ID W4BIR2_9BACL Unreviewed; 2086 AA.
AC W4BIR2;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=5'-Nucleotidase domain-containing protein {ECO:0000313|EMBL:ETT43638.1};
GN ORFNames=C169_00225 {ECO:0000313|EMBL:ETT43638.1};
OS Paenibacillus sp. FSL R5-808.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1227076 {ECO:0000313|EMBL:ETT43638.1, ECO:0000313|Proteomes:UP000019053};
RN [1] {ECO:0000313|EMBL:ETT43638.1, ECO:0000313|Proteomes:UP000019053}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL R5-808 {ECO:0000313|EMBL:ETT43638.1,
RC ECO:0000313|Proteomes:UP000019053};
RX PubMed=24422886; DOI=10.1186/1471-2164-15-26;
RA Moreno Switt A.I., Andrus A.D., Ranieri M.L., Orsi R.H., Ivy R.,
RA den Bakker H.C., Martin N.H., Wiedmann M., Boor K.J.;
RT "Genomic comparison of sporeforming bacilli isolated from milk.";
RL BMC Genomics 15:26-26(2014).
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:ETT43638.1}.
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DR EMBL; ASPT01000001; ETT43638.1; -; Genomic_DNA.
DR RefSeq; WP_036636414.1; NZ_ASPT01000001.1.
DR PATRIC; fig|1227076.4.peg.46; -.
DR Proteomes; UP000019053; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal 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 CDD; cd10283; MnuA_DNase1-like; 1.
DR CDD; cd04486; YhcR_OBF_like; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR Gene3D; 3.90.780.10; 5'-Nucleotidase, C-terminal domain; 1.
DR Gene3D; 3.60.10.10; Endonuclease/exonuclease/phosphatase; 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; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR InterPro; IPR001322; Lamin_tail_dom.
DR InterPro; IPR036415; Lamin_tail_dom_sf.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR001119; SLH_dom.
DR PANTHER; PTHR42834; ENDONUCLEASE/EXONUCLEASE/PHOSPHATASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_3G09210); 1.
DR PANTHER; PTHR42834:SF1; ENDONUCLEASE_EXONUCLEASE_PHOSPHATASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_3G09210); 1.
DR Pfam; PF02872; 5_nucleotid_C; 1.
DR Pfam; PF13290; CHB_HEX_C_1; 1.
DR Pfam; PF19580; Exo_endo_phos_3; 1.
DR Pfam; PF00932; LTD; 1.
DR Pfam; PF00149; Metallophos; 1.
DR Pfam; PF00395; SLH; 3.
DR PRINTS; PR01607; APYRASEFAMLY.
DR SUPFAM; SSF55816; 5'-nucleotidase (syn. UDP-sugar hydrolase), C-terminal domain; 1.
DR SUPFAM; SSF56219; DNase I-like; 1.
DR SUPFAM; SSF74853; Lamin A/C globular tail domain; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR PROSITE; PS00785; 5_NUCLEOTIDASE_1; 1.
DR PROSITE; PS51841; LTD; 1.
DR PROSITE; PS51272; SLH; 3.
