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Database: UniProt
Entry: A0A239PCF1_9ACTN
LinkDB: A0A239PCF1_9ACTN
Original site: A0A239PCF1_9ACTN 
ID   A0A239PCF1_9ACTN        Unreviewed;      1041 AA.
AC   A0A239PCF1;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=LTD domain-containing protein {ECO:0000259|PROSITE:PS51841};
GN   ORFNames=SAMN05216276_11143 {ECO:0000313|EMBL:SNT64268.1};
OS   Streptosporangium subroseum.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Streptosporangiaceae; Streptosporangium.
OX   NCBI_TaxID=106412 {ECO:0000313|EMBL:SNT64268.1, ECO:0000313|Proteomes:UP000198282};
RN   [1] {ECO:0000313|EMBL:SNT64268.1, ECO:0000313|Proteomes:UP000198282}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.2132 {ECO:0000313|EMBL:SNT64268.1,
RC   ECO:0000313|Proteomes:UP000198282};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FZOD01000114; SNT64268.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A239PCF1; -.
DR   OrthoDB; 1016457at2; -.
DR   Proteomes; UP000198282; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd12215; ChiC_BD; 2.
DR   CDD; cd10283; MnuA_DNase1-like; 1.
DR   CDD; cd04486; YhcR_OBF_like; 1.
DR   Gene3D; 2.10.10.20; Carbohydrate-binding module superfamily 5/12; 2.
DR   Gene3D; 3.60.10.10; Endonuclease/exonuclease/phosphatase; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR015919; Cadherin-like_sf.
DR   InterPro; IPR003610; CBM_fam5/12.
DR   InterPro; IPR036573; CBM_sf_5/12.
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; IPR006311; TAT_signal.
DR   NCBIfam; NF033681; ExeM_NucH_DNase; 1.
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; PF02839; CBM_5_12; 2.
DR   Pfam; PF03372; Exo_endo_phos; 1.
DR   Pfam; PF05345; He_PIG; 1.
DR   Pfam; PF00932; LTD; 1.
DR   SMART; SM00495; ChtBD3; 2.
DR   SUPFAM; SSF49313; Cadherin-like; 1.
DR   SUPFAM; SSF51055; Carbohydrate binding domain; 2.
DR   SUPFAM; SSF56219; DNase I-like; 1.
DR   PROSITE; PS51841; LTD; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198282};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..1041
FT                   /note="LTD domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012218655"
FT   DOMAIN          28..167
FT                   /note="LTD"
FT                   /evidence="ECO:0000259|PROSITE:PS51841"
FT   REGION          206..238
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        210..238
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1041 AA;  107450 MW;  CB7B90E246897135 CRC64;
     MSAPLFRRVV IAALTLSTAG VACSLFAAPA SANSTGTGLI ISEAYVNGGS SGASYLNKFV
     ELYNPTPNAI SLAGDTLQYR APTSTTVPGG SQVFALSGTV AGHGHLLIQL PSNNASTNPG
     APLPTPDLST GGSVNPGAGG GTLFIAASTS GVLPTDSTVI DKIGWGTSNS PEASAPTGNS
     LTLSYQRDAA GADTDDNAAD FHVAAPNPQN AASDAGNPGD GTGTITVTDP GSQSATSGTA
     ITPLTLHASG GTEPYTWTAT GLPAGLTISS DGTVSGTPTS AGTSSVTVTA TDSTGATGSA
     TFRFQVAGDG STIIPIASIQ GTNTDTSPYK GQTVTTEGVV TAVYATGGFN GFFLETGGAG
     GTKANDKTPG ASDAVFVFGT ESAGQVKIGE SVQVTGEVTE FQGETEIQFP TVTKLATPLA
     AVVPGQIPWS DLATDAAKEE HEGELIAPQG DFTVSDNYDA NFYGSFTLAA GDKPLRQPTD
     AGTAGSAEAK AAAADNAARM VTLDDGSSSN YSTSAARDTP LPWLTATKAV TVGSKVTFHA
     PVILEYRFSL WNFQPRQQVT DDGSAVATFS DLRTGNQRPS AVGGGIRLAT FNVENYFPMT
     GENYVAKGLG SCTYYTDRQG NRIAVNTCTG TDRSSGPRGA ADGANFARQQ AKIVTGVNRL
     DASVVSLEEI ENSVKFGEPR DTALAGLVDA LNAAAGSKVW AYAPSPSADK LPPLSQQDVI
     RTAFIYKPAD VTLAGPSTVL TGDSGPGQPF SIARQPLAQG FKKVGATDKD AFLAVANHLK
     SKGAGTPLYD GDAEDTSSPD VNQGAFNATR VRQAQAVSAF ASQAAAGLGT DRIFLLGDFN
     AYTHEDPMQV LYSDGYTDLG STFDPSESTY SFNGLQGSLD HVLANPAAKA MVTGADVWQI
     NAQESVAYNY SRYNYNAAQL FNGTDPFAAS DHDPVIVGLN LPVTPVAPAW NTSKVYNTGD
     KVTYQGSTWQ ASWWTQNQKP GDPNGPWEQI ETAADGTAVW TPSRVFNTGD VVMYKNKKYK
     AQWWTRNQAP GQPYGPWQPV D
//
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