ID   A0A1J1IJF8_9DIPT        Unreviewed;       945 AA.
AC   A0A1J1IJF8;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=deoxyribose-phosphate aldolase {ECO:0000256|ARBA:ARBA00012515};
DE            EC=4.1.2.4 {ECO:0000256|ARBA:ARBA00012515};
DE   AltName: Full=2-deoxy-D-ribose 5-phosphate aldolase {ECO:0000256|ARBA:ARBA00032755};
GN   Name=putative Putative ATPase N2B {ECO:0000313|EMBL:CRK99898.1};
GN   ORFNames=CLUMA_CG013201 {ECO:0000313|EMBL:CRK99898.1};
OS   Clunio marinus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Chironomoidea; Chironomidae;
OC   Clunio.
OX   NCBI_TaxID=568069 {ECO:0000313|EMBL:CRK99898.1, ECO:0000313|Proteomes:UP000183832};
RN   [1] {ECO:0000313|EMBL:CRK99898.1, ECO:0000313|Proteomes:UP000183832}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Syromyatnikov M.Y., Popov V.N.;
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-deoxy-D-ribose 5-phosphate = acetaldehyde + D-glyceraldehyde
CC         3-phosphate; Xref=Rhea:RHEA:12821, ChEBI:CHEBI:15343,
CC         ChEBI:CHEBI:59776, ChEBI:CHEBI:62877; EC=4.1.2.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00000764};
CC   -!- SIMILARITY: Belongs to the AFG1 ATPase family.
CC       {ECO:0000256|ARBA:ARBA00010322}.
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DR   EMBL; CVRI01000054; CRK99898.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J1IJF8; -.
DR   STRING; 568069.A0A1J1IJF8; -.
DR   OrthoDB; 1617at2759; -.
DR   UniPathway; UPA00002; UER00468.
DR   Proteomes; UP000183832; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0004139; F:deoxyribose-phosphate aldolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042302; F:structural constituent of cuticle; IEA:UniProtKB-UniRule.
DR   GO; GO:0009264; P:deoxyribonucleotide catabolic process; IEA:InterPro.
DR   GO; GO:0046386; P:deoxyribose phosphate catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00959; DeoC; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR005654; ATPase_AFG1-like.
DR   InterPro; IPR031311; CHIT_BIND_RR_consensus.
DR   InterPro; IPR011343; DeoC.
DR   InterPro; IPR002915; DeoC/FbaB/LacD_aldolase.
DR   InterPro; IPR000618; Insect_cuticle.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; NF040713; ZapE; 1.
DR   PANTHER; PTHR12169:SF6; AFG1-LIKE ATPASE; 1.
DR   PANTHER; PTHR12169; ATPASE N2B; 1.
DR   Pfam; PF03969; AFG1_ATPase; 1.
DR   Pfam; PF00379; Chitin_bind_4; 1.
DR   Pfam; PF01791; DeoC; 1.
DR   SMART; SM01133; DeoC; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00233; CHIT_BIND_RR_1; 1.
DR   PROSITE; PS51155; CHIT_BIND_RR_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cuticle {ECO:0000256|ARBA:ARBA00022460, ECO:0000256|PROSITE-
KW   ProRule:PRU00497}; Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000183832};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..945
FT                   /note="deoxyribose-phosphate aldolase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012385062"
FT   REGION          24..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        38..54
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   945 AA;  107717 MW;  70F523C8C4BF5099 CRC64;
     MKVIIFMLAL VLAVSARPQE YEDYEQQTAR PAARNLPHQG YHQQQKSGDR ETSTWIPIIQ
     YDKQQGTDGS YQTHYETGNN ILAEESGYLK DINEDNPAGT LVQKGSYSYE TPEGQIINVE
     YQADEKGFRV HGDHLPTPPP VSPEIQKGLD LIYEGIKLQE ERRRNNPNYA ADKAERDRLN
     YLGLYMINSF RYLRCIPNIR SSFYLSFNQS KNFATEHQDG PLKVLKKKIA NNELMPDEHQ
     MKVVEDLQYL YEETKDYEPL SSGIVSWFAL NKKNITSDIK GLYIYGSVGG GKTMLMDMFF
     DCCKIEKKKR VHFNSFMTDV HKEIHKIKQL QVRDTTSTKP QPFDPIEPVA ELIKEDAYLI
     CFDEFQVTDI ADAMILKRLF TSLFDKGVIV VATSNRKPDD LYKSGLQRSN FLPFIPILKN
     HCDVRALESG IDYRSTNKGE GEHYFLTSDP DSESKVKAIF KVLCSQENDI VRPKTFTHFG
     RNITFEKTCG QVLFTTFNEL CDRALGASDY LQLAQYFHTI IIRDVPQLNL KLKSQTRRFI
     TLIDSLYDRR IRIVIVSEVP LNYLFSNVVP DGMELSDEHR SLMDDLKLSK DSADLSANIF
     TGEEELFAFE RFLHFAPHVC FSSIRKMNKY LVNQPVPFDE TWFKDVNINL RGLEAKIKTL
     SQYKVSDTEN RIAWALKAMT LTDLTTLAGD DCKSNVERLC IRACYPLGMH SMNINERDEF
     LKQLHVAAVC VYPTKVKDAF DTLSSLHKIG DIHIAAVATG FPTGLYPLET RLKEITFAIE
     NGATEIDIVI DRSLVLTNQW RKLYDEVVEM RKACGTAAHM KTILGIGECG TMTNVYIASM
     ICMMAGADFI KTSTGKETVN ANLPVGLCMI RAIQEFKRRT GENIGLKPAG GVRTVNDAID
     WLILIKMTLG DEYLCPHLFR FGASGLLDDI EKFLVKELVN KKVIE
//