ID A0A142XB67_9BACT Unreviewed; 816 AA.
AC A0A142XB67;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase {ECO:0000313|EMBL:AMV23994.1};
GN ORFNames=VT84_06335 {ECO:0000313|EMBL:AMV23994.1};
OS Gemmata sp. SH-PL17.
OC Bacteria; Planctomycetota; Planctomycetia; Gemmatales; Gemmataceae;
OC Gemmata.
OX NCBI_TaxID=1630693 {ECO:0000313|EMBL:AMV23994.1, ECO:0000313|Proteomes:UP000076098};
RN [1] {ECO:0000313|EMBL:AMV23994.1, ECO:0000313|Proteomes:UP000076098}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SH-PL17 {ECO:0000313|EMBL:AMV23994.1,
RC ECO:0000313|Proteomes:UP000076098};
RA van der Voort M., Raaijmakers J.M.;
RT "Genome minning of novel planctomycete species.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP011271; AMV23994.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A142XB67; -.
DR STRING; 1630693.VT84_06335; -.
DR KEGG; ges:VT84_06335; -.
DR PATRIC; fig|1630693.3.peg.1335; -.
DR Proteomes; UP000076098; Chromosome.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.50.1460; -; 1.
DR Gene3D; 3.40.50.1580; Nucleoside phosphorylase domain; 1.
DR InterPro; IPR048915; bDLD3.
DR InterPro; IPR029030; Caspase-like_dom_sf.
DR InterPro; IPR000845; Nucleoside_phosphorylase_d.
DR InterPro; IPR035994; Nucleoside_phosphorylase_sf.
DR InterPro; IPR011600; Pept_C14_caspase.
DR PANTHER; PTHR46832; 5'-METHYLTHIOADENOSINE/S-ADENOSYLHOMOCYSTEINE NUCLEOSIDASE; 1.
DR PANTHER; PTHR46832:SF1; 5'-METHYLTHIOADENOSINE_S-ADENOSYLHOMOCYSTEINE NUCLEOSIDASE; 1.
DR Pfam; PF20690; bDLD3; 1.
DR Pfam; PF00656; Peptidase_C14; 1.
DR Pfam; PF01048; PNP_UDP_1; 1.
DR SUPFAM; SSF52129; Caspase-like; 1.
DR SUPFAM; SSF53167; Purine and uridine phosphorylases; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000076098}.
FT DOMAIN 13..282
FT /note="Nucleoside phosphorylase"
FT /evidence="ECO:0000259|Pfam:PF01048"
FT DOMAIN 473..713
FT /note="Peptidase C14 caspase"
FT /evidence="ECO:0000259|Pfam:PF00656"
FT DOMAIN 742..814
FT /note="Bacterial Death-like"
FT /evidence="ECO:0000259|Pfam:PF20690"
FT REGION 432..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..458
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 816 AA; 88724 MW; 6E0B614336213517 CRC64;
MLAASDIRGS VTFGILTVRS DEYTAVLEHF PNRETVKGRV FYEYSQQEAA DGKRVGIAVA
RSLEQGPGAA HDLTRDLIED LDPDWILVVG IAGGLPEDDY SLGDVLLASR IYDFSVSAEI
LDGEQHQREW SLGGGAVHPD VAAVLGAIPG WESKLKGWNK QTTVGMKKPV CEIPHDASSD
RLYGPVDWRS KVQKSLARHF PESRKPRLPN YAVIPVGGGG ILVKDPALIT EWKQSARALG
FVEMEAGGVY RAARRTEREY PVLVVRGLSD IVGFKRAGEW TSYACKTAAS FAGAFVRSGI
VTPKPLKYTQ AQAKSPTVAA GKNDRAEQQG DNRAEHVVFI EFLLRGPIEE FNESNFRQAL
QTTTGLDVSS ARIASIQKRS TLVRLEGDPE VLARIVAQFK ASQDALHAFA TTTGLTLIRW
HVGSQQYELT VQSEGNSPHE AKQVTPQLLS SPSSDQKAHG LPPASGRTAT FAKGRALVIG
VANYPHVNKL PGSVLDDARD VADLLRSSDF CGYPPANVEV LLDAQATLNG IRESLTRLTQ
TSAPDETVVV YFSGHGGRIP SGEFLIPFDC NPRNIANTAL SGAELTTFLS TIKAERLAIL
LDACHSSGTA ELKSLDPAEG VKAGLSDAAY NLLAQGKGRV MMASCRADET SVVLGGMRNS
LFTHHLLDAL RGKASTENVV RVFDVFNYVS DKVPAQEKKQ HPVFKAHNLE TNFPLSLRAG
GKALGGPEAP VPPAPRLIKL SGKAKLTLYA GLVTRWSALA TYLDISLEDR AKFLQGHEPR
QIFEWLEERN RLGELRGAFK DLGWPDLIEE LDRHPQ
//
