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Database: UniProt
Entry: A0A1U7LPB5_NEOID
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ID   A0A1U7LPB5_NEOID        Unreviewed;       515 AA.
AC   A0A1U7LPB5;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Putative hydroxymethylpyrimidine/phosphomethylpyrimidine kinase 2 isoform A {ECO:0000313|EMBL:OLL24495.1};
DE   SubName: Full=Putative hydroxymethylpyrimidine/phosphomethylpyrimidine kinase 2 isoform B {ECO:0000313|EMBL:OLL24496.1};
GN   ORFNames=NEOLI_004528 {ECO:0000313|EMBL:OLL24495.1};
OS   Neolecta irregularis (strain DAH-3).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Neolectales;
OC   Neolectaceae; Neolecta.
OX   NCBI_TaxID=1198029 {ECO:0000313|EMBL:OLL24495.1, ECO:0000313|Proteomes:UP000186594};
RN   [1] {ECO:0000313|EMBL:OLL24495.1, ECO:0000313|Proteomes:UP000186594}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DAH-3 {ECO:0000313|EMBL:OLL24495.1,
RC   ECO:0000313|Proteomes:UP000186594};
RA   Cisse O., Nguyen A., Hewitt D.A., Jedd G., Stajich J.E.;
RT   "Evolutionary innovation and constraint leading to complex multicellularity
RT   in the Ascomycota.";
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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:OLL24495.1}.
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DR   EMBL; LXFE01000766; OLL24495.1; -; Genomic_DNA.
DR   EMBL; LXFE01000766; OLL24496.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1U7LPB5; -.
DR   STRING; 1198029.A0A1U7LPB5; -.
DR   OMA; FWEMFPY; -.
DR   OrthoDB; 5477821at2759; -.
DR   Proteomes; UP000186594; Unassembled WGS sequence.
DR   GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro.
DR   GO; GO:0050334; F:thiaminase activity; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro.
DR   CDD; cd01169; HMPP_kinase; 1.
DR   CDD; cd19367; TenA_C_ScTHI20-like; 1.
DR   Gene3D; 3.40.1190.20; -; 1.
DR   Gene3D; 1.20.910.10; Heme oxygenase-like; 1.
DR   InterPro; IPR016084; Haem_Oase-like_multi-hlx.
DR   InterPro; IPR004399; HMP/HMP-P_kinase_dom.
DR   InterPro; IPR013749; PM/HMP-P_kinase-1.
DR   InterPro; IPR029056; Ribokinase-like.
DR   InterPro; IPR004305; Thiaminase-2/PQQC.
DR   InterPro; IPR027574; Thiaminase_II.
DR   NCBIfam; TIGR00097; HMP-P_kinase; 1.
DR   NCBIfam; TIGR04306; salvage_TenA; 1.
DR   PANTHER; PTHR20858:SF17; HYDROXYMETHYLPYRIMIDINE_PHOSPHOMETHYLPYRIMIDINE KINASE THI20-RELATED; 1.
DR   PANTHER; PTHR20858; PHOSPHOMETHYLPYRIMIDINE KINASE; 1.
DR   Pfam; PF08543; Phos_pyr_kin; 1.
DR   Pfam; PF03070; TENA_THI-4; 1.
DR   SUPFAM; SSF48613; Heme oxygenase-like; 1.
DR   SUPFAM; SSF53613; Ribokinase-like; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:OLL24495.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186594};
KW   Transferase {ECO:0000313|EMBL:OLL24495.1}.
FT   DOMAIN          17..277
FT                   /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT                   /evidence="ECO:0000259|Pfam:PF08543"
FT   DOMAIN          299..508
FT                   /note="Thiaminase-2/PQQC"
FT                   /evidence="ECO:0000259|Pfam:PF03070"
SQ   SEQUENCE   515 AA;  57091 MW;  B0EE96A1F979CA28 CRC64;
     METSKYLSRV LVIAGSDSSG GAGIQADLKV LTAHGVYGMT AITALTSQNT QEVNGIEVMD
     SQFVRKQIDT CIEDIGIDVL KTGMLASPEI VAEVAAAIDR HKLINTVVDP VMVSTSGSVL
     LSPSAVETYA KLLLPRTLIL TPNRDEARLL LCQTNSNCSD SKDDAMSLAR DIKALGPSYV
     LVKGGQCPYM ENLTDANTIK KKFVIDILYD GSRFWEFKSE FVDSTSTHGT GCSLAAAIAS
     NLALSQPVIQ AVENAIHYVQ AALSEAVSLG KGHGPINHTV SIYRLPFYKG KFYDYLIRHP
     KICNIWTEYV DHSFVRQLAE GTLDKKAFMY YLVQDYMWLR HYARAHSLAG YKASTLSQSA
     SSAAIVLYIE REIVLHKSFF DDFGISENDI NTTPESVESM AYSRYLLDLG LQGDWMGLQV
     GLSPCLLGYG VIAKRLLTDS KIKRENNPYH RWIENYAGQD YERAVRLGQE LLEEHALKQS
     TSRIAELVDI FAHATRLEAA FWQMGLDYVT KLMNT
//
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