PIL24341.1, ECO:0000313|Proteomes:UP000230002}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZZ0214-1 {ECO:0000313|EMBL:PIL24341.1,
RC ECO:0000313|Proteomes:UP000230002};
RX PubMed=26046933; DOI=10.1038/srep11087;
RA Zhu Y., Xu J., Sun C., Zhou S., Xu H., Nelson D.R., Qian J., Song J.,
RA Luo H., Xiang L., Li Y., Xu Z., Ji A., Wang L., Lu S., Hayward A., Sun W.,
RA Li X., Schwartz D.C., Wang Y., Chen S.;
RT "Chromosome-level genome map provides insights into diverse defense
RT mechanisms in the medicinal fungus Ganoderma sinense.";
RL Sci. Rep. 5:11087-11087(2015).
CC -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family.
CC {ECO:0000256|ARBA:ARBA00009283, ECO:0000256|RuleBase:RU003833}.
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:PIL24341.1}.
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DR EMBL; AYKW01000067; PIL24341.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G8RS74; -.
DR STRING; 1077348.A0A2G8RS74; -.
DR OrthoDB; 180318at2759; -.
DR Proteomes; UP000230002; 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 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:UP000230002};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 565..588
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 649..771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..701
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 719..761
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 164
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-1"
FT BINDING 196..200
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-2"
SQ SEQUENCE 771 AA; 84791 MW; 2ED7F81ED080692B CRC64;
MPPPTSVDSW LSSRRFGIVI DAGSSGSRLQ IYSWKDARTV RQEHGADALR SLPEVGKGTE
NGEEWSIKSE PGLSYFADNV QGIPTYLAPL LEHARTHIPP SLQPETPLFL LATAGMRLLT
PEKQAHVLSA TCEFLRFHSN FKIDDPSSNG PCGSSVRIIT GEEEGLFGWI AVNYLMDGFK
GSDDTRLTYG FLDMGGASTQ IAFEPSKQEQ ERAKNLLDVR LRLLDGHDIN HKVFVTTWLG
YGTNQARERY VGRLINDYEA NRTLSTEPEH INDPCLPKDL ILLNTPVQPE TASDHAKSTH
KFVGTGSWEQ CLQRTLPLLN KDAPCPDSHC LFNGVSVPAI DFTASHFIGV SEYWYSTEQS
FGLGGAYDFV QYERAASEFC AQDWTRVLEG HEDKRKQGHE HLGGDGEVEE DGVIVDTGRW
GLDVEIPRLQ MQCFKAAWLV NVLHEGIRMP RIVDAGGNVT AATAGGEKVT AQAQTKGLGR
PSFQSMDAVG DIAITWTLGK MVLEASKEVP PVSRQAKPIV DPLDDIPDIS TSPVQPIRPP
FLDFDAFEDS ISQHLPPSLT RHQLGFSPVA FVFYLFICAL FTSSLYRLRH RIRSTVRRFV
NKRERSYIAE GYMMEEGLSL TGGTLPPSRS APGPRLSFNN IVRPIQRLAS NGLRQSRPSP
LTISRESSTT SEQHSPARVS PMRSLSFPGI QTVSNIGPHD EPNGTATAYG PAPSSPRLPD
GSFVSNGSVS SLQSRSRNSS HINLSSLAPR QAISRTFSGG NHAPSAPYRD E
//