ID K9T5R4_9CYAN Unreviewed; 2563 AA.
AC K9T5R4;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Putative extracellular nuclease {ECO:0000313|EMBL:AFY77334.1};
GN ORFNames=Ple7327_1998 {ECO:0000313|EMBL:AFY77334.1};
OS Pleurocapsa sp. PCC 7327.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Pleurocapsales; Hyellaceae;
OC Pleurocapsa.
OX NCBI_TaxID=118163 {ECO:0000313|EMBL:AFY77334.1, ECO:0000313|Proteomes:UP000010382};
RN [1] {ECO:0000313|EMBL:AFY77334.1, ECO:0000313|Proteomes:UP000010382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7327 {ECO:0000313|EMBL:AFY77334.1,
RC ECO:0000313|Proteomes:UP000010382};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A., Kyrpides N.,
RA Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT "Finished genome of Pleurocapsa sp. PCC 7327.";
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR601952-2};
CC Note=Binds 1 Mg(2+) ion. {ECO:0000256|PIRSR:PIRSR601952-2};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR601952-2};
CC Note=Binds 2 Zn(2+) ions. {ECO:0000256|PIRSR:PIRSR601952-2};
CC -!- SIMILARITY: Belongs to the alkaline phosphatase family.
CC {ECO:0000256|RuleBase:RU003946}.
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DR EMBL; CP003590; AFY77334.1; -; Genomic_DNA.
DR RefSeq; WP_015143638.1; NC_019689.1.
DR STRING; 118163.Ple7327_1998; -.
DR KEGG; plp:Ple7327_1998; -.
DR PATRIC; fig|118163.3.peg.2213; -.
DR eggNOG; COG0584; Bacteria.
DR eggNOG; COG0737; Bacteria.
DR eggNOG; COG1785; Bacteria.
DR eggNOG; COG2374; Bacteria.
DR eggNOG; COG2931; Bacteria.
DR eggNOG; COG4222; Bacteria.
DR HOGENOM; CLU_228086_0_0_3; -.
DR Proteomes; UP000010382; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016791; F:phosphatase activity; IEA:InterPro.
DR GO; GO:0008081; F:phosphoric diester hydrolase activity; IEA:InterPro.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR GO; GO:0009166; P:nucleotide catabolic process; IEA:InterPro.
DR CDD; cd08602; GDPD_ScGlpQ1_like; 1.
DR CDD; cd10283; MnuA_DNase1-like; 1.
DR CDD; cd04486; YhcR_OBF_like; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR Gene3D; 3.90.780.10; 5'-Nucleotidase, C-terminal domain; 1.
DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR Gene3D; 3.60.10.10; Endonuclease/exonuclease/phosphatase; 1.
DR Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 1.
DR InterPro; IPR008334; 5'-Nucleotdase_C.
DR InterPro; IPR036907; 5'-Nucleotdase_C_sf.
DR InterPro; IPR001952; Alkaline_phosphatase.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR InterPro; IPR030395; GP_PDE_dom.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR027372; Phytase-like_dom.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR InterPro; IPR011049; Serralysin-like_metalloprot_C.
DR PANTHER; PTHR42834; ENDONUCLEASE/EXONUCLEASE/PHOSPHATASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_3G09210); 1.
DR PANTHER; PTHR42834:SF1; ENDONUCLEASE_EXONUCLEASE_PHOSPHATASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_3G09210); 1.
DR Pfam; PF02872; 5_nucleotid_C; 1.
DR Pfam; PF00245; Alk_phosphatase; 1.
DR Pfam; PF19580; Exo_endo_phos_3; 1.
DR Pfam; PF03009; GDPD; 2.
DR Pfam; PF13449; Phytase-like; 2.
DR PRINTS; PR00113; ALKPHPHTASE.
DR SMART; SM00098; alkPPc; 1.
DR SUPFAM; SSF55816; 5'-nucleotidase (syn. UDP-sugar hydrolase), C-terminal domain; 1.
DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
DR SUPFAM; SSF51120; beta-Roll; 1.
DR SUPFAM; SSF56219; DNase I-like; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR SUPFAM; SSF51695; PLC-like phosphodiesterases; 1.
DR PROSITE; PS51704; GP_PDE; 1.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|PIRSR:PIRSR601952-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR601952-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000010382};
KW Zinc {ECO:0000256|PIRSR:PIRSR601952-2}.
