ID S7NR03_MYOBR Unreviewed; 714 AA.
AC S7NR03;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Ectonucleoside triphosphate diphosphohydrolase 7 {ECO:0000313|EMBL:EPQ19686.1};
GN ORFNames=D623_10025678 {ECO:0000313|EMBL:EPQ19686.1};
OS Myotis brandtii (Brandt's bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=109478 {ECO:0000313|EMBL:EPQ19686.1, ECO:0000313|Proteomes:UP000052978};
RN [1] {ECO:0000313|Proteomes:UP000052978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23962925; DOI=10.1038/ncomms3212;
RA Seim I., Fang X., Xiong Z., Lobanov A.V., Huang Z., Ma S., Feng Y.,
RA Turanov A.A., Zhu Y., Lenz T.L., Gerashchenko M.V., Fan D., Hee Yim S.,
RA Yao X., Jordan D., Xiong Y., Ma Y., Lyapunov A.N., Chen G., Kulakova O.I.,
RA Sun Y., Lee S.G., Bronson R.T., Moskalev A.A., Sunyaev S.R., Zhang G.,
RA Krogh A., Wang J., Gladyshev V.N.;
RT "Genome analysis reveals insights into physiology and longevity of the
RT Brandt's bat Myotis brandtii.";
RL Nat. Commun. 4:2212-2212(2013).
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; KE164716; EPQ19686.1; -; Genomic_DNA.
DR AlphaFoldDB; S7NR03; -.
DR eggNOG; KOG1386; Eukaryota.
DR Proteomes; UP000052978; Unassembled WGS sequence.
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 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:SF37; ECTONUCLEOSIDE TRIPHOSPHATE DIPHOSPHOHYDROLASE 7; 1.
DR Pfam; PF01150; GDA1_CD39; 2.
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, ECO:0000313|EMBL:EPQ19686.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR600407-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000052978};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 87..105
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 662..680
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT ACT_SITE 327
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-1"
FT BINDING 371..375
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-2"
SQ SEQUENCE 714 AA; 80641 MW; 51A05761688995AC CRC64;
MNYGSQSPRE PPTQRGRSVL GAAAEKAAGG DLPLLRRRSE PGVRAAGLGD AWDKETTFSG
QKEKEVTGVG TTEGNPWLVS PFPRQRVAFL GLFFISCLLL LMLIMDFRHW GASLPRDRQY
ERYLARVGEL EATDTEDPNL NYGLVVDCGS SGSRIFVYFW PRHNGNPHDL LDIKQMRDRN
SQPVVKKIKP GISAMADTPE HASDYLRPLL SFAAAHVPVK KHKETPLYIL CTAGMRLLPE
REEYRSAVAN LADLTDHQWP ADHRLATAGL DNTVVPHHKS VNSLIYVSPR RSRKQLAILA
DLVKDLPLEF DFLFSRSQAE VISGKQEGVY AWIGINFVLG RFDHVDESDA EAPQELAAGR
RRTVGILDMG GASLQIAYEV PTSTSVLPPK QEEAAKILLA EFNLGCDVHH TEHVYRVYVT
TFLGFGGNFA RQRYEDLVLN ETLHKNRLLG QKTGLSPDSP FLDPCLPVGL TDVVERNSQV
LHVRGKGDWS TCGAMLSPLL ALSNTSQASL NGIYQSPIDF NNSEFYGFSE FFYCTEDVLR
IGGRYHGPTF AKAAQDYCGM AWSVLTQRFK NGLYSSHADE HRLKYQCFKS AWMYQVLHEG
FHFPYDYPNL RTAQLVYDRE VQWTLGAILY KTRFLPLRDL RQEGVRQAHS SWFRLSFVYN
HYLFFACILV VLLAIILYLL RLRRIHHRQT RASAPLNLLW IEEVVPMIGV QVGP
//
