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Database: UniProt
Entry: H6N4P1_GORPV
LinkDB: H6N4P1_GORPV
Original site: H6N4P1_GORPV 
ID   H6N4P1_GORPV            Unreviewed;       673 AA.
AC   H6N4P1;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   SubName: Full=HAD-superfamily hydrolase, subfamily IIA {ECO:0000313|EMBL:AFA73623.1};
GN   OrderedLocusNames=GPOL_c25970 {ECO:0000313|EMBL:AFA73623.1};
OS   Gordonia polyisoprenivorans (strain DSM 44266 / VH2).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC   Gordonia.
OX   NCBI_TaxID=1112204 {ECO:0000313|EMBL:AFA73623.1, ECO:0000313|Proteomes:UP000009154};
RN   [1] {ECO:0000313|EMBL:AFA73623.1, ECO:0000313|Proteomes:UP000009154}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44266 / VH2 {ECO:0000313|Proteomes:UP000009154};
RX   PubMed=22327575; DOI=10.1128/AEM.07969-11;
RA   Hiessl S., Schuldes J., Thurmer A., Halbsguth T., Broker D., Angelov A.,
RA   Liebl W., Daniel R., Steinbuchel A.;
RT   "Involvement of two latex-clearing proteins during rubber degradation and
RT   insights into the subsequent degradation pathway revealed by the genome
RT   sequence of Gordonia polyisoprenivorans strain VH2.";
RL   Appl. Environ. Microbiol. 78:2874-2887(2012).
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DR   EMBL; CP003119; AFA73623.1; -; Genomic_DNA.
DR   RefSeq; WP_014360205.1; NC_016906.1.
DR   AlphaFoldDB; H6N4P1; -.
DR   STRING; 1112204.GPOL_c25970; -.
DR   KEGG; gpo:GPOL_c25970; -.
DR   eggNOG; COG0457; Bacteria.
DR   eggNOG; COG0647; Bacteria.
DR   HOGENOM; CLU_024300_0_0_11; -.
DR   Proteomes; UP000009154; Chromosome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.300.290; -; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 2.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   InterPro; IPR041065; GNAT-like.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006357; HAD-SF_hydro_IIA.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   NCBIfam; TIGR01460; HAD-SF-IIA; 1.
DR   PANTHER; PTHR19288; 4-NITROPHENYLPHOSPHATASE-RELATED; 1.
DR   PANTHER; PTHR19288:SF96; D-GLYCEROL 3-PHOSPHATE PHOSPHATASE; 1.
DR   Pfam; PF18407; GNAT_like; 1.
DR   Pfam; PF13344; Hydrolase_6; 1.
DR   Pfam; PF13242; Hydrolase_like; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:AFA73623.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009154}.
FT   DOMAIN          605..670
FT                   /note="GCN5-related N-acetyltransferase-like"
FT                   /evidence="ECO:0000259|Pfam:PF18407"
FT   REGION          1..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          258..337
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..32
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        289..312
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   673 AA;  71185 MW;  4F55C6A1C9788CE1 CRC64;
     MNDRDRTRGR RQRPDRADQS GRPHREGRQR TDGPTDPALP EDVVASDLDP DTRRDLLSLE
     KGTAERVARH LVMVAELLYE DADLALEHAR AARRRAARVG VVRETAGVAA YNAGQWQEAI
     SELRAARRIT GSSALLPLIA DAERGLGRPE RAIEIARSEE GRALRDDEAT EMRIVEAGAR
     LDIGEPEKAL VTLQLEDLSP SRTGTAAARL FYAYASALEA AGRLDEATTW FMNASAADTE
     DATDAEFRLM EISVGSAEPD VDPAHEDQQD SGAAIAETEP ASEPEPAPRS ESLGSTESQP
     GSVRQASVAE PESEQGSEIA VAPARETEPV PPPPAPARVV DAYDALLLDL DGTVFAGKSP
     IPGVPETLER IDVTTIFVTN NASRRPDAVA EHLRSMGFTA TPEQVVTSAQ SAARLLSEHL
     EPGSRALVLG TDGLAQEVRE VGIAVTRSAD DRPLAVIQGF SPETSWESLS EAALAIRAGA
     LWVATNVDAT LPSERGLLVG NGSLVAAVAN ATGQEPLVAG KPAAPLMADA INRSGADTPL
     VVGDRLDTDI QGAHSVGLDS LLVLSGVSTA TDLLAAPPQQ RPTFVCADLS GVLDPADSLR
     IADNDDWRIE QTGDTLTVSP VTEPPATLRL LPSLAARVWA LADADEIDLT EITITADDPT
     TRSALEDLGL GAE
//
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