ID R7WM12_9NOCA Unreviewed; 609 AA.
AC R7WM12;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Putative glycerone kinase {ECO:0000313|EMBL:EOM75069.1};
GN ORFNames=Rrhod_3598 {ECO:0000313|EMBL:EOM75069.1};
OS Rhodococcus rhodnii LMG 5362.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1273125 {ECO:0000313|EMBL:EOM75069.1, ECO:0000313|Proteomes:UP000013525};
RN [1] {ECO:0000313|EMBL:EOM75069.1, ECO:0000313|Proteomes:UP000013525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 5362 {ECO:0000313|EMBL:EOM75069.1,
RC ECO:0000313|Proteomes:UP000013525};
RX PubMed=23788540;
RA Pachebat J.A., van Keulen G., Whitten M.M., Girdwood S., Del Sol R.,
RA Dyson P.J., Facey P.D.;
RT "Draft Genome Sequence of Rhodococcus rhodnii Strain LMG5362, a Symbiont of
RT Rhodnius prolixus (Hemiptera, Reduviidae, Triatominae), the Principle
RT Vector of Trypanosoma cruzi.";
RL Genome Announc. 1:e00329-13(2013).
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:EOM75069.1}.
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DR EMBL; APMY01000108; EOM75069.1; -; Genomic_DNA.
DR RefSeq; WP_010839626.1; NZ_APMY01000108.1.
DR AlphaFoldDB; R7WM12; -.
DR PATRIC; fig|1273125.3.peg.3427; -.
DR eggNOG; COG1461; Bacteria.
DR OrthoDB; 9760324at2; -.
DR Proteomes; UP000013525; Unassembled WGS sequence.
DR GO; GO:0004371; F:glycerone kinase activity; IEA:InterPro.
DR GO; GO:0006071; P:glycerol metabolic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.340; -; 1.
DR InterPro; IPR004007; DhaL_dom.
DR InterPro; IPR036117; DhaL_dom_sf.
DR InterPro; IPR033470; FakA-like_C.
DR InterPro; IPR048394; FakA-like_M.
DR InterPro; IPR019986; YloV-like.
DR NCBIfam; TIGR03599; YloV; 1.
DR PANTHER; PTHR33434; DEGV DOMAIN-CONTAINING PROTEIN DR_1986-RELATED; 1.
DR PANTHER; PTHR33434:SF4; PHOSPHATASE PROTEIN-RELATED; 1.
DR Pfam; PF02734; Dak2; 1.
DR Pfam; PF13684; FakA-like_C; 1.
DR Pfam; PF21645; FakA-like_M; 1.
DR SMART; SM01121; Dak1_2; 1.
DR SMART; SM01120; Dak2; 1.
DR SUPFAM; SSF101473; DhaL-like; 1.
DR PROSITE; PS51480; DHAL; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:EOM75069.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000013525};
KW Transferase {ECO:0000313|EMBL:EOM75069.1}.
FT DOMAIN 48..251
FT /note="DhaL"
FT /evidence="ECO:0000259|PROSITE:PS51480"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..285
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..385
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 609 AA; 61749 MW; 3D39FC7C266FBFDA CRC64;
MTTESETAAD AAAPRDSGKA VAAVSSNRTG ISAAPTAETG TAADASGLVL LDWARAAVAA
LDDRRAAIDE INVFPIPDGD TGTNLLFTMR SALAAAENAA RAGRPGVHRI AVALAHGAVA
GGRGNSGVIL SQILRGLAEA TAGSGSSSAD AESRVLDTAV LAAAVQAASN LVADAVSRPV
EGTIVTVLRV VADHAARLPH STGLVDAASA IAGVAADALD RTSGQLDVLR ERGVVDAGAY
GFVVVLDALV AVLGGEPPRR EIGRAPAAAP GRHDHEHHAH HDPGPGGPDF EVMYLVGESD
ADRISALRVT LDALGDSVVV VGDGAGSWSV HVHCADAGGA VEAGLAAGVV SRVRISSFLV
DERRGRHGAV DRGREQSHDN PDAHRGSPGR PAGRAVLAIA SGDGAAALFE AEGATVLRSD
EPVTRAHLLG AVRSLGRPEV IVLPNGALPP QELVTVGAAA RDSAHEVLLV ATSSMVQGLA
ALAVHDDERG LLDDAYTMSE AASSTRWGSV RIAGERALTY VGPCEPGEAI GLMGHEVVVI
DEDGAAAAIR LVDLAVRTGG ELVTLVVGGG APPGFGDRLR EHIEHRHPGV EVMVYNGGQH
AELLQLGVE
//
