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Database: UniProt
Entry: I4LWJ5_GARVA
LinkDB: I4LWJ5_GARVA
Original site: I4LWJ5_GARVA 
ID   I4LWJ5_GARVA            Unreviewed;       404 AA.
AC   I4LWJ5;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=MutT1 protein {ECO:0000313|EMBL:EIK81335.1};
GN   ORFNames=CGSMWGv55152_00670 {ECO:0000313|EMBL:EIK81335.1};
OS   Gardnerella vaginalis 55152.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Gardnerella.
OX   NCBI_TaxID=698955 {ECO:0000313|EMBL:EIK81335.1, ECO:0000313|Proteomes:UP000005936};
RN   [1] {ECO:0000313|EMBL:EIK81335.1, ECO:0000313|Proteomes:UP000005936}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=55152 {ECO:0000313|EMBL:EIK81335.1,
RC   ECO:0000313|Proteomes:UP000005936};
RX   PubMed=22609915; DOI=10.1128/JB.00056-12;
RA   Ahmed A., Earl J., Retchless A., Hillier S., Rabe L., Cherpes T.,
RA   Powell E., Janto B., Eutsey R., Hiller N.L., Boissy R., Dahlgreen M.,
RA   Hall B., Costerton J., Post J.C., Hu F., Ehrlich G.;
RT   "Comparative Genomic Analyses of 17 Clinical Isolates of Gardnerella
RT   vaginalis Provide Evidence of Multiple Genetically Isolated Clades
RT   Consistent with Subspeciation into Genovars.";
RL   J. Bacteriol. 194:3922-3937(2012).
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:EIK81335.1}.
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DR   EMBL; ADEQ01000002; EIK81335.1; -; Genomic_DNA.
DR   AlphaFoldDB; I4LWJ5; -.
DR   PATRIC; fig|698955.3.peg.128; -.
DR   Proteomes; UP000005936; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   CDD; cd03673; Ap6A_hydrolase; 1.
DR   CDD; cd07067; HP_PGM_like; 1.
DR   Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
DR   Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR   InterPro; IPR013078; His_Pase_superF_clade-1.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR   InterPro; IPR020084; NUDIX_hydrolase_CS.
DR   InterPro; IPR000086; NUDIX_hydrolase_dom.
DR   PANTHER; PTHR21340; DIADENOSINE 5,5-P1,P4-TETRAPHOSPHATE PYROPHOSPHOHYDROLASE MUTT; 1.
DR   PANTHER; PTHR21340:SF8; NUDIX HYDROLASE; 1.
DR   Pfam; PF00300; His_Phos_1; 1.
DR   Pfam; PF00293; NUDIX; 1.
DR   SMART; SM00855; PGAM; 1.
DR   SUPFAM; SSF55811; Nudix; 1.
DR   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR   PROSITE; PS51462; NUDIX; 1.
DR   PROSITE; PS00893; NUDIX_BOX; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT   DOMAIN          9..192
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000259|PROSITE:PS51462"
FT   REGION          309..328
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   404 AA;  45549 MW;  6D14655BE3F35911 CRC64;
     MNMSVVTTRY VEAAGGIIYR KRNTIDSSNT SDLKKTSNQA SMISDDDFEL CLVYRPKYDD
     WSWPKGKNED NESHRHTAVR EVGEETGYAV TLGPHIAQIE YPLENEGKKS ISKSGAKNSS
     QNNNKTEVVK RIHYWMMREI DENSAMRRLP AFGPIKPAKP TEIGNVIWLT PSKARKKLTH
     DSDRKVLDAF LEKLHACQTE YKTLILVRHG KAESRKSWQG SEATRPITPL GSAASYALGR
     ELACYAPNRI VSSPWKRCVE TVATFAHDSS LPIEQIAELT EDHHENKPKS TLSVLISEIQ
     NLDCNVKNTQ NTQNTQNTQN TQNTQNTQNA EENINNSTVM CLHRPIIGTF FDYLRGITKP
     RAHKRILSQK SPYMPTGSAI VLHISNTSKG ARIIDIEKVL PIVY
//
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