ID V5FVE3_BYSSN Unreviewed; 1001 AA.
AC V5FVE3;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=pyridoxal kinase {ECO:0000256|ARBA:ARBA00012104};
DE EC=2.7.1.35 {ECO:0000256|ARBA:ARBA00012104};
GN ORFNames=PVAR5_1160 {ECO:0000313|EMBL:GAD92567.1};
OS Byssochlamys spectabilis (strain No. 5 / NBRC 109023) (Paecilomyces
OS variotii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Thermoascaceae; Paecilomyces.
OX NCBI_TaxID=1356009 {ECO:0000313|EMBL:GAD92567.1, ECO:0000313|Proteomes:UP000018001};
RN [1] {ECO:0000313|Proteomes:UP000018001}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=No. 5 / NBRC 109023 {ECO:0000313|Proteomes:UP000018001};
RX PubMed=24407650; DOI=10.1128/genomeA.01162-13;
RA Oka T., Ekino K., Fukuda K., Nomura Y.;
RT "Draft genome sequence of the formaldehyde-resistant fungus Byssochlamys
RT spectabilis No. 5 (anamorph Paecilomyces variotii No. 5) (NBRC109023).";
RL Genome Announc. 2:E0116213-E0116213(2014).
CC -!- SIMILARITY: Belongs to the pyridoxine kinase family.
CC {ECO:0000256|ARBA:ARBA00008805}.
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:GAD92567.1}.
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DR EMBL; BAUL01000029; GAD92567.1; -; Genomic_DNA.
DR AlphaFoldDB; V5FVE3; -.
DR eggNOG; KOG2599; Eukaryota.
DR HOGENOM; CLU_299558_0_0_1; -.
DR InParanoid; V5FVE3; -.
DR OrthoDB; 5472295at2759; -.
DR Proteomes; UP000018001; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0008478; F:pyridoxal kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR GO; GO:0009443; P:pyridoxal 5'-phosphate salvage; IEA:InterPro.
DR CDD; cd12148; fungal_TF_MHR; 1.
DR CDD; cd01173; pyridoxal_pyridoxamine_kinase; 1.
DR Gene3D; 3.40.1190.20; -; 1.
DR InterPro; IPR013749; PM/HMP-P_kinase-1.
DR InterPro; IPR004625; PyrdxlKinase.
DR InterPro; IPR029056; Ribokinase-like.
DR InterPro; IPR007219; Transcription_factor_dom_fun.
DR NCBIfam; TIGR00687; pyridox_kin; 1.
DR PANTHER; PTHR10534; PYRIDOXAL KINASE; 1.
DR PANTHER; PTHR10534:SF2; PYRIDOXAL KINASE; 1.
DR Pfam; PF04082; Fungal_trans; 1.
DR Pfam; PF08543; Phos_pyr_kin; 1.
DR SMART; SM00906; Fungal_trans; 1.
DR SUPFAM; SSF53613; Ribokinase-like; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000018001}.
FT DOMAIN 283..356
FT /note="Transcription factor"
FT /evidence="ECO:0000259|SMART:SM00906"
FT REGION 942..972
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 957..972
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1001 AA; 110836 MW; 747E49001C6B3180 CRC64;
MSDGEEAKGT AAAHPDFQSI IALIEDRLSR IEGLLQDLAA NSNVATLPTR IRADVNSSCT
VQEASLPPVA QPPSEPDMTT ANKTFEGESS FRAHFVHASK LFERAMSVDN LVGRSPEMQE
AISNLRSLVE KQNTLSVHHD LRFPGQKAAP ALDFSSVKMP PMASVVSLLR LCKETMSSNF
LELPFLDYMK FDDMCKKVYF ATEDYSMALF TLVNGGLYYL FSEVCMLRGQ NSAEFKECAA
ICRSNFEYTI GKFDVLTAPT LENIQALCLG AFYSIDISRP SLCWALASNA ARLCQILGYH
RSVATPGDTR SEIELKKKMF WFVYVLDKSL SLRLGRSSTL QDYDITLERP GESSDVGLRA
WDTVYNFWID LARFNGRVYE QLYSARALSD SEADRVQRAK DIIRDMQCWY QGILDTDHKA
VYSPYYFEAT TSACAIVYYS VLTLVYRTIP PDPANHSAIF SNDCIETARA TLRAHYQNSS
RYKESNNYIW NGYISWTLMH CPFTPFLVVF CQAIAVADLS DLKLLGEFVS SLQPVSEVSE
ATEKLYRLCQ VFHRVAELYI DAKIKHNSNV HIHQDASVSG ANTMYPVNDF DPYLSALGFT
SAGGMSSFPH GGISAGEMPS SEYDGMAASG SLGDWFAGNL NIMALLEADL SNINTINIYV
GNTMATFAMQ SLGCEVAALN TVHFSNHTGY KQVKGTKATA QEIRDLYQGL QQSYLTDFDV
LLSGYAPSAA AVEAVGEIGL DLQHKAEKKP GSFFWILDPV MGDQGRIYVN EDVVPAYKKI
IHHADLILPN QFEAELLSGI KITSLHTLAE AITAIHKTYS VPHIIVTSVQ LMTLDHSAST
TAPPSTLTII GSTTKSDGTP RLFRVDVPAL DCFFSGTGDM FAALTVARLR EAVFSADPAL
RHTKSWVSPD SVPATELPLA KATVKVLASM HSVLENTMKA RDEELQRSSA GADEEPIADS
EEARQKREHL RRTKAAEVRL VRNVKFLRDP VAKFEVQAWS E
//