ID C1D2U9_DEIDV Unreviewed; 1267 AA.
AC C1D2U9;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 2.
DT 24-JAN-2024, entry version 75.
DE SubName: Full=Putative metal dependent phosphohydrolase {ECO:0000313|EMBL:ACO47738.2};
GN OrderedLocusNames=Deide_2p00740 {ECO:0000313|EMBL:ACO47738.2};
OS Deinococcus deserti (strain DSM 17065 / CIP 109153 / LMG 22923 / VCD115).
OG Plasmid pDeide2 {ECO:0000313|Proteomes:UP000002208}.
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=546414 {ECO:0000313|EMBL:ACO47738.2, ECO:0000313|Proteomes:UP000002208};
RN [1] {ECO:0000313|EMBL:ACO47738.2, ECO:0000313|Proteomes:UP000002208}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17065 / CIP 109153 / LMG 22923 / VCD115
RC {ECO:0000313|Proteomes:UP000002208};
RC PLASMID=pDeide2 {ECO:0000313|Proteomes:UP000002208};
RX PubMed=19370165; DOI=10.1371/journal.pgen.1000434;
RA de Groot A., Dulermo R., Ortet P., Blanchard L., Guerin P., Fernandez B.,
RA Vacherie B., Dossat C., Jolivet E., Siguier P., Chandler M., Barakat M.,
RA Dedieu A., Barbe V., Heulin T., Sommer S., Achouak W., Armengaud J.;
RT "Alliance of proteomics and genomics to unravel the specificities of Sahara
RT bacterium Deinococcus deserti.";
RL PLoS Genet. 5:E1000434-E1000434(2009).
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DR EMBL; CP001116; ACO47738.2; -; Genomic_DNA.
DR AlphaFoldDB; C1D2U9; -.
DR KEGG; ddr:Deide_2p00740; -.
DR HOGENOM; CLU_006776_0_0_0; -.
DR OrthoDB; 62858at2; -.
DR Proteomes; UP000002208; Plasmid pDeide2.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd01949; GGDEF; 1.
DR CDD; cd00077; HDc; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR Gene3D; 1.10.3210.10; Hypothetical protein af1432; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 4.
DR InterPro; IPR000160; GGDEF_dom.
DR InterPro; IPR003607; HD/PDEase_dom.
DR InterPro; IPR006674; HD_domain.
DR InterPro; IPR037522; HD_GYP_dom.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR NCBIfam; TIGR00254; GGDEF; 1.
DR PANTHER; PTHR45228; CYCLIC DI-GMP PHOSPHODIESTERASE TM_0186-RELATED; 1.
DR PANTHER; PTHR45228:SF8; TWO-COMPONENT RESPONSE REGULATOR-RELATED; 1.
DR Pfam; PF00990; GGDEF; 1.
DR Pfam; PF13487; HD_5; 1.
DR Pfam; PF13424; TPR_12; 3.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00267; GGDEF; 1.
DR SMART; SM00471; HDc; 1.
DR SMART; SM00028; TPR; 9.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR SUPFAM; SSF48452; TPR-like; 4.
DR PROSITE; PS50887; GGDEF; 1.
DR PROSITE; PS51831; HD; 1.
DR PROSITE; PS51832; HD_GYP; 1.
DR PROSITE; PS50005; TPR; 5.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000313|EMBL:ACO47738.2};
KW Plasmid {ECO:0000313|EMBL:ACO47738.2};
KW Reference proteome {ECO:0000313|Proteomes:UP000002208};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT REPEAT 186..219
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 228..261
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 274..307
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 325..358
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 365..398
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 491..688
FT /note="HD-GYP"
FT /evidence="ECO:0000259|PROSITE:PS51832"
FT DOMAIN 513..637
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 1138..1267
FT /note="GGDEF"
FT /evidence="ECO:0000259|PROSITE:PS50887"
FT COILED 1080..1107
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1267 AA; 139711 MW; E5F88D46009F608D CRC64;
MTTESCSEPG NLTNPLEALA TTSWAEELRL QNAQARDRVK EDPQGAYREA GSLLAQAEKL
GDLASQASAL HTQLLSLLEL GDTEHAQSLA ALAADRYLQS AQTNGYCEVQ LLRAGLALSS
NRSDEALRLC DDIIDASQDE PTTTLAEALL TKAMVLFRQG RHADASSSLQ HSGEVRLLLG
DKAGHAKCLN NIGLIYEADG DFVQALNSFM RCLEFLRTNE MAMDGLLSAC LVNVGKVYRE
LGETDNAVDS LNRGVEIAEQ ARHLDKAGIY VSLAAGHSEL GLIHRERKQF SQALDAFMQA
LHVTQSDGMR RERSTQGGSA LHEEAEVLDN IGQTYALMGE TDQAFKALNQ ALQLSLAADD
TSSQASVLTH LGSLYAASGQ HQQAIPLLRR ALKFADTMAL KRQALEAHEQ LARALMGAGQ
DTEAASHLLV VTELQRDLFR TDNERRLRNL TGQLELEKAR YQADIYRQLN DVSLKARQDA
EKEVQERTAE LERAQLEIVN RLGLAAEYRD DKTGLHTYRV GNITALLAEA LGLPAPKVEL
IRLAARLHDV GKIGIPDTIL LKPGKFTPEE YEVMKHHTII GARVLQGGRT ELMHLAEQIA
LTHHERWDGQ GYPRRLSGQD IPLVGRLVAV ADVWDALTSE RPYKGAWSSE DALAELRAQA
GRQFDPAAVE AFVQLVENGV LEQLDDRLNS QAEHADDAPP LIPGAAGPDL PFEIHNSSFD
NVIPYIDALI KGAWQVRDEG PEALIGPSLQ ALELAHQYGY ASGVGYAQRN LAYAHAAQHQ
YSEAVDLLTK ARMCAEQLPD LVLKRDCAVQ LGRIYAQLLD PERALAYGQL SLEVSRMLHD
QAGEAQALFD LGQVYRTLEG RHEQALESIK GAGSLFDGLT DLKAAASCHA ELAELHFGLG
HYEEAAFEGR RALALAASGG AAAVQVHALT ITARALEALG DWSNAKGLYE AAWDTGEPSE
PRMAAQVAWS RLYAACSLLR HGELEEGERL LEGTLNLAQQ HDLKAVAEQA CREYVRLYKA
RGDAEQALAF QEQAHTLEVE QFRQDNGRRA LALTIGHHSD RVRMESNSFQ SRSMELATTN
VALEQANQEK TALLAALQEQ TKVLQRQSRE DGLTGVYNRR YIEEALATEH SRHRQTHRTL
SLLMIDIDHF KAVNDKFSHP VGDEVLRRIA KLFKATCRAH DLVGRYGGEE FLIILPDTTV
PQAIEVAERI RRLVEEYPWR EIHPKLHVTL SLGVCGRMDV ANHERLLSLV DEKLYEAKHG
GRNRVAS
//
