ID A0A182N9D8_9DIPT Unreviewed; 1032 AA.
AC A0A182N9D8;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=adenosine deaminase {ECO:0000256|ARBA:ARBA00012784};
DE EC=3.5.4.4 {ECO:0000256|ARBA:ARBA00012784};
OS Anopheles dirus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7168 {ECO:0000313|EnsemblMetazoa:ADIR004263-PA, ECO:0000313|Proteomes:UP000075884};
RN [1] {ECO:0000313|Proteomes:UP000075884}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WRAIR2 {ECO:0000313|Proteomes:UP000075884};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Walton C., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles dirus WRAIR2.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:ADIR004263-PA}
RP IDENTIFICATION.
RC STRAIN=WRAIR2 {ECO:0000313|EnsemblMetazoa:ADIR004263-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine + H(+) + H2O = inosine + NH4(+);
CC Xref=Rhea:RHEA:24408, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16335, ChEBI:CHEBI:17596, ChEBI:CHEBI:28938; EC=3.5.4.4;
CC Evidence={ECO:0000256|ARBA:ARBA00001466};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Adenosine and AMP deaminases family. ADGF subfamily.
CC {ECO:0000256|ARBA:ARBA00006083}.
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DR AlphaFoldDB; A0A182N9D8; -.
DR STRING; 7168.A0A182N9D8; -.
DR EnsemblMetazoa; ADIR004263-RA; ADIR004263-PA; ADIR004263.
DR VEuPathDB; VectorBase:ADIR004263; -.
DR OrthoDB; 4403at2759; -.
DR Proteomes; UP000075884; Unassembled WGS sequence.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0046936; F:2'-deoxyadenosine deaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0004000; F:adenosine deaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006154; P:adenosine catabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 2.
DR InterPro; IPR001365; A_deaminase_dom.
DR InterPro; IPR013659; A_deaminase_N.
DR InterPro; IPR006331; ADGF.
DR InterPro; IPR006330; Ado/ade_deaminase.
DR InterPro; IPR032466; Metal_Hydrolase.
DR NCBIfam; TIGR01431; adm_rel; 2.
DR PANTHER; PTHR11409; ADENOSINE DEAMINASE; 1.
DR PANTHER; PTHR11409:SF39; ADENOSINE DEAMINASE 2; 1.
DR Pfam; PF00962; A_deaminase; 2.
DR Pfam; PF08451; A_deaminase_N; 2.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 2.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..1032
FT /note="adenosine deaminase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008129505"
FT DOMAIN 35..119
FT /note="Adenosine/AMP deaminase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08451"
FT DOMAIN 216..503
FT /note="Adenosine deaminase"
FT /evidence="ECO:0000259|Pfam:PF00962"
FT DOMAIN 542..622
FT /note="Adenosine/AMP deaminase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08451"
FT DOMAIN 721..1008
FT /note="Adenosine deaminase"
FT /evidence="ECO:0000259|Pfam:PF00962"
SQ SEQUENCE 1032 AA; 118543 MW; 2CBAD5E61ADE951D CRC64;
MAAMRPKLTC SSSTGTLLMC CLLVLLSTPE ANVIVERPSR PTPEDYWHQR ALLAASEAEL
ALGADIILST NESAVNSYLM GLKLAELSSG FSDPINFNPA RHFFEVLDQI KASPLFEFIR
EMPKGAVLHA HDTALASTEV ILNATYRPHL WQRGDFKSES GPEFKFSRTE PSTGDGWELV
AAIRRRMGAD KYDDEIRQLF TLYDADPLNA YRTINDVWNR FSRLFLALDP IVTYRPVWEY
YFREALREFR EDNVMYLEFR GLLPTLYDLD GNTYTPEDVV EIYRRVTEEF KAANPGFAGT
KFIYAPLRFA DNQTVDQYLS LAERLHIQYG DYVVGFDLVG QEDTGNPLQQ FVPQLLNMPA
SINFVFHAGE TNWHGMPSDE NLFDAIMLGT KRIGHGYALL KHPVLLEKVK QRKICVEVNP
VSNQVLKLVA DYRNHPASVL FTSDFPLVVS SDDPSFWRAA PLSHDFYMAF LGMASAHQDL
RLLKRLALNS LHYSLMSERE KEEANGMFLE SWNNFINAKV EQLTKERKPK RLLLQQFDPR
MARPAYDEFQ RQREEFFTRE QGRGLGADLV LSADEERLNR YVMHLKQQEL AKGVENPYEL
VSGRHFFEML ERINESTLFK LIQKMPKGGI LHAHDTAIGS TELIVRATYH DHLWQSGNIP
QAEGDPMPVY KFSRAKPTAD GEWRLVADIR SSMDNGAYDA ALRKMFTLYT KDPLNAHRDI
NDVWQKFMAM FICFEPMVTY RPVWEEYFYG CLEELLADNV TYLEFRGLLP PVYDLDDRTY
SPEDIVQMYV DQSDKFLRTH PKFMGVKFIY APLKFCDDAT FDGYLELVQK LKQRFPDFIA
GFDLVGQEDL GRPHTDFNER LLRLPPTINF FFHAGETNWI GRRDENLIDA ILLGTKRIGH
GFAALKHPVV LEEIKKRQVC IELNPISNQV LKLVQDFRNH AGTFYFSDNY PVVVSSDDPS
FWSAAPLSHD FFVAFMGLAS ARADLRLLKK LALNSIEFSS MDAAEKNVAT EKWTTAWNTF
LQEALQTVPA EF
//