PE 4: Predicted;
FT DOMAIN 29..155
FT /note="LTD"
FT /evidence="ECO:0000259|PROSITE:PS51841"
FT DOMAIN 1901..1960
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT DOMAIN 1961..2024
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT DOMAIN 2026..2086
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT REGION 1646..1699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1670..1690
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2086 AA; 222104 MW; 2F85FD01BA90A9C0 CRC64;
MHIRLHKYQK HLSMLLAIVM LLSILVPFSP VKVAEAAPHN DQVVISQVYG GGGNSGAQYK
NDFIELFNPT GSPVDLTGWK VRYASAASGA FNGTTSLNGI MEPYTYLLVQ QSGGTTGNAL
PTPDVLGSLN LSGSNGIVDL VNAAGDRIDL IGYGSTAIES ETNPTAVLSN GTAAIRKELT
TGQSDRGLDT DNNAADFIVA TPDPRNSAAP ATPVNPGNGL GLVTANPGPN AWPAGTEITL
SPPTVGASVY ADVYLSGGNG SGFQLINNPI VINEPTRVDA YAAQDGQPDG PVTSFQYDVL
TQKSVTEARS KAKGEHVWTE GIITHIEGRE TYIQDDAAGI VLYDYPLNAG VGDRVSVAGV
MEIYNNLQEI KPHALLPNSV TGTQVGLPQA LPITGADLSP ATGETYEARL VSLEDVTIKS
ENKPGEYTAE QGGHEFIIYS GLSKLKTVKS FSLVTGVVKQ FGSIYELIPL GEDALIEELF
SVMASPGAGP IVTGGKVTLS SPTQGANIYY TLDGSVPTTS STQYSSPIPI DRDTTIKAIV
VSGVDVSKVY EFAYKATQQP RIADIQGETH ASPYNGQTVK DIEGVVTQYG YTFSNGNIKG
FYIQDPKPDS NPNTSDAIFV YSTDPSRPQI GDLVSVTGKV AEFNEGSSSN LTSTQIELQS
LKNLDQGQPL PEPVTLGKGG RPIPAAIIDN DGMTAFEPQE DAIDFYESLE GMRVRLPQPT
IISPYWTSSG TYNIATRVEN HIADVITPAG GLVLKEQGNF NPQRLIIAYG NPGQEVSTGD
TFADDVIGVI GYNSGNFKVI PGKGELPAIN SSPFQQEVST IDVNAEQLRV ATYNIENFYP
GVGSSKINKL AESIVSSIKS PDIIGLVEVQ DNNGEQNNGT TAADLSYDAL IKAIKAAGGP
TYSFTDIDPV NNNDGGAPGA NIRVGFLYNP DRVQLSDSVN NKKGSSTDFV AYDAAKDQLT
YNPGRIDPQN PAFNASRKPL AAQFEFRGEK VIVIANHFNS KSGDQGPFGN TQPPVLSSET
QRHQIAAVVN GFVKSVVTAN PDANVVVLGD LNDFQFTQTA TILKGNELDN LIDTLPLKEQ
YTYTYDGNSQ VLDHILVSKN LTRSTQVDVV HLNADFPASK GRVSDHDPVV AQIDLQGEAA
NGFPLTILHT NDTHANLDTT SSPNNVARRV TAIKEARAHA VNPLLVDAGD VFSGTLYFNQ
YLGLADLEFM NMVQYDAMTF GNHEFDKGSE VLNDFIEHAK FPFVSSNVNF SADAILSQKF
KNEVARDAKD ATIYPAIIME VDGEQVGLIG LTTEDTANIA SPGDVTFDDA VQKAKDTVAM
LKNEGINKIV VLSHLGYDVD VNLAKQVEGI DIIVGGHSHT KLDQAVVDRS DSEPKLIVQT
GEKGQFLGQL EVVFDNEGVL QEWNSRLISV DEKNSKGEYV IQPDTEALAI LNAKYKPGVD
QLKQTEVGTT EVKLNGVRAD VRTKETNLGN LIADGMLNAA QTAGTNAVIA LQNGGGIRDS
IGAGKVTMGD VMTVLPFNND LVTITLTGSE IKEAMENGVS KTPAEDGRFP HIAGMKFIYD
STKPVGSRVL RIEVKGKNGY EPIDMNKSYE VATNAFTAKG GDFYASLEKA YLEGRVNLLY
MPDYEVFSNY VKKVGTITDK TSAVEGRITD LKGAPLPGGP GEPGTGNPGN PGTPGTPGPT
TPPVNPTNPG TTPPAEAGKV KVPVKVENGA AAGSVTGAAM KEALKLPSDG KVTIEVTSAQ
PIESSSITIE NEALRAWLDQ SSAQVLNVVT PYGSYELPKR EINLQALATQ AGSDINSIQL
VIQLAVDSNA LKSAASKGHN GLQAVSYTVT ATSGSGKTIT LDKFQSYVKR SLNVAKTYRS
SEIAVVRVDG TGSGYTPVPF KVNGQRIDIY SQTNSTYLVL LNPVTFQDMG THWSKGDVES
LAANMIVTGR SEQNFVPNAP ITRAEFAALV VRALGLTADA KAVAFQDIAL SDWYAGEIQA
AADAGIITGY LDGNFKPNRD ITREQMALMV YKAMDYAGYH QADAAKAQFA DASSISAWSQ
AAVYELAGLG ILNGDPKLRF NPQSSATRAE SAAVLHRMIQ DLTYVK
//
