ID K9Z126_CYAAP Unreviewed; 2350 AA.
AC K9Z126;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=5'-nucleotidase {ECO:0000313|EMBL:AFZ52437.1};
DE EC=3.1.3.5 {ECO:0000313|EMBL:AFZ52437.1};
GN OrderedLocusNames=Cyan10605_0289 {ECO:0000313|EMBL:AFZ52437.1};
OS Cyanobacterium aponinum (strain PCC 10605).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Geminocystaceae; Cyanobacterium.
OX NCBI_TaxID=755178 {ECO:0000313|EMBL:AFZ52437.1, ECO:0000313|Proteomes:UP000010480};
RN [1] {ECO:0000313|Proteomes:UP000010480}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 10605 {ECO:0000313|Proteomes:UP000010480};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
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DR EMBL; CP003947; AFZ52437.1; -; Genomic_DNA.
DR RefSeq; WP_015218169.1; NC_019776.1.
DR STRING; 755178.Cyan10605_0289; -.
DR KEGG; can:Cyan10605_0289; -.
DR PATRIC; fig|755178.3.peg.299; -.
DR eggNOG; COG0737; Bacteria.
DR eggNOG; COG3211; Bacteria.
DR eggNOG; COG3391; Bacteria.
DR eggNOG; COG4222; Bacteria.
DR HOGENOM; CLU_000765_0_0_3; -.
DR Proteomes; UP000010480; Chromosome.
DR GO; GO:0106411; F:XMP 5'-nucleosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0009166; P:nucleotide catabolic process; IEA:InterPro.
DR Gene3D; 3.60.21.10; -; 1.
DR Gene3D; 3.90.780.10; 5'-Nucleotidase, C-terminal domain; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR008334; 5'-Nucleotdase_C.
DR InterPro; IPR036907; 5'-Nucleotdase_C_sf.
DR InterPro; IPR006179; 5_nucleotidase/apyrase.
DR InterPro; IPR010895; CHRD.
DR InterPro; IPR011048; Haem_d1_sf.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR008557; PhoX.
DR InterPro; IPR027372; Phytase-like_dom.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR46928; MESENCHYME-SPECIFIC CELL SURFACE GLYCOPROTEIN; 1.
DR PANTHER; PTHR46928:SF1; MESENCHYME-SPECIFIC CELL SURFACE GLYCOPROTEIN; 1.
DR Pfam; PF02872; 5_nucleotid_C; 1.
DR Pfam; PF07452; CHRD; 1.
DR Pfam; PF05787; PhoX; 1.
DR Pfam; PF13449; Phytase-like; 1.
DR PRINTS; PR01607; APYRASEFAMLY.
DR SMART; SM00754; CHRD; 1.
DR SUPFAM; SSF55816; 5'-nucleotidase (syn. UDP-sugar hydrolase), C-terminal domain; 1.
DR SUPFAM; SSF51004; C-terminal (heme d1) domain of cytochrome cd1-nitrite reductase; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:AFZ52437.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010480}.
FT DOMAIN 745..883
FT /note="CHRD"
FT /evidence="ECO:0000259|SMART:SM00754"
FT REGION 924..952
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2350 AA; 253862 MW; 231F1ABBCAE1070D CRC64;
