ID A0A0A2KT41_PENIT Unreviewed; 612 AA.
AC A0A0A2KT41;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Carbohydrate kinase, FGGY, N-terminal {ECO:0000313|EMBL:KGO70949.1};
GN ORFNames=PITC_066300 {ECO:0000313|EMBL:KGO70949.1};
OS Penicillium italicum (Blue mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO70949.1, ECO:0000313|Proteomes:UP000030104};
RN [1] {ECO:0000313|EMBL:KGO70949.1, ECO:0000313|Proteomes:UP000030104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHI-1 {ECO:0000313|EMBL:KGO70949.1,
RC ECO:0000313|Proteomes:UP000030104};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the FGGY kinase family.
CC {ECO:0000256|ARBA:ARBA00009156}.
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:KGO70949.1}.
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DR EMBL; JQGA01000986; KGO70949.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2KT41; -.
DR STRING; 40296.A0A0A2KT41; -.
DR HOGENOM; CLU_009281_10_1_1; -.
DR OMA; HKAMWHE; -.
DR OrthoDB; 120218at2759; -.
DR PhylomeDB; A0A0A2KT41; -.
DR Proteomes; UP000030104; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd07782; FGGY_YpCarbK_like; 1.
DR Gene3D; 1.20.58.2240; -; 1.
DR Gene3D; 3.30.420.40; -; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR018485; FGGY_C.
DR InterPro; IPR018484; FGGY_N.
DR InterPro; IPR006003; FGGY_RbtK-like.
DR NCBIfam; TIGR01315; 5C_CHO_kinase; 1.
DR PANTHER; PTHR43435:SF4; FGGY CARBOHYDRATE KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43435; RIBULOKINASE; 1.
DR Pfam; PF02782; FGGY_C; 1.
DR Pfam; PF00370; FGGY_N; 1.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
PE 3: Inferred from homology;
KW Kinase {ECO:0000313|EMBL:KGO70949.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030104};
KW Transferase {ECO:0000313|EMBL:KGO70949.1}.
FT DOMAIN 33..204
FT /note="Carbohydrate kinase FGGY N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00370"
FT DOMAIN 330..542
FT /note="Carbohydrate kinase FGGY C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02782"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 612 AA; 66741 MW; 2AB04999CCE62BEF CRC64;
MASLPYHRAS HQSSRKATRD HREDLAVHLD HFIGIDVGTG SARACIIDAK GEIVGLASEN
IGLWQPEHGY YEQSTSDIWH CICVAVQRAI SQHNVNPDTV RGIGFDATCS LSVFSNDTDE
PISITGPNFD SDRNVILWLD HRPVEEAEKI NATNHNLLRY VGGKMSIEME IPKVLWLKNH
MPKELFEKCK FYDLADALTH IATGNEKRSF CSVVCKQGYV PVGVDGSVKG WQEDFLQDIG
LGDLTEDNFK RMGGVDGVNG DYLSAGELVG TLCDKAAAEL GLPVGIAIGS GVIDAYAGWI
GTVGSKVDLD AGQSSADVPR LDRSEAFSRL AAVAGTSTCH LAMSPDPVFV DGVWGPYRDT
ILPGYWMAEG GQSATGELLK HVIETHPAFN QATSIAESSH ANIYEYLNEH LKEMAHSQGA
PCISYLGRHF FFYGDLWGNR SPIADPKMTG SIFGLTSDKS VDGLAIYYYA TLEFIALQTK
QIVETMNKAG HRITSVFMSG SQSQNDILVS LVASACGMPV LIPRYIHAAV CHGAAMLGAK
AASSDSQGKT EDLWDIMDRM SKPGKKVLPT EDKNEKALLG VKYEVFLEQC FKQQKYRGMV
DDAVGDWNSK ST
//
