ID A0A2R7YRX9_9ACTN Unreviewed; 2036 AA.
AC A0A2R7YRX9;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=LTD domain-containing protein {ECO:0000259|PROSITE:PS51841};
GN ORFNames=C7S10_20790 {ECO:0000313|EMBL:PUA79175.1};
OS Nocardioides currus.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=2133958 {ECO:0000313|EMBL:PUA79175.1, ECO:0000313|Proteomes:UP000244867};
RN [1] {ECO:0000313|EMBL:PUA79175.1, ECO:0000313|Proteomes:UP000244867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IB-3 {ECO:0000313|EMBL:PUA79175.1,
RC ECO:0000313|Proteomes:UP000244867};
RA Keele B.F.;
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
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:PUA79175.1}.
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DR EMBL; PYXZ01000012; PUA79175.1; -; Genomic_DNA.
DR OrthoDB; 1016457at2; -.
DR Proteomes; UP000244867; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProt.
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 Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR InterPro; IPR008334; 5'-Nucleotdase_C.
DR InterPro; IPR036907; 5'-Nucleotdase_C_sf.
DR InterPro; IPR006179; 5_nucleotidase/apyrase.
DR InterPro; IPR032109; Big_3_5.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR InterPro; IPR047971; ExeM-like.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR001322; Lamin_tail_dom.
DR InterPro; IPR036415; Lamin_tail_dom_sf.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR NCBIfam; NF033681; ExeM_NucH_DNase; 1.
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; PF16640; Big_3_5; 2.
DR Pfam; PF03372; Exo_endo_phos; 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; SSF56219; DNase I-like; 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 Reference proteome {ECO:0000313|Proteomes:UP000244867}.
FT DOMAIN 77..220
FT /note="LTD"
FT /evidence="ECO:0000259|PROSITE:PS51841"
FT REGION 30..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2036 AA; 209280 MW; 961BC36E818E4092 CRC64;
MPSGHLGLPC GTHIRDRVHA RAIPGSGSLT CLATPRRPSE GSLPVSSLLN SRPDGGSRRR
RGLVAAAAAA LVVSPLAAIT PASAVSPNVV ISEVYGGNGA TAAYGNDFIE LYNPTANDVV
MNNWSVQYKA AAGNGAFQVT TLNGTVKAGK HFLVQQGNAT TGTALPTPDA TGSIAMAAGA
GVVALVSNNT TYPTFGTSTT NVDLAGVTAN GLVDTVGYGT TATTYETSNT ASNLTATTSA
QRTAAVDSDR NAADFSSATP TPENSGPVAP TALEATSPGN KTGQVGSPIT GFTLAATGGT
APYTWSATGL PGGVSVAPNG AVSGTPDATG TFTVTATATD SAATPASDDV SFTFTINAAA
SLIPIAEIQG TGATTPLNGQ QVKTQGVVTA AYPTGGLNGF YIQTPGADTA NASDAVFVYG
GTSGFATYPA VGDSVQVVGE AAEFSGATQI IASNAGVTAV TPSLGEVTPK TQIPGADCAL
PGAACLDGAA LDEAREVVEG ELFKPTAPWT ATDVYDGGPY YSNGSNGSAF RGEIGVVSNS
TKPLVAPTEI IDAQATAAVA ERKKYNDAHR IILDDASSWT YSTTENSDKP FPWFTANHSV
RVGSAITFPK PVIFTFGFNA WRILPQAQVV GDPTGTINFT QTRPAAPQNV GGDLKLATFN
VLNFFPTTGE EFDAGPGSCT FYTDRAGNRI SNNSCTPNGP RGAANEANLA RQRDKIVAAI
NTADADIVSL EELENSVQFG KDRDFAINAL VTALNADAGA GTWAAVPSAP VLPTLAEQDV
IRNGFIYQPA NVALVGESVV LSDESTGTEA FADAREPLAQ AFKKVGDADA DAFAVIVNHF
KSKGSGNPDP NGQGNANDRR VLQANSLVAF ADSFKSQRGI TRVFLAGDFN AYSEEDPIQV
LKAAGYDNLE STSNADEETY NFDGQVGSLD HVLANAAAKA DVNAVDIWDI NGYESVYYEY
ARFNTNVTNL YAPNPFRSSD HSPEIVGINT EPAVPAEEEI QILGINDFHG RILNEDGTNG
TTAGITAGAA VLSGAVKQLR SENPNTVFAA AGDLIGASTF ESFIQKDKPT IDALNEAGLE
VSAVGNHELD AGYNDLVNRV MAPYDAVTNP LGGARWKYIA ANLRKKSDDS HAVDDAWIKD
FGDVQVGFVG AVTEDLPALV SPDGIADIKV TDIVDEVNAS ADQLEADGAD VIVLLIHEGA
ANTTLAAATD PNSAFGQVVN GVDANIDAIV SGHTHLAYNH AVPVPAWVAQ GRAVTTRPVV
SAGQYGTYLN QLKLTVDTAT GDVLAQTQNV LNLKQQTAPF TANYPADPNV TPIVNDAIAK
SNVLGAVELG KIAAPFNRAK LSNGTTENRG GESTLGNLVA EVQRWATQTP EAGGAQIAFM
NPGGLRQDMV GNAGGYPTTL TYKQAAVVQP FANTLVNMKM TGAQIKTALE QQWQRDGAGN
IPTRPFLRLG TSKGFRYTYD PSRTEGDRIT AMWLNGTPIA AGTSYSVTVN SFLGSGGDNF
RVFAQGTQKR DTGKIDLQGM VDYMDEFANT AEGDAPLAPD FTQHSVGVAF PAGAPASYKQ
GDDVTFTLSS LAFSTAPDIK DTSVEVRFGG ALLGEAPVDN TIGTAVFDEY GTSTVTVKVP
NGAPDGRVVL KVTGNNTGTT VDVPITITDN RAPSTVTVPD VSLAYGQAGQ LDITVAPAAT
GSVEVFEGTT SLGTAPLTNS AATFALAAKS LPVGVHTLRV AYPGDSNVKA SSISATVTVT
KATSSTAATV APTELKAGVD TGTISVTVNG ESPTGLVGAV LDGQVIGGAE LVDGKASIAI
GPFAAAGTKA ITVRYYGDAN NAASSADVSV TVVANPVPEK ATPTITATVD PVTLKVKKDS
ATVSVTVTRP GGTATGSVLA LIDNKVVGAG ELAAGKTSIV VGPFDTVGAK AITLKYLGDD
ATKAGEGSTS VTVQKATPKL TVKAPKKLKE DEVLEVSVAA AADGFEVTGQ VTAKVKGTSK
TKTLSGGEVD FRLGKLTKPG TYEVTITFLG SNLAEPVTKT VEVKVKKDKK GKNKKR
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