ID B1R6Z5_CLOPF Unreviewed; 724 AA.
AC B1R6Z5;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=Ser/Thr protein phosphatase family protein {ECO:0000313|EMBL:EDT23978.1};
GN ORFNames=AC1_2652 {ECO:0000313|EMBL:EDT23978.1};
OS Clostridium perfringens B str. ATCC 3626.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=451754 {ECO:0000313|EMBL:EDT23978.1, ECO:0000313|Proteomes:UP000004342};
RN [1] {ECO:0000313|EMBL:EDT23978.1, ECO:0000313|Proteomes:UP000004342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B str. ATCC 3626 {ECO:0000313|Proteomes:UP000004342};
RA Paulsen I., Sebastian Y.;
RT "Annotation of Clostridium perfringens B str. ATCC 3626.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a nucleoside 2',3'-cyclic phosphate + H2O = a nucleoside 3'-
CC phosphate + H(+); Xref=Rhea:RHEA:19621, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:66949, ChEBI:CHEBI:66954; EC=3.1.4.16;
CC Evidence={ECO:0000256|ARBA:ARBA00001730};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 3'-phosphate + H2O = a ribonucleoside +
CC phosphate; Xref=Rhea:RHEA:10144, ChEBI:CHEBI:13197,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:18254, ChEBI:CHEBI:43474; EC=3.1.3.6;
CC Evidence={ECO:0000256|ARBA:ARBA00000527};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|ARBA:ARBA00001968};
CC -!- SIMILARITY: Belongs to the 5'-nucleotidase family.
CC {ECO:0000256|RuleBase:RU362119}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EDT23978.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ABDV01000010; EDT23978.1; -; Genomic_DNA.
DR RefSeq; WP_003457402.1; NZ_ABDV01000010.1.
DR AlphaFoldDB; B1R6Z5; -.
DR Proteomes; UP000004342; Unassembled WGS sequence.
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; cd07410; MPP_CpdB_N; 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; IPR006146; 5'-Nucleotdase_CS.
DR InterPro; IPR006179; 5_nucleotidase/apyrase.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR041827; CpdB_N.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR NCBIfam; TIGR01167; LPXTG_anchor; 1.
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; PS00786; 5_NUCLEOTIDASE_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Hydrolase {ECO:0000256|RuleBase:RU362119};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362119};
KW Signal {ECO:0000256|RuleBase:RU362119}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|RuleBase:RU362119"
FT CHAIN 23..724
FT /evidence="ECO:0000256|RuleBase:RU362119"
FT /id="PRO_5039751627"
FT DOMAIN 40..257
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
FT DOMAIN 352..501
FT /note="5'-Nucleotidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02872"
FT REGION 600..700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..627
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..690
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 724 AA; 81424 MW; 301E3704F04B71D4 CRC64;
MRKLIKPLSV ATMMFLSLNL CFFNGKLVKG EEISNETKVT ILGTSDIHGR FVPWEYSSDT
ENKSGSLSQI STIVKKERNE NPNLILVDAG DSIQDNFVET FNKGPQQPMV LGMNKMKYDV
WEMGNHEFNF GLDVLKHVTS QFEGKVLAGN IYNDDGTRFM DGYTIIERDG IKIGIIGMDT
PMIKEFEKPY NIKGIEFRDP VKETKKIIKE LDGKVDAMIG VMHMGLDNEN AISNTGVTDI
ANQCPELTAI VGGHMHKLVK NEVVNGVIIT EPGKYGQAVS KIDLTFKKEN GKNVLKNKNA
DTISVANVES DKEIEDLLKP FHEELRKDAN SVIGRLEGVN MVDEDYIKGI PTIHIEDTPL
IDFFHEVGKY YSKADVIALS IDNDKAKLNV GDIKKKDIAY NYRYTGGEIS VYEVTGKDLK
KYMEWAAGYF NTLNPGDITP SFNPKRRASK YSTNDMFGGI TYKIDLREKE GNRIKDVKYK
DGRELKDTDV LKLGMNSYRL GQLQGKGGIF EGKEFKKLWD SKTAYGEEEG TIRNLAIDYI
KNVKNGLINA KKQNNWCLLG IDPNSENYKK VRDLVNSGEL KIPTSEDGKY TNIASINEKD
LPLDNNTSKE NEENINLDSI NNKNNKDQVV NEESKKDVPK VEENIEKQKN NKENNSNEDN
TLVKEDSKSK EENEKNNEQN NIEEVSKKEN KLPNTGSPIG AEAMSQIGIL VLGAGVILKK
KNKK
//