FT DOMAIN 607..984
FT /note="GP-PDE"
FT /evidence="ECO:0000259|PROSITE:PS51704"
FT REGION 327..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 435..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1195..1227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1205..1227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 57
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT BINDING 13
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 13
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 264
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 269
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 312
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ SEQUENCE 2563 AA; 274212 MW; 4F81AE3F3F2C2726 CRC64;
MANTNSVIFI HPDGTSPSHY AAARFLHYGP DGRLNWDRMS NAGVYLGHMK DQLTGTSNAG
AVTHAMGVKV QADSFGLDEN GNPVVSQSGK TGLTIMEEAI AAGKATAIIN SGIIAEPGTG
AFLAQAESRS DLTGITAQIL ESGVNVILGG GEIHYLPVGT VGRFGEEGVR KDGRNLIEQA
RAKGYTVVYT LEELQNLPPR TQKVLGIFAA EDTYNDQPEE VNAAEGLGNY GQPGNENPPT
VAQMLEAALS IVSQNPNGFM VVMEEEGTDN FSNNNNAAGL VEAAKRADDA IGVAQNYIDN
VNPNTLLITA ADSDAGGLEV RDPLAADETV GTEEVNPTTE PGTEVPLDGT NGANTEPFIS
QPDANGNTYP FGIGWATQSD VPGSIVAKTY GLNADKLPST LDNTEIYRLM YQTLFGVKPK
EVPRPELEGF ASLPADSFAQ GPPAGADNGK GQPIAANDRT GPFEGQPIQG FSGVQFADGE
NFWFLSDNGF GAKNNSADYL LRIYKADPNF VGSEAGDGSV NVEEFVQLSD PKRLIPWEIT
NANTEERLLT GADFDVESLV VAEDGSFWMG EEFGPYLLHF DANGVLQEAP ISTPNLPNLK
TLNEQEPLVI GHRGASGELP EHTLAAYERA ILQGADFIEP DLVSTKDRVL IARHEPMLAV
VDPATGEVIP ANTTTDVATR PEFADRRTTK TVDGVSYTGW FAEDFTLEEI KTLRAVQPRD
YRDQSFNGLY EIPTLEEIID LVQDIEARTG QKIGIYPETK HPTYFAQQGL SLEEPLVETL
LDKGFTDPNR LFIQSFEVQN LLKLDKQLLP GTPLENTPLV QLYDEFQLQP YDIVSNFSDP
NFDPVSIYGT DLITAETTYG DLINQGSDSE VNLLKDFVAT YADGIGPWKR TFVLTEKLDT
PVDGNGDGIP EITEQLTGEV LPVVEDAHEA GLQVHPYTFR DEERFLVLKE DGTPQTAEEE
YEQYIQLGVD GFFTDFPKTG DLVRDRVIGE FVRSPDNPFL TDDPEEANLA SSRGFEGMAY
SPDRATLYPL LEGSVEGDPD NALRIYEYDV ANSSYSKDLV GYYRLDDPSH AIGDFTPINQ
NEFLVIERDG NEGEEAQFKK IFQVDFSKVD ENGFVFKKEL VDLLNVQDPN DINGDGSTTF
TFPFVTIEDL LVIDENTLLV ANDNNYPFSI GRPPEIDNTE IIQIKLPEPL NLDPRLGRAS
GDRNPSPSAI ATAQITPASD PNAQSNSKGT VEISAIQGES QTSPLVGQTV KTTGIVTAVD
ERGFYLQDAE VDSNDATSEG IFVFTDSAPT VAVGDELEIE GTVQEFLSGG KDTGNLSVTQ
IVRPAITTRS TGNDLPAALI LGEGGRTPPS EIVENDNFEV FDPQEDAIDF YESLEGMRVT
IQNPVAVSPT NEFGEIWTVT DKGALATPGL NSRGGIPLQA DDTNPERIQV QLDAQVLPDF
ETSVKVADKL SDVTGVVNYN FGNYEVVATE AFEVTNGGLG QEETTLVGTE NQLTVASYNV
LNLDPSDTEQ IAQIASQIVN NLKSPDILAL QEIQDNSGAT DDGTTAGDRT LQTLADAIAA
AGGPTYQFAE VPPADGTSGG QPGGNIRVAY LYNPQRVQLN KNSLQSLDVE AFNDSRDPLV
ADFTFNGETV TIVNNHWTSR VGSTPIFGAT QPFVQAGEDE RNAQAEVVNN FVDGLLAKNP
DANVIVTGDF NTFEFTDTLS QLAGEGDERV LTNLIGKATD DATYSYNFQG NSQSLDHIFA
SDRLYENAEF DSIHVNADFP TQASDHEPIL GRFRLTESKP EPASEAFTLQ LLHGSDFEAG
IEALDDAPRF SAVINGLRDD YKNTLVLSSG DNYIPSPFLF AASDPSLANT PVGTEGIGRA
DIEILNQIGI QASAFGNHEF DLGTREVQGL ISPDENYRGT QFPYLSSNLD FSTDSNLSGL
VTANGQEAST IPNTIAESTV ITVNGEKIGI VGATTPLLPS ISSSGDVGVI PSDPNNVAAL
AAEIQKTVDE LTATGIDKVV LLSHFQQLRI EQAVAPLLRD VDIIVGGGSH TLLSDESDRL
RSGDTSGGTY PILTTSASGE PIALVNTDAN YRYVGRLVAD FDANGVLVPE SIDPNISGAY
ATDEQGVTDV GGTPDPEVVA ITDTLGNVIN EQDGNIFGKT DVFLRGDRTF VRTEETNLGN
LTADANLAAA QAVDPSTVIS IKNGGGIRSS IGVIEAAGGS TDPDDFALLP TAANPEASKE
EGDISQLDIA NSLRFNNGLT LLTLTAEQLL QTIEHGVAAT ASGETPGQFP QVSGISFSFD
PDLPEGDRVL SLAVTDDEGN VTDVVAQNGE LQGDPNRTFR TVTLDFLAGG GDDYPFATFA
NTNPVELVTE DSENPAPSNR TGVATFAADG SEQDALAEYL AANFNEQNPF DVADVAPEKD
TRIQNLNFRE DTVLSANVAP ASTELPETVF GTSGDDVFDA ADPSGNFDGS KDIVSAGEGS
DRFFLGAGEG DNLLTGGIGA DQFWITSSDD GLPSVANTIT DFNSTEGDVI GFADTSLSYG
ALGGDWNLRQ AGNDAVIEAF GQDVAILQGI QADSLTETNF VFG
//
