ID A0A0P1B7Z1_9BASI Unreviewed; 1044 AA.
AC A0A0P1B7Z1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=thiamine diphosphokinase {ECO:0000256|ARBA:ARBA00013245};
DE EC=2.7.6.2 {ECO:0000256|ARBA:ARBA00013245};
OS Ceraceosorus bombacis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Ceraceosorales; Ceraceosoraceae; Ceraceosorus.
OX NCBI_TaxID=401625 {ECO:0000313|EMBL:CEH11983.1, ECO:0000313|Proteomes:UP000054845};
RN [1] {ECO:0000313|EMBL:CEH11983.1, ECO:0000313|Proteomes:UP000054845}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Magalhaes I.L.F., Oliveira U., Santos F.R., Vidigal T.H.D.A.,
RA Brescovit A.D., Santos A.J.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CCYA01000089; CEH11983.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P1B7Z1; -.
DR STRING; 401625.A0A0P1B7Z1; -.
DR OrthoDB; 206891at2759; -.
DR Proteomes; UP000054845; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0009378; F:four-way junction helicase activity; IEA:InterPro.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030975; F:thiamine binding; IEA:InterPro.
DR GO; GO:0004788; F:thiamine diphosphokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006271; P:DNA strand elongation involved in DNA replication; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:InterPro.
DR GO; GO:0006772; P:thiamine metabolic process; IEA:InterPro.
DR CDD; cd00009; AAA; 1.
DR CDD; cd18139; HLD_clamp_RarA; 1.
DR CDD; cd07995; TPK; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 1.20.272.10; -; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 1.10.3710.10; DNA polymerase III clamp loader subunits, C-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10240; Thiamin pyrophosphokinase, catalytic domain; 1.
DR Gene3D; 2.60.120.320; Thiamin pyrophosphokinase, thiamin-binding domain; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR032423; AAA_assoc_2.
DR InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR InterPro; IPR021886; MgsA_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR006642; Rad18_UBZ4.
DR InterPro; IPR008824; RuvB-like_N.
DR InterPro; IPR006282; Thi_PPkinase.
DR InterPro; IPR007373; Thiamin_PyroPKinase_B1-bd.
DR InterPro; IPR036371; TPK_B1-bd_sf.
DR InterPro; IPR007371; TPK_catalytic.
DR InterPro; IPR036759; TPK_catalytic_sf.
DR PANTHER; PTHR13779:SF7; ATPASE WRNIP1; 1.
DR PANTHER; PTHR13779; WERNER HELICASE-INTERACTING PROTEIN 1 FAMILY MEMBER; 1.
DR Pfam; PF16193; AAA_assoc_2; 1.
DR Pfam; PF12002; MgsA_C; 1.
DR Pfam; PF05496; RuvB_N; 1.
DR Pfam; PF04265; TPK_B1_binding; 1.
DR Pfam; PF04263; TPK_catalytic; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00734; ZnF_Rad18; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF48019; post-AAA+ oligomerization domain-like; 1.
DR SUPFAM; SSF63999; Thiamin pyrophosphokinase, catalytic domain; 1.
DR SUPFAM; SSF63862; Thiamin pyrophosphokinase, substrate-binding domain; 1.
DR PROSITE; PS51908; ZF_UBZ4; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|PROSITE-
KW ProRule:PRU01256};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|PROSITE-
KW ProRule:PRU01256}; Hydrolase {ECO:0000313|EMBL:CEH11983.1};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000054845};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU01256}.
FT DOMAIN 41..68
FT /note="UBZ4-type"
FT /evidence="ECO:0000259|PROSITE:PS51908"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 75..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 601..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 704..749
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 918..941
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..205
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 704..725
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 924..938
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1044 AA; 113765 MW; 4F30389889D49BB5 CRC64;
MSTLRGKQHD NDDDGSSGGG GGGGDMAQEA ASERLWPNNK LVPCPSCAKS ICASEVNEHL
DTCLSFEAAH PITSASASTS ASTSTSASTS ASTSAKTSQD VFRRMMSSQS TAHPHPHPQH
CTTTTTTTPS RRSSAIASLA HTDASATAKR PRLDSTQHPH ADSASSVEQE QQEQEQEQQR
EACVAAPVRQ RSKTREDADT RPLAEKLRPA SLDDFLGQGT LLHTLKSLHA AGKVPSCILW
GPPGSGKTTL ARILSKSSSQ QQQQQRKNRL VEISATNTGA VELKRILEEA LSRLKLMGQR
TLVFVDEIQR WSRAVQDVLL PSVEKGDIIL LAATTENPSF RLQAALLSRL RVFVLERMTV
EHTRALLRKA RERVVSASGD DHAMPLGARD EMLDWIAVMA DGDARTALNS LELALLMSSQ
DSPTDMDSLK TLLRRSAMQY DRTGDDHYDL ISALHKSIRG SDVDASVFWL VSMIERGEDP
LFIARRMIVA ASEDVNTPEA LNIALNTYQA CQLVGYPECA ENLAQAVVFL AESEKSTRAY
RALQKARTLV RQGTNYPVPV HIRNAPTKLM RSLDYAKDYR YEPSFAHPVH QEYFPSQLKG
TRLVSPPPGR APDAPLSAKG EQSTSTKLAA VSPAKQWTGA HAVSANEGVA QSLRLATSDA
QGPGSCQRVW KIGARAVDLD LLDEWERERN GGMRWHGRDA LEKSLGVERD DSKEAKEDPP
RDSRAANDSA DVATPRRTAG RFRPSAQQWD PSVMLQDPAA SGVARPAYAI ILLNAPIHAD
HRRTFERLWN GANYRVCADG GANRLHEAYR SGGESGETVL DPHAILGDLD SLHAHVRDYF
SSLGVAIHHR ASQYATDLQK CIQHIEDVEA QSRSNAGVPG TTSEGEMQLV IFGGLSGRLD
QTLHTIHTLW LLAPGVSNGR GVEDPDGGES DDAERRRGGG LKKRKRTFVV SENSVAWVLP
QGEHELHLSP TILGKTCGML PIGAGPVGVR IQTEGLEWDL DGSQRSSIGG FLSTSNHVAR
ARVKVQTDGE FCWTVELRKD LERV
//
