ID S6FAI5_9CLOT Unreviewed; 698 AA.
AC S6FAI5;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Putative Ser/Thr protein phosphatase family protein {ECO:0000313|EMBL:SLK19494.1};
GN ORFNames=CCH01_16860 {ECO:0000313|EMBL:SLK19494.1};
OS Clostridium chauvoei JF4335.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1351755 {ECO:0000313|EMBL:SLK19494.1, ECO:0000313|Proteomes:UP000190476};
RN [1] {ECO:0000313|Proteomes:UP000190476}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Falquet L., Falquet L.;
RL Submitted (MAR-2017) 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; LT799839; SLK19494.1; -; Genomic_DNA.
DR RefSeq; WP_021876001.1; NZ_LT799839.1.
DR AlphaFoldDB; S6FAI5; -.
DR STRING; 1351755.CCH01_16860; -.
DR GeneID; 66302010; -.
DR OrthoDB; 9800780at2; -.
DR Proteomes; UP000190476; Chromosome i.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; -; 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; IPR006179; 5_nucleotidase/apyrase.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
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; 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.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Hydrolase {ECO:0000256|RuleBase:RU362119};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362119};
KW Reference proteome {ECO:0000313|Proteomes:UP000190476};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 672..691
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 141..358
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
FT DOMAIN 435..578
FT /note="5'-Nucleotidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02872"
FT REGION 624..670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..646
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 647..669
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 698 AA; 76941 MW; 0550CA875DC70CE4 CRC64;
MWKKTNKKKF IAFLTTLTLV LGLIMPINCE KVYAVDGQPT EKVSEVFNNK DLENKILKDD
KKTIPEVTKS VEEVYTNIKN IKILGYEDNK DLESKVVQLI NLGKIKLNKD QDSITWEEIK
KQLSAEDLKA LVKGVNKKID ILSFNDIHGS VQETKKNTGV AKLTTEIKKY TNKNNEIYNS
FIVSGGDMYQ GSAMSNLKLG EPINKFAKEV GLLASAVGNH EFDWGTNNFE KWQEDGGFQF
LAANLIDKRT NNIASFAKPY LVVEENGVKI GLIGLATPDT LYTTKPTNVV DYDFTSGVEE
VNKYGKLLRE QEHVDAVVVI THMGAKLENG ELKGEAVDIA KNVQKGMVDA IVAAHDHRFT
AGEVNGVRIA EGGCNGKGLG KVSFTFDPSG KLVSVESSYD EVYKRKDTIK ADEKVQAMVK
QYEKELEIIL GEKIADLDVD LTNDKYNGIT VLGVTVCEAM KKITGADIAI TNGGGLRAPI
NKGVVTMGDL YTVLPFDNTL VTMDLKGEDI IKIIDYGIDP KTRGWGQFSG VKIWYNPENE
LGNRITSVRL PDGTKLESNK YYKVVTNDFM AVGGDNYDFS KAINVNNAGL VMRDEIADLW
RKEGISPKET NILVSGVDDT KDVVIPNTSK DKNETISKDE NKKPEVSQGK TTQANKVNKG
KSTKLPKTGT PFGATAMEIT GFMALAIGGY LSKKKKVS
//