MTINLNLIGT YATGQFDEGA AEIPAFDPST NRLFVVNAEA VTVDVLDLSN PNNPVKIGEI
DASALGGVAN SVAVKNGIVA IAIEANIKTD NGSVAFFNSD SDFSNPVNPV NTVTVGALPD
MVTFTPDGMK VLTANEGEAN DDYSVDPEGS ISIIDISTGV ENASVTNANF NAFDSQKDAL
VAQGVRIFGL NASVSQDLEP EYIAFSADSQ TAYVTLQENN ALAVVDVTTG TVSGIVPLGF
KNYNASPNLE TAFFEESELP IIGTSQTRGD IRLGGFSGLT FLGMNDSGNY EFLTHMDLGP
SETGNRDIND DGVEERVRTY LIPDLQPRLV KFEYNPNNGD TNILDQVLLT RQDGSPLTGL
PNLPTDDGGR IPIDEDGNIL DFDPLGADLE GLIQAPDGTF WAADEYRPAL YKFSAEGVLI
DRFVPEGLPA EVGTGVFPEA YNTRQANRGF EAIAFQDGKV YAFVQSPFDN PDSGETATTR
ILEFDPVSET VTGEYLYIQE DIGGGSDKIG DAVATNKNGE FLVIERDSSL EADSQKVIFR
INLNDATNLQ TLPDDVLEGD ETFDSLTPEE LAQKGINPVT KEVAINLTEI GYDFTDKPEG
LTVIDETTIA VINDNDFDEA GIPIGLGIIS LNNALDASNR DDSINIRNWP VFGMYQPDAI
ASYEVDGQTY LVTANEGDAR IRPDGDLEDD QGNVIIEEGE IFNEENRIND IILDPVAFPN
ARQLQENDQL GRLNITNTLG VSDRAIFVAE LTPDQEVPPA MSDAEGESFA FVDDNGFLNV
ELQVTGVDFG AVTGNPLTAD TGDDVILLHI HEAMRGMNGG VVWDLLADPD TEILIDNEGN
ATLTSIWQES DIPKTPQGED TNYYFNLHTE RNPGGELRGQ IQGEIAYEEL YAYGSRSFSI
WDSNGNLVFD SGDDFEQITA SLIPDDFNSN NDENGSFDAR SDDKGPEPEG VTVGEINGVP
YAFVGLERVG GVMVYDISDP TDAKFVQYIN NRDFSVDAQL EDGSPNPEAG DLGPEGLVFI
SAEDSPNGIP LLVVANEVSG TTSVYEIDDG FTRPNQPSQM KGLGDFVTEP VFTIGQIFNG
SQGYYVPPGI LDGLGAFALD EDTIRVLANH ELGSEVGYAY TLANGTQLTG GRISFFDINK
DTRQLEDVGQ AYDTIINRAG EVVDEASDLD FMGLDRLCSA QYIEANQFGE GRGLVDGLFF
TGEETDGGSE FVLDPETNTL YAVPWMGRAA WESVTELDTG TTDKVALLIG DDRGGAPLLL
YVGEKGQGEG ADILIRNGLA QGKLYVWVAD SGETTPEQFN GTNEQRSGSF VEIDFYRPDL
AGNGEYDELG FATQEKQDAL AEEVGAFKFS RPEDLATSPD DGTVAVLAST GRDSLFPSDS
WGTTYEIDAD FSDLDNITAQ LDVLYDGDDA GNGQFAGPDF GLRSPDNLEW ADNGLIYIQE
DRSIDEFGLT SGEEASIWEL NPETGVLNRI AQIDRTAVPE GQTDGDPDDI GDWESSGIID
VSNLFDETPG SLFLFDVQAH SIRDGIIAEE GLVQGGQLAF LENTNPTFTL QLLHASDQEA
GIPALQDAIG FSAVLNALDA QYLNTLKLSS GDLFIAGPFF NASRDIYGEV GIADILIQNE
LGWDAAAVGN HEFDAGPEAF YNAIAPNADI QGTGIDPTTG FTGANFPYLS TNLDYSTDSS
DLKDLVVPAG EAPESASLTE SVVVDVNGEQ IGVIGAVVPY LPQIANIGGI TMLTDPNSRD
IEENAQAIAD SVQPFVDELV AQGINKIVLM THLQQFEVEQ ALASKLRHVD ILMGGGSHRV
MANDDDTLRQ DETQTPPELL QPYPQVFQDA DGNDIYLINT AANYRYVGQL IVDFDAEGNI
ISVGDESGAF ATDIAGVDRL YEADITTFEQ VKAVADPELV EIVDGVGDFI NGKDGNIFGN
TEVWLNGLRS SVRTEETNLG NLTADANLWY AEQYGLEIDI SVKNGGGIRD QIGVSFIDGG
TNELIQLPPQ ANPAVGKEEG DVSQLDIENS LRFDNKLSVA DISAQGIKDL AEHLVAQWAE
GATPGQFGQI GGFSFSFDPD NTPIEFTRNN DGDATGVATP GERIQNLVLN REDGTQEAIV
VDGELVVDPS TTYKMVILDF LAGGGDGYPA FYFENVVRLD SLNPDSLPNN SDLPIAGEQD
ALAEYLAEFF PDGSQPFDQA DTPIEEDTRI QNLNFREDTI IADPTDPLLD TTIYRFRTGE
GTYIYVENEE RQRILQGGFN FVEEGEAFKV ALEDGENLEP IYRFRNNDLG GAYLYVGEAE
RQSIRQNFTN FIEEGLAFYT YGADAEQADD IFRFQTQPGG YIFVGDAERQ SIVNSDFNFA
QEGIAFEALA
//
