ID A0A067QJC1_ZOONE Unreviewed; 472 AA.
AC A0A067QJC1;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Sedoheptulokinase {ECO:0000313|EMBL:KDR08845.1};
GN ORFNames=L798_01331 {ECO:0000313|EMBL:KDR08845.1};
OS Zootermopsis nevadensis (Dampwood termite).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Polyneoptera; Dictyoptera; Blattodea; Blattoidea; Termitoidae;
OC Termopsidae; Zootermopsis.
OX NCBI_TaxID=136037 {ECO:0000313|EMBL:KDR08845.1, ECO:0000313|Proteomes:UP000027135};
RN [1] {ECO:0000313|EMBL:KDR08845.1, ECO:0000313|Proteomes:UP000027135}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Whole organism {ECO:0000313|EMBL:KDR08845.1};
RX PubMed=24845553; DOI=10.1038/ncomms4636;
RA Terrapon N., Li C., Robertson H.M., Ji L., Meng X., Booth W., Chen Z.,
RA Childers C.P., Glastad K.M., Gokhale K., Gowin J., Gronenberg W.,
RA Hermansen R.A., Hu H., Hunt B.G., Huylmans A.K., Khalil S.M.,
RA Mitchell R.D., Munoz-Torres M.C., Mustard J.A., Pan H., Reese J.T.,
RA Scharf M.E., Sun F., Vogel H., Xiao J., Yang W., Yang Z., Yang Z., Zhou J.,
RA Zhu J., Brent C.S., Elsik C.G., Goodisman M.A., Liberles D.A., Roe R.M.,
RA Vargo E.L., Vilcinskas A., Wang J., Bornberg-Bauer E., Korb J., Zhang G.,
RA Liebig J.;
RT "Molecular traces of alternative social organization in a termite genome.";
RL Nat. Commun. 5:3636-3636(2014).
CC -!- SIMILARITY: Belongs to the FGGY kinase family.
CC {ECO:0000256|ARBA:ARBA00009156}.
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DR EMBL; KK853292; KDR08845.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A067QJC1; -.
DR STRING; 136037.A0A067QJC1; -.
DR EnsemblMetazoa; KDR08845; KDR08845; L798_01331.
DR eggNOG; KOG2517; Eukaryota.
DR InParanoid; A0A067QJC1; -.
DR OMA; TWQDTRC; -.
DR OrthoDB; 70798at2759; -.
DR Proteomes; UP000027135; Unassembled WGS sequence.
DR GO; GO:0050277; F:sedoheptulokinase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd07777; FGGY_SHK_like; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR018484; FGGY_N.
DR InterPro; IPR042027; SHK.
DR PANTHER; PTHR10196:SF67; SEDOHEPTULOKINASE; 1.
DR PANTHER; PTHR10196; SUGAR KINASE; 1.
DR Pfam; PF00370; FGGY_N; 1.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000313|EMBL:KDR08845.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000027135};
KW Transferase {ECO:0000313|EMBL:KDR08845.1}.
FT DOMAIN 8..264
FT /note="Carbohydrate kinase FGGY N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00370"
FT REGION 33..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 472 AA; 51423 MW; DA3615481D5AC8DE CRC64;
MAAGEGNLIL GIDIGTTSVK VCLVDPNNKQ VLSKQTKDTQ ANVPSDLGSE GNKQDVPKII
SALNSCVSRL PKDQLKQVGR IGICGQMHGV MLWSNKEDKK AWDCIETYMG CRFEIPKENV
SALYTWQDTR CERSFLDTLP VPQCHLPTYS GYGCATLFWI TRNRPDKLER YNRAGTVQDF
AVAMLCNLDH PIMSVQNAAG WGYFNTCVAE WNSDILQGAS FPTHLLPHIV KSGAIAGTLD
RPWYGIPSGT SVGAALGDLQ CSVLATMQKP DDAVLNISTS AQLAYVMPPQ FEPNIQCPVV
TPVEYFPYFD QKYLAVAASL NGGNALAAFV CMLQHWTHEL GFNVTQSKIW DTVLSLGGQD
CAVSSLRVVP TLLGERHVPE QNASILNVDP GTLGLGQVFQ AVCSGLIENL YGMMPRQMLV
ASNIERIIGI GSALTRNKVL QKQVQEWYKL PVDFMSGGDA AMGAALAVVE CQ
//
