ID A1CB50_ASPCL Unreviewed; 717 AA.
AC A1CB50;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 24-JAN-2024, entry version 78.
DE SubName: Full=Nucleoside diphosphatase (Ynd1), putative {ECO:0000313|EMBL:EAW12968.1};
GN ORFNames=ACLA_014050 {ECO:0000313|EMBL:EAW12968.1};
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612 {ECO:0000313|EMBL:EAW12968.1, ECO:0000313|Proteomes:UP000006701};
RN [1] {ECO:0000313|EMBL:EAW12968.1, ECO:0000313|Proteomes:UP000006701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1
RC {ECO:0000313|Proteomes:UP000006701};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
CC -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family.
CC {ECO:0000256|ARBA:ARBA00009283}.
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DR EMBL; DS027049; EAW12968.1; -; Genomic_DNA.
DR RefSeq; XP_001274394.1; XM_001274393.1.
DR AlphaFoldDB; A1CB50; -.
DR STRING; 344612.A1CB50; -.
DR EnsemblFungi; EAW12968; EAW12968; ACLA_014050.
DR GeneID; 4706091; -.
DR KEGG; act:ACLA_014050; -.
DR VEuPathDB; FungiDB:ACLA_014050; -.
DR eggNOG; KOG1386; Eukaryota.
DR HOGENOM; CLU_010246_3_0_1; -.
DR OMA; WHDALFD; -.
DR OrthoDB; 180318at2759; -.
DR Proteomes; UP000006701; 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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PIRSR:PIRSR600407-2};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR600407-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000006701};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 525..544
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 612..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 680..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..638
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 694..710
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 152
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-1"
FT BINDING 189..193
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-2"
SQ SEQUENCE 717 AA; 79639 MW; B6985ECE4F0DB7DD CRC64;
MYSTLSLDSR RHYGVVLDAG SSGTRVHVYR WLDHTVARKQ ADTDELKTLP ELKTKPEWTK
KIHPGVSSFA ERPEAIGPDH LAELLDHARK IVPASEIKDT PIFLLATAGM RLLPNLEREL
LLNQICTYAN ENYDFLLPDC GVHIQVIPGV TEALYGWIAT NYLLGSFDEP KGHDHGKGHH
TYGFLDMGGA SAQIAFAPNI TETEKHADDL TLLRLRNVDG STQEHRVFVT SWLEYGVHEA
RRRYLEALQT ALGSAKELPD PCLPQGLRTT IDGKPMPSDG KVELSLLGTG RFDECLRQTY
PLLDKDAPCA DQPCLLHGVH VPAIDFDVNH FIGISEYWHT THEILEMGHK DKAYDFNTYQ
QRVQQFCSQD WEAIEKGVEK HKWGKKVDQQ SAYEVCFKAS WIINMLHDGI GIPRVGLEDT
TGSGHNGTKE VLSHGKNKGF LDPFQAVHKI DSTEVSWTLG KMVLYASSQV PTESEEVLPV
GFGSNVAGVP NDFQYPSVEL FPNTETLHGS NWQDALFDGS SPRRAPGFVL FLLIVAMAAF
FLCGRSRRSR MFHKFNTLFK RGGPSRANYP KRRGFFGGKL PFFGRRSPSY ERVLEDGARE
YDLGASHFGR ASLDRRHSSE TDSSSFMPPK RTSSWSGPAT PSFKFSLDNS STATIGLGIS
ADSGVNAIDR AGLVVRTESR DHLAPVALGP TTNGRRSRAG SPTRSHRTPI TSPLAED
//
