ID Q97M47_CLOAB Unreviewed; 1193 AA.
AC Q97M47;
DT 01-OCT-2001, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2001, sequence version 1.
DT 27-MAR-2024, entry version 133.
DE SubName: Full=2,3-cyclic-nucleotide 2'phosphodiesterase (Duplication) {ECO:0000313|EMBL:AAK78333.1};
GN OrderedLocusNames=CA_C0353 {ECO:0000313|EMBL:AAK78333.1};
OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS / VKM B-1787).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=272562 {ECO:0000313|EMBL:AAK78333.1, ECO:0000313|Proteomes:UP000000814};
RN [1] {ECO:0000313|EMBL:AAK78333.1, ECO:0000313|Proteomes:UP000000814}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787
RC {ECO:0000313|Proteomes:UP000000814};
RX PubMed=11466286; DOI=10.1128/JB.183.16.4823-4838.2001;
RA Nolling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA Doucette-Stamm L., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA Smith D.R.;
RT "Genome sequence and comparative analysis of the solvent-producing
RT bacterium Clostridium acetobutylicum.";
RL J. Bacteriol. 183:4823-4838(2001).
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DR EMBL; AE001437; AAK78333.1; -; Genomic_DNA.
DR PIR; B96943; B96943.
DR RefSeq; NP_346993.1; NC_003030.1.
DR RefSeq; WP_010963675.1; NC_003030.1.
DR AlphaFoldDB; Q97M47; -.
DR STRING; 272562.CA_C0353; -.
DR DNASU; 1116536; -.
DR GeneID; 44996864; -.
DR KEGG; cac:CA_C0353; -.
DR PATRIC; fig|272562.8.peg.546; -.
DR eggNOG; COG0737; Bacteria.
DR HOGENOM; CLU_001272_0_0_9; -.
DR OrthoDB; 9800780at2; -.
DR Proteomes; UP000000814; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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: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 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; IPR019931; LPXTG_anchor.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR NCBIfam; TIGR01167; LPXTG_anchor; 1.
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; PF00746; Gram_pos_anchor; 1.
DR Pfam; PF00149; Metallophos; 2.
DR PRINTS; PR01607; APYRASEFAMLY.
DR SUPFAM; SSF55816; 5'-nucleotidase (syn. UDP-sugar hydrolase), C-terminal domain; 2.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 2.
DR PROSITE; PS00786; 5_NUCLEOTIDASE_2; 1.
PE 4: Predicted;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Cell wall {ECO:0000256|ARBA:ARBA00022512};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Peptidoglycan-anchor {ECO:0000256|ARBA:ARBA00023088};
KW Reference proteome {ECO:0000313|Proteomes:UP000000814};
KW Secreted {ECO:0000256|ARBA:ARBA00022512};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1164..1182
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 46..250
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
FT DOMAIN 334..491
FT /note="5'-Nucleotidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02872"
FT DOMAIN 543..774
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
FT DOMAIN 853..1029
FT /note="5'-Nucleotidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02872"
FT DOMAIN 1147..1187
FT /note="Gram-positive cocci surface proteins LPxTG"
FT /evidence="ECO:0000259|Pfam:PF00746"
FT REGION 1091..1147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1193 AA; 128814 MW; FB5642C7F8845B87 CRC64;
MSKQKKLNYL TARMLLIFFV IFTLLGNFPL RSFAASNDKT FDLVEINDFH GALEDTSNPA
NPVASVLGNR VKAVSASNPD TIVFGGGDLY QGSALSNILK GVPVQKVMDS LGMQFTTLGN
HEFDWGLDTL TNTTMQGANY NIICSNLYNK NPDGSKGSRV FDPYKIITKD GVRIAFIGGI
TNETPNIVTP SYVSDKIFTD LATEINSVAS DIKNNNKADV IIAVVHEGED NLDNIVSKLS
NVNAVFGGHT NTIEEKLVNN IPVINANCNG KGFADLKMTV AADGSVHFLN TTSSYIALDN
ANGYKSSNPT TDPDISSIVN DAKASVGPTL NQVLGNIKNT ITRTQTSNPY GESALGNWAS
DVIKNYANAD IGISNNGGLR TDLSSGDVTY GDIYALMPFD NDIETVTLNK AQLKDILEQA
VGNYQDSSYP NTTLGGKGLQ VSGIKFTYDP SKSYGNKITS ITRENETPIN DTETLKLAGP
DFVLTGGDGF LRFNKSDIKS TLADTHKLVR DALMDNVKAN NTVNYTMDNR IVNSATQIPS
TISILATSDI HGNVLNYDYA TGKAPTNTQG LAKVSSYVNS VRASKPNVML IDDGDTIQGT
PLSYYYDKID TTSEYPLMKI MGAMKYDTWT LGNHEFNYGL PTLNRVISDA RKENINVLSA
NTYNSDNTNF VNPYYIKTFN INGKTVNVGI LGLTTKCIPD WEDPSHYAGL HFNDLVDEAK
LWVPRMKAAG ANVVIVAAHS GEEGAADTIP ENQIKAIATN VSGIDAIVAG HAHVTVNDTS
LKNPNGKTVP VVEPNKWGTF VSQIDITLDN SGNASTINTQ NVKMTDSIPE DPNIVNIIQP
YQNKTLDYIS TKLGTSTGEF TGSNQTTQPT AIMELINKVQ KDAANAQLSI AAPLSSSAYI
PKGDVTIKDI MSVYVYENYL YGIKMTGKQL KDWLEYSVRY YKQVSSPNDS IAKDPALNVP
DYNLDQLYGA TYDIDLTQPA CTIDPSTGRI ASGDRIKNLK INGVPIKDSD VFTVAINDYR
YNGGGGFMKA AGISNTDPSI VTYSSAKALG DDGQVRSLMQ SYIKNNQTIS PENSNNWKLY
TTPVSDTSTV PVAPTPIVNP LPTNNSTTST GSNIPGEATT GAQPSSTTTS DAPNCQLSPN
SECQENTTSI KTLPKTGSMI DSTVLLIIGT LLLLLGLAFI IWNKFKNKQK SVQ
//
