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Database: UniProt
Entry: E6W1K2_DESIS
LinkDB: E6W1K2_DESIS
Original site: E6W1K2_DESIS 
ID   E6W1K2_DESIS            Unreviewed;       792 AA.
AC   E6W1K2;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=Metal dependent phosphohydrolase {ECO:0000313|EMBL:ADU66551.1};
GN   OrderedLocusNames=Selin_1824 {ECO:0000313|EMBL:ADU66551.1};
OS   Desulfurispirillum indicum (strain ATCC BAA-1389 / DSM 22839 / S5).
OC   Bacteria; Chrysiogenota; Chrysiogenetes; Chrysiogenales; Chrysiogenaceae;
OC   Desulfurispirillum.
OX   NCBI_TaxID=653733 {ECO:0000313|EMBL:ADU66551.1, ECO:0000313|Proteomes:UP000002572};
RN   [1] {ECO:0000313|EMBL:ADU66551.1, ECO:0000313|Proteomes:UP000002572}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1389 / DSM 22839 / S5
RC   {ECO:0000313|Proteomes:UP000002572};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Chertkov O., Held B., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Mikhailova N., Haggblom M., Rauschenbach I.,
RA   Bini E., Woyke T.;
RT   "Complete sequence of Desulfurispirillum indicum S5.";
RL   Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP002432; ADU66551.1; -; Genomic_DNA.
DR   RefSeq; WP_013506431.1; NC_014836.1.
DR   AlphaFoldDB; E6W1K2; -.
DR   STRING; 653733.Selin_1824; -.
DR   KEGG; din:Selin_1824; -.
DR   eggNOG; COG1480; Bacteria.
DR   HOGENOM; CLU_015767_1_2_0; -.
DR   InParanoid; E6W1K2; -.
DR   OrthoDB; 9806952at2; -.
DR   Proteomes; UP000002572; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   CDD; cd00077; HDc; 1.
DR   Gene3D; 1.10.3210.10; Hypothetical protein af1432; 1.
DR   InterPro; IPR003607; HD/PDEase_dom.
DR   InterPro; IPR006674; HD_domain.
DR   InterPro; IPR006675; HDIG_dom.
DR   InterPro; IPR011624; Metal-dep_PHydrolase_7TM_extra.
DR   InterPro; IPR011621; Metal-dep_PHydrolase_7TM_intra.
DR   NCBIfam; TIGR00277; HDIG; 1.
DR   PANTHER; PTHR36442; CYCLIC-DI-AMP PHOSPHODIESTERASE PGPH; 1.
DR   PANTHER; PTHR36442:SF1; CYCLIC-DI-AMP PHOSPHODIESTERASE PGPH; 1.
DR   Pfam; PF07698; 7TM-7TMR_HD; 1.
DR   Pfam; PF07697; 7TMR-HDED; 1.
DR   Pfam; PF01966; HD; 1.
DR   SMART; SM00471; HDc; 1.
DR   SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR   PROSITE; PS51831; HD; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:ADU66551.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002572};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        21..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        288..305
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        325..347
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        359..377
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        384..409
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        429..448
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        455..482
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          515..656
FT                   /note="HD"
FT                   /evidence="ECO:0000259|PROSITE:PS51831"
FT   REGION          720..792
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        720..739
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   792 AA;  88588 MW;  C577CE1FFE025C8B CRC64;
     MSNLIGRWHQ YFLAHTINQP LGVKVIAMVT VVLVAFFAIP EERFTGDIYE VGDIASRNIK
     SDRELLVIDE AATIQKRREA HEHAGLLFDH DRSVERSFVI AIEETFQAAR RAASAPEGSG
     EVKELEAMLG RFHLQPEVLA HFQERQFSEA LEQRIKQCVG TAYGQGVYLP GSRSHVFDNA
     FVRDISTGGV QRIVPERPPR TPSEVAAVID QHCQESAVVM FTMANLSPDI TFNERATITR
     REELSQQVKP VYIVVRQGEM IVREGEIVDA MTRQKLNTLL RVKSPLEHWF SFMATLIMAS
     ILILIPWKYF EKARKKIFNS SDRLYIFFTI LLGSIALVKL FSIIAAGLSF NLPYVSYDYL
     IYAVPIAAGA MLVAILLDLH IAMIYTTVFS IICGVMVGHD ISFALYTFVS GLVAAYSSFS
     FRNRMDLTFA ALWSSAAGAL VMVSILLFNG DLFSWGALWA FAFVFISGQI SMLLVMGLLP
     IFESGFHVTS DLRLLELSNM GHPLLKQLIL RAPGTYHHSI IVGSLVEAAA EEIGVNPLLA
     RVGAYYHDIG KMKKPEYFIE NQRGINRHDT LSPAMSSLVI TNHVKHGMEL AEEYSLPKSI
     REIIQQHHGR TLIQYFYKKA LEGGEKVDDE KFRYAGPKPQ TRAAALVMLG DSCEAATRAL
     SEPSHTRIQN LVQKIINNIF VDGQLDECEL TLKDIGMIAA SFTKTLTGIY HQRIEYPEDK
     KEVQVPKEKP EKAPDAELDT RSRPGSGNPP IPTKKVPASI RHFTHQDVDI PGTPEADAKD
     KGEKNGSNPQ YF
//
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