ID   D6ZVI7_BIFLJ            Unreviewed;      1311 AA.
AC   D6ZVI7;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   SubName: Full=5'-nucleotidase/2',3'-cyclic phosphodiesterase-like esterase {ECO:0000313|EMBL:ADH00893.1};
GN   OrderedLocusNames=BLJ_1449 {ECO:0000313|EMBL:ADH00893.1};
OS   Bifidobacterium longum subsp. longum (strain JDM301).
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=759350 {ECO:0000313|EMBL:ADH00893.1, ECO:0000313|Proteomes:UP000006740};
RN   [1] {ECO:0000313|EMBL:ADH00893.1, ECO:0000313|Proteomes:UP000006740}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JDM301 {ECO:0000313|EMBL:ADH00893.1,
RC   ECO:0000313|Proteomes:UP000006740};
RX   PubMed=20525832; DOI=10.1128/JB.00538-10;
RA   Wei Y.X., Zhang Z.Y., Liu C., Zhu Y.Z., Zhu Y.Q., Zheng H., Zhao G.P.,
RA   Wang S., Guo X.K.;
RT   "Complete genome sequence of Bifidobacterium longum JDM301.";
RL   J. Bacteriol. 192:4076-4077(2010).
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; CP002010; ADH00893.1; -; Genomic_DNA.
DR   RefSeq; WP_013141101.1; NC_014169.1.
DR   KEGG; bll:BLJ_1449; -.
DR   HOGENOM; CLU_260659_0_0_11; -.
DR   Proteomes; UP000006740; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
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   Gene3D; 2.60.40.1260; Lamin Tail 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; IPR001322; Lamin_tail_dom.
DR   InterPro; IPR036415; Lamin_tail_dom_sf.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
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; PF00932; LTD; 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; SSF74853; Lamin A/C globular tail domain; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR   PROSITE; PS51841; LTD; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius}; Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..36
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           37..1311
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003092076"
FT   TRANSMEM        1282..1303
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          42..168
FT                   /note="LTD"
FT                   /evidence="ECO:0000259|PROSITE:PS51841"
FT   REGION          166..215
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1248..1277
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        166..204
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1311 AA;  138474 MW;  50B3D4E1EA2C904B CRC64;
     MFHTNNFTAM SRRAIALLTA AVTLSSIALI GVPAAAADEQ QATAEQNTAA KPSVIINEVY
     AGNTKAAGDP DSKRCDWVEL KNTGSTDVDV KGWGIYDSGK KAKKHYTIGT SEVTNTDTVI
     KAGGYLVAYI DPDKAEPGLG SDADEAYLTT TSGDFTDSDV VDSTSWNTDT TGVKKMSDSQ
     SWSRKDDGTF ALSDTPTLGA QNVFDDPTPT PPAGETMTVD AWSGLADVTT VDAEGEFGAK
     GQGGDHTDGN LSGLVYEAGK DGKQGVLWAA DNDLNPTLGN TADKGPGSIN KFVYQNGTWQ
     QDPTDGWTFT NNGQTKGGKQ LHFKDGKGGV DSEGITLING DSSKGIFIGA ERDNENKNVP
     RPSILQYDVT EKTTDANGDG AHDLNATHEW NLIAALTQFG VTLGHGADAN LGVEGIAFIP
     DSVLTANGFQ SNLDPKNVVT YDPDGFGNDF GGLFFAALEK TGHIYAFALQ TVNDEDLVHP
     VADIDLPQSA VNAGYDGPRD LTWDAEHNQL LAQSDNDANT GAKIGTYEFK NGVLQLTKLT
     DAPDEIRTQN TEGFAITPDT EATKVVNGKV YKPVFWADDG VTNGHSLRMG YMATNQPVPA
     STTINLLNFN DFHGRIDKNL TVPFAATIEQ LKGEYPDSSL LLSAGDNIGA SLFNSSVQQD
     QPTIDVLNAL GVKASAVGNH EFDQGYADLT DRVIGKEGAR NAQWDYLGAN VYKKGTTTPA
     LPEYSIQEVN GVKVGIIGAV TQETGTLVAP GGVKDIEFGD PVEAVNRVAK QLTDGDESNG
     EADVIVAEYH EGAASNEDDA TAKPTLDEQK AASLVFQKIV DDTDAAVNVI FTAHTHMKYS
     YTDPAHNNRP IIQTGSYAAN IGQVVLTYNT ATGAVSYDKS GNTAVQVASQ PADKNDPHYN
     DYAEYNDGLL AAANPTVAKV RDIVYQALKV ADEKGGEKVG KVSADITTAF KDGKRDDRAS
     ESTMGNLVAD ALLDSLKGED RGAAEIGVVN SGGLRAEFCK SGTNDACTLD TDGNITYAQA
     NAVLPFLNNL WTTTLTGAQF KEALEQQWQT NADGSTPSRA YLQLGLSHNV SYTYDPDAAQ
     GHHITSVTVN GEPLDLKRNY RIGSFSFLLE GGDNFRAFAQ GTNTKDTGLV DRDAWIDYLK
     DNNPVAPRYD RRAVAVTGIP TGAVKAGGSF TLHFSKLTLT SLGVPDETKL TATIGEQMVG
     EAQVANGDTS ELKVTIPAGT KTGDISLTVT GATNKTTVAL PVAVTGVSTG TDDKDNGNHS
     GSVNANGSTK PQQTEHTANT GASVALVVVL ATLFAAGGVT IVVKRHDAAR K
//