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Database: UniProt
Entry: V5EMP8_KALBG
LinkDB: V5EMP8_KALBG
Original site: V5EMP8_KALBG 
ID   V5EMP8_KALBG            Unreviewed;       969 AA.
AC   V5EMP8;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=Nucleoside phosphatase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PSEUBRA_SCAF3g03902 {ECO:0000313|EMBL:EST06400.1};
OS   Kalmanozyma brasiliensis (strain GHG001) (Yeast) (Pseudozyma brasiliensis).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Kalmanozyma.
OX   NCBI_TaxID=1365824 {ECO:0000313|EMBL:EST06400.1, ECO:0000313|Proteomes:UP000019377};
RN   [1] {ECO:0000313|Proteomes:UP000019377}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GHG001 {ECO:0000313|Proteomes:UP000019377};
RX   PubMed=24356824; DOI=10.1128/genomea.00920-13;
RA   Oliveira J.V.D.C., dos Santos R.A.C., Borges T.A., Riano-Pachon D.M.,
RA   Goldman G.H.;
RT   "Draft genome sequence of Pseudozyma brasiliensis sp. nov. strain GHG001, a
RT   high producer of endo-1,4-xylanase isolated from an insect pest of
RT   sugarcane.";
RL   Genome Announc. 1:E0092013-E0092013(2013).
CC   -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family.
CC       {ECO:0000256|ARBA:ARBA00009283}.
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DR   EMBL; KI545873; EST06400.1; -; Genomic_DNA.
DR   RefSeq; XP_016291389.1; XM_016437839.1.
DR   AlphaFoldDB; V5EMP8; -.
DR   STRING; 1365824.V5EMP8; -.
DR   GeneID; 27420517; -.
DR   eggNOG; KOG1386; Eukaryota.
DR   HOGENOM; CLU_304867_0_0_1; -.
DR   OMA; IPRIVDH; -.
DR   OrthoDB; 180318at2759; -.
DR   Proteomes; UP000019377; 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.
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:UP000019377};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        627..646
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          1..81
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          726..754
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          780..861
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          935..969
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..51
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        728..746
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        823..861
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        939..955
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        249
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600407-1"
FT   BINDING         293..297
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600407-2"
SQ   SEQUENCE   969 AA;  103635 MW;  FF76E55200D15C48 CRC64;
     MSYSIQGSSS QPYGAYTFNT PVKRRQRAQV LQTSQQQQRR SSQSNHPSRR ENIADAYTWN
     AAAKTNKPKP GSKLNESPLK DAVPGAAQLD APASWLEGRK YAVLIDAGSS GSRMQVYSWK
     DPKLERALRA SKGLDAKVLP KVEKGTWENS GVDWSHKVEP GLSSFGDRPA EVGNYLKGLL
     DHAEKIVPPS AWADTPIYVM ATAGMRLLPD QQRTSVLFET CRYIREHTRF SLDGGGCEEH
     VQVISGEEEG LLGWISVNYL MDGFHIRGKK ASLDGETDIM EGKSTFGFLD MGGASTQIAF
     EPSKKALQGD GAAAEADLTT VPLRMLDGTE VSHKVFVTTF LGYGTNKARD RYIDLLQSGA
     VKAHETSHTL SDPCLPNGLQ LANVNVGGKT DLSLMGAGNF TACLESMHPL LDKEAVCDKP
     PCLFHGVHVP KIDFSVNHFI GVSEYWFSSH DVFGLGGVYD FVDFQKAAEG FCEKPWADLK
     KHLDAGDLFG PEVQLSRLQT QCFKAAWMVT VLHEGIGIPR IVDHKGAGDG TDHADQANDK
     GEQKNLFQSV NDINGFSVSW TLGKAVLEAS RDIPPAPGSL PSPFDELSKT NPKLGKWDPF
     RPKWPTTGEG SAFPPALGET ARHVSPISLI IMVAAFLILL LTCVCTRGRG PRASRRRAAM
     KDMLPPPLGT LGGFCSSKRT SRGDYVLANM EEAAGDASKS GFWSKLGKRA EFKSYSPTME
     AEFGFNAEGS SEESSSGSSG SAGRGGSRTA SRKRANAGVV GALGWPARRL AFALTSTFPS
     LSSRRKPRSK KRDSSLPISR DGAGSDGGLG HSARIASRRG ATTPTMVRIS RPASPTFTGM
     TTGAAISRPA SRTSSRAPTP VLGHRLTSAT LSTRSGAITP GGSVMASSVG PAGILSPSGP
     SSPLGERHAR PGLFSASLSR VHSITDMTTI ESGLLVAPAT RTPSRQGSPS ASGLSPMSEL
     RREDGEIDV
//
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