ID B0KCW2_THEP3 Unreviewed; 1226 AA.
AC B0KCW2;
DT 18-MAR-2008, integrated into UniProtKB/TrEMBL.
DT 18-MAR-2008, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE SubName: Full=5'-nucleotidase., 2',3'-cyclic-nucleotide 2'-phosphodiesterase {ECO:0000313|EMBL:ABY95569.1};
DE EC=3.1.3.5 {ECO:0000313|EMBL:ABY95569.1};
DE EC=3.1.4.16 {ECO:0000313|EMBL:ABY95569.1};
DE Flags: Precursor;
GN OrderedLocusNames=Teth39_1938 {ECO:0000313|EMBL:ABY95569.1};
OS Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) (Clostridium
OS thermohydrosulfuricum).
OC Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Thermoanaerobacter.
OX NCBI_TaxID=340099 {ECO:0000313|EMBL:ABY95569.1, ECO:0000313|Proteomes:UP000002156};
RN [1] {ECO:0000313|Proteomes:UP000002156}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33223 / DSM 2355 / 39E
RC {ECO:0000313|Proteomes:UP000002156};
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Bruce D., Goodwin L., Saunders E., Brettin T.,
RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Lykidis A., Hemme C., Fields M.W., He Z., Zhou J.,
RA Richardson P.;
RT "Complete sequence of Thermoanaerobacter pseudethanolicus 39E.";
RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP000924; ABY95569.1; -; Genomic_DNA.
DR RefSeq; WP_012269670.1; NC_010321.1.
DR AlphaFoldDB; B0KCW2; -.
DR STRING; 340099.Teth39_1938; -.
DR KEGG; tpd:Teth39_1938; -.
DR eggNOG; COG0737; Bacteria.
DR eggNOG; COG3103; Bacteria.
DR HOGENOM; CLU_001272_0_0_9; -.
DR Proteomes; UP000002156; Chromosome.
DR GO; GO:0008663; F:2',3'-cyclic-nucleotide 2'-phosphodiesterase activity; IEA:UniProtKB-EC.
DR GO; GO:0106411; F:XMP 5'-nucleosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009166; P:nucleotide catabolic process; IEA:InterPro.
DR CDD; cd00845; MPP_UshA_N_like; 1.
DR Gene3D; 3.60.21.10; -; 2.
DR Gene3D; 3.90.780.10; 5'-Nucleotidase, C-terminal domain; 2.
DR Gene3D; 2.30.30.40; SH3 Domains; 2.
DR InterPro; IPR008334; 5'-Nucleotdase_C.
DR InterPro; IPR036907; 5'-Nucleotdase_C_sf.
DR InterPro; IPR006179; 5_nucleotidase/apyrase.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR019079; Capsule_synth_CapA.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR003646; SH3-like_bac-type.
DR PANTHER; PTHR11575:SF48; 5' NUCLEOTIDASE, ECTO-LIKE; 1.
DR PANTHER; PTHR11575; 5'-NUCLEOTIDASE-RELATED; 1.
DR Pfam; PF02872; 5_nucleotid_C; 2.
DR Pfam; PF00149; Metallophos; 2.
DR Pfam; PF08239; SH3_3; 2.
DR PRINTS; PR01607; APYRASEFAMLY.
DR SMART; SM00854; PGA_cap; 1.
DR SMART; SM00287; SH3b; 2.
DR SUPFAM; SSF55816; 5'-nucleotidase (syn. UDP-sugar hydrolase), C-terminal domain; 2.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 2.
DR PROSITE; PS51781; SH3B; 2.
PE 4: Predicted;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Hydrolase {ECO:0000313|EMBL:ABY95569.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002156}.
FT DOMAIN 1096..1158
FT /note="SH3b"
FT /evidence="ECO:0000259|PROSITE:PS51781"
FT DOMAIN 1166..1226
FT /note="SH3b"
FT /evidence="ECO:0000259|PROSITE:PS51781"
FT REGION 1071..1092
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1075..1092
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1226 AA; 134247 MW; 56BCE5CD65B9932D CRC64;
MFRSRSRILA IFVGAIMVFS MFFSAVPQIA FAATSKTFDF IEVTDFHGYL QNDGKLSDGT
IYKQQIAGVL AKQIKDIKAQ NPDRTVILSD GDMFQGTPLS NVLKGQPVIE MIKNIGFDAM
TLGNHEYDWG IDSVIDTQNA TLKNSTIPVL AANVYDKTTG QPVNYVKPYV MIEKDGVKIG
IIGIVDNKEF PNIIMPAYIQ NVEFKDPVPI VNDLAQQLRQ QGAQIVVVLA HMGAYQDKSG
NATGNLIDFA KQVQGVDAIF GGHTHSIVTT RVNGIPVGVA YYYGRGFIDL KITLNNDGTV
TTGDMQYIDI TGLYSTQNPV VDPEVQAIVD KAVQDVGPIF NEVIGQAAID LTRTQSAQPY
GDSLLGNWAA QVTKDAVGAD FGFANNGGLR IDIPKGDITV GMMYQLMPFD NTIVTMKMTG
AQVKTILEQA VQDGGKGIQV AGLTFKYDPS KPSMQRVFDM RKSDGTPILM DKTYLVATNN
FMGTGGDGFT GFTDPDVVKT YVDTYKLVRD AFIDAVKAQK TVTSKIDNRI APAKMSDATI
AVLATSDIHG NIFPWDYNTA KPANQGLAKV STYVKQVRAQ YPYVVLVDNG DTIQGTPLSY
YYDKIDTTTE YPLAKVMGAM KYDTWTLGNH EYNYGLDVLN RVINDMRNEG IHVLSANTYK
DDGTNFVDPY YIKTFDTPQG PVKVGILGLT TKTIPSWEDK DHYAGLHFND LVEEANKWVP
KLREAGADIV VVAMHSGEES PTDVIPENQV IAVATQVNGI DAIVAGHTHA IISQHTYKNP
AGETVIVTEP GKWGQYVSQI NFNISKNADG KWVIDSKWSA TIKMDDSVQA DPDILNLAQP
YQDATLKYIG TKIGVATGDF LGTEQTVKET AIMDLINKVQ KYYAKTDLSI AAPLSSSAKI
LKGDITIQDI MGVYVYENYL YGIKMTGKQL KDWLEWSARY YKQVSSPNDP ITKDPTLNIP
DYNLDQLYGA SYVIDLTQPA GHRIKNLKVN GKLVKDDDVF TVAINNYRFN GGGGFMQAAG
ITNPEIVFDS AKAYGDDGQV RNLMIRYIQE HGTITPTVEK YWYVSTTPVA EETPSPVTQP
TPAPTPQPQP APQPVYNYGI VTASALNVRA GASTSSKIIG VLPAGKVVTL LEEVNGWYKI
DYNGKTGYIY GKYVAATPNP SKVTVLKAVK VTAKSGLNVR VGNSINAKKI GAVPYGTELK
VVGEYNGWYQ IQYNGGFGYV YAKYTK
//
