ID H6NPI7_9BACL Unreviewed; 1505 AA.
AC H6NPI7;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=LTD domain-containing protein {ECO:0000259|PROSITE:PS51841};
GN ORFNames=PM3016_5940 {ECO:0000313|EMBL:AFC32599.1};
OS Paenibacillus mucilaginosus 3016.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1116391 {ECO:0000313|EMBL:AFC32599.1, ECO:0000313|Proteomes:UP000007523};
RN [1] {ECO:0000313|EMBL:AFC32599.1, ECO:0000313|Proteomes:UP000007523}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3016 {ECO:0000313|EMBL:AFC32599.1,
RC ECO:0000313|Proteomes:UP000007523};
RX PubMed=22535950; DOI=10.1128/JB.00323-12;
RA Ma M., Wang Z., Li L., Jiang X., Guan D., Cao F., Chen H., Wang X.,
RA Shen D., Du B., Li J.;
RT "Complete Genome Sequence of Paenibacillus mucilaginosus 3016, a Bacterium
RT Functional as Microbial Fertilizer.";
RL J. Bacteriol. 194:2777-2778(2012).
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DR EMBL; CP003235; AFC32599.1; -; Genomic_DNA.
DR STRING; 1116391.PM3016_5940; -.
DR KEGG; pmq:PM3016_5940; -.
DR HOGENOM; CLU_248464_0_0_9; -.
DR Proteomes; UP000007523; Chromosome.
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 Gene3D; 2.60.40.1080; -; 1.
DR Gene3D; 2.60.40.2700; -; 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; IPR046780; aBig_2.
DR InterPro; IPR041498; Big_6.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR001322; Lamin_tail_dom.
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; PF20578; aBig_2; 3.
DR Pfam; PF17936; Big_6; 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; SSF56300; Metallo-dependent phosphatases; 1.
DR PROSITE; PS00786; 5_NUCLEOTIDASE_2; 1.
DR PROSITE; PS51841; LTD; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000007523};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1505
FT /note="LTD domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038914525"
FT DOMAIN 1330..1447
FT /note="LTD"
FT /evidence="ECO:0000259|PROSITE:PS51841"
FT REGION 1316..1336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1316..1334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1505 AA; 155294 MW; 0F29F5B8D343E9DA CRC64;
MRSPAFKLAL ALLLSGSTLA PSASYASSDT YRILAASGDT APVQTSVYGG EIGTGTTVQE
AAYGPVSVQL LNINDLHGKV DQTYPVDLDG DKVNESNLGR MDYVAAYLKQ REAGNPNTLI
LHSGDTIGGS SPVTALLQDE PTVEMLESIG FDGGTVGNHE FDEGTAEMLR MIQGGTHPKG
TENYDGMNFP VVAANIEYKA DGSPVLPPYF IREIGGVKIG FIGVVTQSTA SIVMPGGIAD
IRFTDETAAV NKAAAELKAQ GIRSIVVLSH LDAVQSGTGV TGAAADLASS VDDEVDVIFA
AHNHTIVNGT VDNKLIVQAW EYGKAISDVD LQIDPATGDI VQKSAEIVYV NQAGITPDPA
VGTILQKYVD RVAPIINEVV GVTAAEMTGG YGVRGPIGDN ALGNFIADGM RHAMNSDFAL
MNGGGIRDNL NRGDVTWGEL YNIQPFNNQL VKVEVTGADL ETILNAQLSS LYGPDYSIGG
FSYTWNGSTT KVVDIFLPDG SKIDKTKTYT VTVNNFMQTA TSSKYKPIGT LGKNPVYGPE
DLEASVAFTR SFGGTPISYK AEGRIKEVSG VPTDPALLTV AQFRALADGT AGKAQGVITT
TPLGNKSFYM QDSTGGIFVY SPSVTETLAL GDKVSVSGIK KTFNGELEFD SGATVTKIGT
EPVPAPIQIT PAQVGDHQGK LVTLKGVKVS DIRANDFNVT SGGSTVMVYT GAYGVGTTQV
KDGDIIDLTG IAAYYNKNQI KPRSAADIMV TGGLSDAEIT AADHKALTLG DTSAVTLNLT
LPTTGAKGSV ITWSSSNPAV VAADGTVTRP EKGQPAATAV LTATITKGTS TLTKSFSITV
KPKRLTDQEA VANAKAALFL TYDGVSDKLK LITAGADMTT ISWRLTNPEL SRIVDVTTGA
VDRTKVIGGS EKVTLVATIS RGTYSDIDVF TILVRGLPAP AVVNAVYEND TFVTGTAKAG
STVTVRTGDT VLGSAASHAT TGAYQVAIAA QPAGTVLEVI ATATGYTSTP AYVLVLTPVL
NDAGAVAADK NALTDSVILN GNPSLDAVTG ALKLPVSGEN GTTISWQSSQ PSVVSASGTV
TRPSSSSENA VVTLTATISR GGASDTKSFT VTVLKQTAPS GDTLTVLEAK ASPLGTLVKV
RGYLTSKTAA SNSNIVFVLA DQEGVTDFTG NAGAIQIPQT NSYYVDPAAK QTLLDAPIGS
IVIVEGKIDT YNSKPSIEAI RSAALQGAEN TAPTVTNVTY SGVPQVGATL TGVYTYTDAE
NDPEGASVYA WYRSDSADGT GLTAIAGASG KSYTVTEADL GKYLVFEVTP AAASGTSAGQ
PVKSAPTGQV TGQQGPGPVG ADLFFSEYVE GTSNNKAIEI FNPSGTAVNL TGYTVELYAN
GATAPTNKLD LSGTLAAGDV FVIANASANA AILAVADVTS TVTFFNGDDA LVLKKNGVIV
DVIGQVGTDP GTEWGTGVTS TLDNTIRRMP GTTAGDTNAS DAFDPAAQWI GYPVDTLDGL
GQHTN
//
