ID E3KEE8_PUCGT Unreviewed; 833 AA.
AC E3KEE8;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE RecName: Full=Golgi apyrase {ECO:0008006|Google:ProtNLM};
GN ORFNames=PGTG_08877 {ECO:0000313|EMBL:EFP82681.1};
OS Puccinia graminis f. sp. tritici (strain CRL 75-36-700-3 / race SCCL)
OS (Black stem rust fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=418459 {ECO:0000313|EMBL:EFP82681.1, ECO:0000313|Proteomes:UP000008783};
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CRL 75-36-700-3;
RG The Broad Institute Genome Sequencing Platform;
RA Birren B., Lander E., Galagan J., Nusbaum C., Devon K., Cuomo C., Jaffe D.,
RA Butler J., Alvarez P., Gnerre S., Grabherr M., Mauceli E., Brockman W.,
RA Young S., LaButti K., Sykes S., DeCaprio D., Crawford M., Koehrsen M.,
RA Engels R., Montgomery P., Pearson M., Howarth C., Larson L., White J.,
RA Zeng Q., Kodira C., Yandava C., Alvarado L., O'Leary S., Szabo L., Dean R.,
RA Schein J.;
RT "The Genome Sequence of Puccinia graminis f. sp. tritici Strain CRL 75-36-
RT 700-3.";
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000008783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CRL 75-36-700-3 / race SCCL
RC {ECO:0000313|Proteomes:UP000008783};
RX PubMed=21536894; DOI=10.1073/pnas.1019315108;
RA Duplessis S., Cuomo C.A., Lin Y.-C., Aerts A., Tisserant E.,
RA Veneault-Fourrey C., Joly D.L., Hacquard S., Amselem J., Cantarel B.L.,
RA Chiu R., Coutinho P.M., Feau N., Field M., Frey P., Gelhaye E.,
RA Goldberg J., Grabherr M.G., Kodira C.D., Kohler A., Kuees U.,
RA Lindquist E.A., Lucas S.M., Mago R., Mauceli E., Morin E., Murat C.,
RA Pangilinan J.L., Park R., Pearson M., Quesneville H., Rouhier N.,
RA Sakthikumar S., Salamov A.A., Schmutz J., Selles B., Shapiro H.,
RA Tanguay P., Tuskan G.A., Henrissat B., Van de Peer Y., Rouze P.,
RA Ellis J.G., Dodds P.N., Schein J.E., Zhong S., Hamelin R.C.,
RA Grigoriev I.V., Szabo L.J., Martin F.;
RT "Obligate biotrophy features unraveled by the genomic analysis of rust
RT fungi.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:9166-9171(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; DS178283; EFP82681.1; -; Genomic_DNA.
DR RefSeq; XP_003327100.1; XM_003327052.2.
DR AlphaFoldDB; E3KEE8; -.
DR STRING; 418459.E3KEE8; -.
DR EnsemblFungi; EFP82681; EFP82681; PGTG_08877.
DR GeneID; 10530064; -.
DR KEGG; pgr:PGTG_08877; -.
DR VEuPathDB; FungiDB:PGTG_08877; -.
DR eggNOG; KOG1386; Eukaryota.
DR HOGENOM; CLU_017667_0_0_1; -.
DR InParanoid; E3KEE8; -.
DR OMA; WEEIIEN; -.
DR OrthoDB; 180318at2759; -.
DR Proteomes; UP000008783; Unassembled WGS sequence.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004382; F:GDP phosphatase activity; IBA:GO_Central.
DR GO; GO:0045134; F:UDP phosphatase activity; IBA:GO_Central.
DR GO; GO:0006256; P:UDP catabolic process; IBA:GO_Central.
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 Nucleotide-binding {ECO:0000256|PIRSR:PIRSR600407-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000008783}.
FT REGION 576..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 634..740
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 776..833
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..592
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..615
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..652
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..740
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 819..833
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 171
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-1"
FT BINDING 209..213
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-2"
SQ SEQUENCE 833 AA; 92070 MW; 9096309013BD7C4B CRC64;
MEEPQTTTAR TTTRTITHSD WLNDRQFGIV LDAGSSGTRI QVYSWKSPRA QLNHRLTSHQ
STKVLPRIET GVQDGNDWQL KVEPGISSFG SHPHHLGQYL KPLLDHALKL IPANQIATTP
FYLLATAGMR LLPQLQQDGI LEEVCSYIKT HYRFRINQCS QHIQIISGEE EGTFGWVAVN
YLMDGFDRPG HPSTGSQASS TFGFLDMGGA STQIAFEPNE LAKIEHADNL TKLTLKLLDG
TDISHSVFVT TWLGYGTNKA RERYAQKLLE QFSSDHQIRK PNQLDQLGII PDPCLPASLL
LPSPSSSYQF NGTGDFKKCI QNVSPLLNKN APCLDEPCLF DGKHVPPIDF SVNRFIGISE
YWYSTQDLWS MGGIYDFVEF EKKAISYCQL NWEEIIESHK SGTKWPSNVE ISRLETQCFK
AAWIINILHE GIGIPRIIDK GGQGDRMDYN QEGIQKAAQK GLLNPPPPNF QSLNEVGNIT
VSWTLGKMVL EISQQLSSSP QSTSSIGRLP GIHTSQLGGG LKAQLSHAKS WIEPMAILGM
TLGALVIWFL YSCSKTLCQF QKERRLGGQG YVLASMEEGD GGRRDSNHTR PSTPRVLRKP
SLSSPRSFFH SAGTGPSGLI QQTVSRALGV WTNRSSNTPV HRSLSASHPS SPRAGRPSRL
GSPNQPKFSI SGGYSEGADD EDQRMLIPPV SITTSLSAPA GGTGYQSTTS SRTSVDEGLF
NTVPISRTGS SSGTKRFNDE WTTPATHHQL SQDGSVIHAD HLFPLERPKF RFSHSKSFQS
LSSPSDHQLD DHLDYRPPSS HDRSLSSAPH EPLHSHQHRT INSHSCSNLT DYS
//
