ID G8QR75_SPHPG Unreviewed; 590 AA.
AC G8QR75;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=5'-nucleotidase/2',3'-cyclic phosphodiesterase-like hydrolase {ECO:0000313|EMBL:AEV31010.1};
GN OrderedLocusNames=SpiGrapes_3266 {ECO:0000313|EMBL:AEV31010.1};
OS Sphaerochaeta pleomorpha (strain ATCC BAA-1885 / DSM 22778 / Grapes).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Sphaerochaetaceae;
OC Sphaerochaeta.
OX NCBI_TaxID=158190 {ECO:0000313|EMBL:AEV31010.1, ECO:0000313|Proteomes:UP000005632};
RN [1] {ECO:0000313|EMBL:AEV31010.1, ECO:0000313|Proteomes:UP000005632}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1885 / DSM 22778 / Grapes
RC {ECO:0000313|Proteomes:UP000005632};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Munk A.C., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Ritalahtilisa K.,
RA Loeffler F., Woyke T.;
RT "Complete sequence of Spirochaeta sp. grapes.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the 5'-nucleotidase family.
CC {ECO:0000256|RuleBase:RU362119}.
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DR EMBL; CP003155; AEV31010.1; -; Genomic_DNA.
DR RefSeq; WP_014271849.1; NC_016633.1.
DR AlphaFoldDB; G8QR75; -.
DR STRING; 158190.SpiGrapes_3266; -.
DR KEGG; sgp:SpiGrapes_3266; -.
DR eggNOG; COG0737; Bacteria.
DR HOGENOM; CLU_005854_4_4_12; -.
DR OrthoDB; 9800780at2; -.
DR Proteomes; UP000005632; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008252; F:nucleotidase activity; IEA:UniProt.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
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 InterPro; IPR008334; 5'-Nucleotdase_C.
DR InterPro; IPR036907; 5'-Nucleotdase_C_sf.
DR InterPro; IPR006146; 5'-Nucleotdase_CS.
DR InterPro; IPR006179; 5_nucleotidase/apyrase.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR PANTHER; PTHR11575:SF6; 2',3'-CYCLIC-NUCLEOTIDE 2'-PHOSPHODIESTERASE_3'-NUCLEOTIDASE; 1.
DR PANTHER; PTHR11575; 5'-NUCLEOTIDASE-RELATED; 1.
DR Pfam; PF02872; 5_nucleotid_C; 1.
DR Pfam; PF00149; Metallophos; 1.
DR PRINTS; PR01607; APYRASEFAMLY.
DR SUPFAM; SSF55816; 5'-nucleotidase (syn. UDP-sugar hydrolase), C-terminal domain; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR PROSITE; PS00785; 5_NUCLEOTIDASE_1; 1.
DR PROSITE; PS00786; 5_NUCLEOTIDASE_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU362119, ECO:0000313|EMBL:AEV31010.1};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362119};
KW Reference proteome {ECO:0000313|Proteomes:UP000005632};
KW Signal {ECO:0000256|RuleBase:RU362119}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|RuleBase:RU362119"
FT CHAIN 23..590
FT /evidence="ECO:0000256|RuleBase:RU362119"
FT /id="PRO_5005133027"
FT DOMAIN 31..248
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
FT DOMAIN 352..496
FT /note="5'-Nucleotidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02872"
FT REGION 566..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 590 AA; 65319 MW; 6CD41B0E04A55398 CRC64;
MKRNIALLFI LALCLIVTPL FATGQNEVTV TILETSDMHG TFAPWDYATD SPLDQGWAKV
ATVIKQERAK DPNLLLVDNG DTSQDNMIQE FRFDTVHPVA RALNFLGYDA WQLGNHEFNF
EFENLQRLIA SVNATVLGGN IYKADGTRFA EPYMIKRVNG VRVAIMGLAP PHITRWEASD
PSHFNNMTFT TPMDETAKIL KELEGKADVI IALVHYGEDG EYDTEGMREI AAKYGDRISA
FLIGHAHSTL AEEQKNGSFI VEPGSKGSSV GKVEIKLLQR VSGGKWLIEE VKGSVIPVKG
QKIAADPAFL TEFKGIDEKS RMIANTAVGK VGADFLPSLY WKNIEGIPTA IVQDTAMIDL
INNVQMEATG ADVSLAALFD ATSDLPKGDF RKRDGVKIYK YDNTLMAVRV TGKQLKAIME
NQAGAFFNQY KKGDVTISFN SKIRMYNYDM FQGVTYDIDI SKPVGQRICN VMYKGKPLSD
SQVLVLALNN YRYGGLSSSG MISNKSEDLV YNSGLAIRDI ISDYVVKQGT IMPKCDNNWK
IIGAPLTDKD AEKIYAMVRE GKIKLPTSED GRTPNIEPLN ADDLRSKKVL
//
