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Database: UniProt
Entry: K9IKT0_DESRO
LinkDB: K9IKT0_DESRO
Original site: K9IKT0_DESRO 
ID   K9IKT0_DESRO            Unreviewed;       495 AA.
AC   K9IKT0;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Putative nucleoside phosphatase {ECO:0000313|EMBL:JAA47808.1};
OS   Desmodus rotundus (Vampire bat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Phyllostomidae;
OC   Desmodontinae; Desmodus.
OX   NCBI_TaxID=9430 {ECO:0000313|EMBL:JAA47808.1};
RN   [1] {ECO:0000313|EMBL:JAA47808.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Salivary gland {ECO:0000313|EMBL:JAA47808.1};
RA   Francischetti I.M.B., Assumpcao T.C.F., Ma D., Vicente E.C.,
RA   Ribeiro J.M.C.;
RT   "The Vampirome: Transcriptome and Proteome Analysis of the Submandibular
RT   and Accessory Glands of the Vampire Bat and Vector of Human Rabies,
RT   Desmodus rotundus.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family.
CC       {ECO:0000256|ARBA:ARBA00009283, ECO:0000256|RuleBase:RU003833}.
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DR   EMBL; GABZ01005717; JAA47808.1; -; mRNA.
DR   AlphaFoldDB; K9IKT0; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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:SF33; ECTONUCLEOSIDE TRIPHOSPHATE DIPHOSPHOHYDROLASE 2; 1.
DR   Pfam; PF01150; GDA1_CD39; 1.
DR   PROSITE; PS01238; GDA1_CD39_NTPASE; 1.
PE   2: Evidence at transcript level;
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   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        461..483
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   ACT_SITE        165
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600407-1"
FT   BINDING         204..208
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600407-2"
SQ   SEQUENCE   495 AA;  53488 MW;  C2935A8D02478C79 CRC64;
     MAGKVLSLLP PFLLAAAGLC GLLLLCVPTR DVREPPALKY GIVLDAGSSH TSMFIYKWPA
     DKENDTGIVG QHSSCDVRGG GISSYADNPS GAGQSLVECL DQALQDVPRE RHAGTPLYLG
     ATAGMRLLNL TSPEASAEVL TAVTRTLTQY PFDFRGARIL SGQDEGVFGW VTANYLLENF
     IKYGWAGRWY RPRKGTLGAM DLGGASTQIT FETASPAEDP ADEVQLRLYG QQYRVYTHSF
     LCYGRDQVLK RLLASVLQTH SAHPCWPRGY SRQVLLRDVY GSPCTAALRP QAFDSSSRVS
     LAGSSNPALC RGLVQGLFNF SACPFSRCSF NGIFQPPVAG DFLAFSAFFY TVDFLSSVMG
     LPVATLQQLE AAVVTVCNQT WSELQARAPG EVAHLPSYCA GAMFVQQLLS TGYGFDERAF
     SRVTFQKKAG DTAVGWALGY MLNLTNMIPA DPPGLRKGTD FNSWVVLLLL FAALLLAALV
     LLARQARSAK SPSAI
//
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