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Database: UniProt
Entry: A0A1X7K0J0_9BACL
LinkDB: A0A1X7K0J0_9BACL
Original site: A0A1X7K0J0_9BACL 
ID   A0A1X7K0J0_9BACL        Unreviewed;      1685 AA.
AC   A0A1X7K0J0;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'-or 3'-nucleotidase, 5'-nucleotidase family {ECO:0000313|EMBL:SMG33991.1};
GN   ORFNames=SAMN06295960_1923 {ECO:0000313|EMBL:SMG33991.1};
OS   Paenibacillus aquistagni.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1852522 {ECO:0000313|EMBL:SMG33991.1, ECO:0000313|Proteomes:UP000193834};
RN   [1] {ECO:0000313|EMBL:SMG33991.1, ECO:0000313|Proteomes:UP000193834}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=11 {ECO:0000313|EMBL:SMG33991.1,
RC   ECO:0000313|Proteomes:UP000193834};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FXAZ01000002; SMG33991.1; -; Genomic_DNA.
DR   STRING; 1852522.SAMN06295960_1923; -.
DR   Proteomes; UP000193834; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0008252; F:nucleotidase activity; IEA:UniProt.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0009166; P:nucleotide catabolic process; IEA:InterPro.
DR   Gene3D; 2.60.40.1080; -; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   Gene3D; 3.90.780.10; 5'-Nucleotidase, C-terminal domain; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 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; IPR003343; Big_2.
DR   InterPro; IPR015919; Cadherin-like_sf.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR011045; N2O_reductase_N.
DR   InterPro; IPR001119; SLH_dom.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   NCBIfam; NF038117; choice_anch_I; 1.
DR   PANTHER; PTHR11575:SF24; 5'-NUCLEOTIDASE; 1.
DR   PANTHER; PTHR11575; 5'-NUCLEOTIDASE-RELATED; 1.
DR   Pfam; PF02872; 5_nucleotid_C; 1.
DR   Pfam; PF02368; Big_2; 1.
DR   Pfam; PF05345; He_PIG; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   Pfam; PF00395; SLH; 3.
DR   PRINTS; PR01607; APYRASEFAMLY.
DR   SMART; SM00635; BID_2; 1.
DR   SUPFAM; SSF75011; 3-carboxy-cis,cis-mucoante lactonizing enzyme; 1.
DR   SUPFAM; SSF55816; 5'-nucleotidase (syn. UDP-sugar hydrolase), C-terminal domain; 1.
DR   SUPFAM; SSF49313; Cadherin-like; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR   SUPFAM; SSF50974; Nitrous oxide reductase, N-terminal domain; 1.
DR   PROSITE; PS00785; 5_NUCLEOTIDASE_1; 1.
DR   PROSITE; PS51272; SLH; 3.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000193834}.
FT   DOMAIN          1499..1558
FT                   /note="SLH"
FT                   /evidence="ECO:0000259|PROSITE:PS51272"
FT   DOMAIN          1559..1622
FT                   /note="SLH"
FT                   /evidence="ECO:0000259|PROSITE:PS51272"
FT   DOMAIN          1625..1685
FT                   /note="SLH"
FT                   /evidence="ECO:0000259|PROSITE:PS51272"
FT   REGION          1241..1280
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1253..1280
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1685 AA;  180023 MW;  8B9E262117D59D01 CRC64;
     MNQRGKQVLA LLLAVEMAAA VLFSGGAIYA AEEKSVSFDN AAEQSVQADT AAAELGISTL
     ALPNATAGAP YSVTMAVYGG QAPYAYAAAG LPAGLSIHSS TGEITGMPEQ ASEKAYDVEL
     IVQDAAEPAH TAKAHVQLKV NRQSTQPLED KIKVEEIAHY AVGASSKDGG VAEIVKYNKD
     NGKFYLVNGS STPASLDVVT LQASGELQRE KQIRIEELVN DSSFTYGDLT SVDVNTAADR
     IAAAVQEADP AKPGKIVVLD YEGNLIHTYE SGVQPDMVTF TSDGRYILSA DEGEPRADVD
     PEGSVTIVDT LTNEVAKIRF DQPERIDDNV HVRGLPNADG QIMGKGSKSD AVHDLEPEFI
     SLSKDEKTAY VALQENNAIA VIDIATKTVT GVHGLGYKSF NEAGNELDLI KDGKIQFENV
     PFYGMYMPDG IAAYEVNGQT YLLSANEGDA TGWSDRTNES KIKDMKAMLA QDSEAAIFLA
     DKGTVYDKVE VASDMGADGL YLYGARSFSI LKAQDMSLVY DSGSDFEKIT AERLPEVFNT
     SNDKKELDSR SAKKGPEPEY VTVGQVGDKT LAFIGLERIG GVMTYDVTNP MEPVFLNYIN
     TRDFDAGIAS DSAPEGLEFI GAEDSPTGRP LLLVANEVSG TVAVLELKVS KVTLDRSTLE
     LRTGSDPVQL HADVEPATGT GVGVKWTSSN PAAASVDQQG RVFPHAAGEA IITAGSEDGY
     GAAQVRVTVV SGSGEEPWKL TVMHTNDTHA HLGDVARRAT LVNQVRSEGG NQLLLDAGDV
     FSGDLYFTKW MGLADLAFMN MMGYDAMTFG NHEFDQGTQV LAAFISKAKF PMVSSNIDLS
     KDRYLSKLIK EPTAFQSNAP KTVEQAGVYP YITVELDGRK VGVFGLTTED TAETSSPGKD
     VAFHDAIEAA RQTVNAMEKE GLDIIIGVTH IGYARDKQLA EAVEGIDLLV GGHTHTTLNA
     PEIVVDPQYQ TPTVIVQANE WGKYLGRVDL AFNSQGVVMI EEINGKLIPV DSKVEENPEA
     KAVLDPYKAE LQEMMNEVVG SSSVQLDGER KNVRSKETNL GNLIADGMLA KAKELKQADI
     ALMNGGGIRA SIDQGEITMG ELRTVMPFGN TLFVLDMTGK QLKEGLENGI SGAKLDDLPG
     KFPQVAGMTF KWDPKQPIGE RVHDVRIKKG SGYVPLDLAA TYRVATNSFV AKGGDGYRSF
     AEAIEQGRYN EDLGYPDYEI FIEHIARLGG IVSPTVDGRI KEQAKPQPGG GDDNGNGSGS
     GSGGGTGTAP TDSESSPANV LTSKQWQLAS VKNEAGRVVH QITVLDEVLK KAAASLHAKQ
     QEIVIRAEKL DGRVEVMLPA AIVASAAEKI KGATLVIETK LASYQLPIEA LPLAKLKQDG
     RLEQAKLLLS MDKASAQVMD KLRAEVQSSG VKLVGGHAAA FALSIVLDKN TQEIKDFERQ
     YVSRIIPLPE GVASSPITAV KVNEETGRFH FVPAVHTTLN GNPAMLIKHT GNGVFALIQH
     RASFTDLNGH WAKAEVELLA SKWLVKGKSS GVFAPNEAIT RGEYTALLIR ALGLAPAADA
     AAFADVDAQH PYAGEIAAAE RLGILEGATG TRFRPEASMT RAEMAVMTAR ALQAAAAEAK
     AKADLDSFKD ASTVPAWAVD AMSQLVELGI LEGDQKGRLT PNNSVTRAQS ALVMSRMLKE
     LKFID
//
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