ID   C7QDX1_CATAD            Unreviewed;       905 AA.
AC   C7QDX1;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   24-JAN-2024, entry version 65.
DE   SubName: Full=Metal dependent phosphohydrolase {ECO:0000313|EMBL:ACU76559.1};
DE   Flags: Precursor;
GN   OrderedLocusNames=Caci_7735 {ECO:0000313|EMBL:ACU76559.1};
OS   Catenulispora acidiphila (strain DSM 44928 / JCM 14897 / NBRC 102108 / NRRL
OS   B-24433 / ID139908).
OC   Bacteria; Actinomycetota; Actinomycetes; Catenulisporales;
OC   Catenulisporaceae; Catenulispora.
OX   NCBI_TaxID=479433 {ECO:0000313|EMBL:ACU76559.1, ECO:0000313|Proteomes:UP000000851};
RN   [1] {ECO:0000313|EMBL:ACU76559.1, ECO:0000313|Proteomes:UP000000851}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44928 / JCM 14897 / NBRC 102108 / NRRL B-24433 / ID139908
RC   {ECO:0000313|Proteomes:UP000000851};
RX   PubMed=21304647; DOI=10.4056/sigs.17259;
RA   Copeland A., Lapidus A., Glavina Del Rio T., Nolan M., Lucas S., Chen F.,
RA   Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S., Mikhailova N.,
RA   Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K., Chain P.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Chertkov O., Brettin T.,
RA   Detter J.C., Han C., Ali Z., Tindall B.J., Goker M., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Catenulispora acidiphila type strain (ID
RT   139908).";
RL   Stand. Genomic Sci. 1:119-125(2009).
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DR   EMBL; CP001700; ACU76559.1; -; Genomic_DNA.
DR   RefSeq; WP_015796284.1; NC_013131.1.
DR   AlphaFoldDB; C7QDX1; -.
DR   STRING; 479433.Caci_7735; -.
DR   KEGG; cai:Caci_7735; -.
DR   eggNOG; COG2206; Bacteria.
DR   HOGENOM; CLU_320489_0_0_11; -.
DR   InParanoid; C7QDX1; -.
DR   OrthoDB; 9802066at2; -.
DR   Proteomes; UP000000851; 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; IPR037522; HD_GYP_dom.
DR   PANTHER; PTHR43155:SF2; CYCLIC DI-GMP PHOSPHODIESTERASE PA4108; 1.
DR   PANTHER; PTHR43155; CYCLIC DI-GMP PHOSPHODIESTERASE PA4108-RELATED; 1.
DR   Pfam; PF13487; HD_5; 1.
DR   SMART; SM00471; HDc; 1.
DR   SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR   PROSITE; PS51832; HD_GYP; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:ACU76559.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000851};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        30..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        59..83
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        134..159
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        180..200
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          222..417
FT                   /note="HD-GYP"
FT                   /evidence="ECO:0000259|PROSITE:PS51832"
FT   REGION          415..439
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          481..905
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        500..516
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        525..543
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        618..659
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        667..691
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        822..836
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   905 AA;  94607 MW;  CAE7B685638F7E15 CRC64;
     MPFSVRCYIF GLVAAAVTVV ATLPLSRTPL PLLLALCALV IAAERLSRVQ IGTSGWTMSV
     SLVVILITVL VLPPPGAALV GLISSVPLPR QPSWTWTKQT VNSALSSLAP ACGSAVCRLV
     GGHNPGHFLS FPEFLWPAAA AVTTCLVVNA LILAGYVGLA TRNRFVDGLR GDIRRATMPY
     YSSGVLALIF LSLWDDIGWF TAPLVVVPMY IAHWSLSQYA KEGAAHEGTI AALVQAVEIK
     DSYTRGHSER VARGAEMLAE QLKMPQDRLA MLRFAGLLHD IGKLGVPTRL LTSTGGLTEE
     EFKLLCMHPN HGVAVLRDIR FLTEVYEGVL YHHERLDGRG YPTGKSGEEI PEFARIIGVA
     DAFDAMTSTR SYRAARSVEE AVAELRRGAG TQFDPDLVHA FENALALAER TGRPWVPTEL
     APAEPPQGDD TAAAASGPWP LPKRVPGFSF ADHDDPFVPV EWFSDWYPSW LLPDAAAIPG
     QRAPELEPPT AAPDPPAADF DDGWSERMHS AVVRETGPEP DEGWSWDGEP AEDADENENA
     DENDPANTEA LPVGAESHPD LELHPDLEPP TAPDAQTAAD ASAASEPQID LSPKLENPTS
     FSAAREPRAE VLAALEQADT DSATTTRAAI DTDSEPAAHS ATGSATATGS VTAARASAES
     ATDSERAAHF ATGSATGNSS ATATGSVTAA RASAESAAEP ERAAHSATGS ATGIGSVTAD
     RAATESEPAP EPTPEPADAP STRWPVDPGL RGDPRGSMRV RAATPAADPD PRGSRAGDGA
     PALTADFDLR KPSGPCPGAA ISVGAPAEDG DDTVPMPQPK AGDPEAWTPS PEPWVAPEPS
     GEVSKGGDSG DSAESGEADG RPGASAGPSW FARGAGGASL HFFGPGDAVW PPRDPDARDS
     EESPA
//