ID A0A162PKN1_9BACT Unreviewed; 604 AA.
AC A0A162PKN1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Bifunctional metallophosphatase/5'-nucleotidase {ECO:0000313|EMBL:KYP14551.1};
GN ORFNames=A1D16_00230 {ECO:0000313|EMBL:KYP14551.1};
OS Flavihumibacter sp. CACIAM 22H1.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Flavihumibacter.
OX NCBI_TaxID=1812911 {ECO:0000313|EMBL:KYP14551.1, ECO:0000313|Proteomes:UP000075747};
RN [1] {ECO:0000313|EMBL:KYP14551.1, ECO:0000313|Proteomes:UP000075747}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CACIAM 22H1 {ECO:0000313|EMBL:KYP14551.1};
RA Moraes P.G., Lima A.R.;
RT "Draft Genome of Flavihumibacter sp. CACIAM 22H1.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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:KYP14551.1}.
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DR EMBL; LUKG01000038; KYP14551.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A162PKN1; -.
DR STRING; 1812911.A1D16_00230; -.
DR Proteomes; UP000075747; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; IPR006179; 5_nucleotidase/apyrase.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR11575; 5'-NUCLEOTIDASE-RELATED; 1.
DR PANTHER; PTHR11575:SF42; SULFUR OXIDATION PROTEIN SOXB; 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; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU362119};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362119}.
FT DOMAIN 91..314
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
FT DOMAIN 388..533
FT /note="5'-Nucleotidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02872"
SQ SEQUENCE 604 AA; 67262 MW; AF9F1B6827AA8EE1 CRC64;
MPIPSSTPCN CSACSGKDLP QAEKILHLQI SENSRRDFLR NAGRLGLGLG IGGGLLASPM
ALSANNPNEA IDKLNEIDRN KAVLTGKANR FTILHTADIH AQLLVHDEFF IEKGQPVYKK
RGGLATLKTM INSLRQQQPA TTLVIDGGDC FQGSGVAALT EGRAIVPLMN NIGYDIMLPG
NWEVVYGKER MMKDMFAYDG VKVCANMFHA TQDELNGDLI FPPYFVKHIG NLKIGFIGYN
DPLTPKRQSP AYSNGINFTA PEKNLAKYIR LLKEYEQCDM VFLLTHMGLA QQIGLSNMQA
AKGADYILGA DTHERVRQPI QGIHAKVTEP GAFGSFLARL DFVVEAGIIK DQSYQLLDVD
PEKYPEDPEM KRMIEAARAP YKKILHRVIG QTKTPLVRYY VIETPMDNFI TDAIMWKFKP
DIALSNGFRF CPPLVPDPKT GKADITMDYL WNMLPVDSEA KRGIITGEQL WNWMEKELHN
AFAKDPAKRF GGWVVRFQGM QVNFTIANEQ GQRINWIKVG GQPLDKSASY SFVACEREGD
PDTTICRVEG VKEPTRLGAT LHSVLQEYLA LHSPIAPKLE GRCTATDAPN SLLTQLMGYG
YEFR
//