ID A0A0G4MC31_VERLO Unreviewed; 2714 AA.
AC A0A0G4MC31;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 18-JUN-2025, entry version 39.
DE RecName: Full=DAGKc domain-containing protein {ECO:0000259|PROSITE:PS50146};
GN ORFNames=BN1708_005518 {ECO:0000313|EMBL:CRK31716.1};
OS Verticillium longisporum (Verticillium dahliae var. longisporum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=100787 {ECO:0000313|EMBL:CRK31716.1, ECO:0000313|Proteomes:UP000044602};
RN [1] {ECO:0000313|EMBL:CRK31716.1, ECO:0000313|Proteomes:UP000044602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VL1 {ECO:0000313|EMBL:CRK31716.1};
RA Wang D.B., Wang M.;
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the RRP1 family.
CC {ECO:0000256|ARBA:ARBA00006374}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CVQH01021862; CRK31716.1; -; Genomic_DNA.
DR STRING; 100787.A0A0G4MC31; -.
DR Proteomes; UP000044602; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0030688; C:preribosome, small subunit precursor; IEA:InterPro.
DR GO; GO:0004048; F:anthranilate phosphoribosyltransferase activity; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0016301; F:kinase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0000162; P:L-tryptophan biosynthetic process; IEA:InterPro.
DR GO; GO:0006364; P:rRNA processing; IEA:InterPro.
DR CDD; cd18617; GH43_XynB-like; 1.
DR FunFam; 3.40.1030.10:FF:000010; Anthranilate phosphoribosyltransferase; 1.
DR Gene3D; 1.10.287.1490; -; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.60.200.40; -; 1.
DR Gene3D; 2.115.10.20; Glycosyl hydrolase domain, family 43; 1.
DR Gene3D; 3.40.1030.10; Nucleoside phosphorylase/phosphoribosyltransferase catalytic domain; 1.
DR Gene3D; 3.40.50.10330; Probable inorganic polyphosphate/atp-NAD kinase, domain 1; 1.
DR InterPro; IPR005940; Anthranilate_Pribosyl_Tfrase.
DR InterPro; IPR017438; ATP-NAD_kinase_N.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR InterPro; IPR055916; DUF7493.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR InterPro; IPR000312; Glycosyl_Trfase_fam3.
DR InterPro; IPR017459; Glycosyl_Trfase_fam3_N_dom.
DR InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR InterPro; IPR035902; Nuc_phospho_transferase.
DR InterPro; IPR010301; RRP1.
DR NCBIfam; TIGR01245; trpD; 1.
DR PANTHER; PTHR43285; ANTHRANILATE PHOSPHORIBOSYLTRANSFERASE; 1.
DR PANTHER; PTHR43285:SF2; ANTHRANILATE PHOSPHORIBOSYLTRANSFERASE; 1.
DR Pfam; PF00781; DAGK_cat; 1.
DR Pfam; PF24321; DUF7493; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR Pfam; PF02885; Glycos_trans_3N; 1.
DR Pfam; PF00591; Glycos_transf_3; 1.
DR Pfam; PF05997; Nop52; 2.
DR SMART; SM00046; DAGKc; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
DR SUPFAM; SSF52418; Nucleoside phosphorylase/phosphoribosyltransferase catalytic domain; 1.
DR PROSITE; PS50146; DAGK; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000044602};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1937..2076
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT REGION 509..749
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 821..843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1117..1247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1346..1373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1832..1870
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2661..2680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 749..797
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1254..1298
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 536..546
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..563
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..582
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..599
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..690
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 691..704
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 727..741
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1144..1159
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1160..1171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1346..1362
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1832..1847
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1848..1870
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 41
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 216
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 154
FT /note="Important for catalytic activity, responsible for
FT pKa modulation of the active site Glu and correct
FT orientation of both the proton donor and substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-2"
SQ SEQUENCE 2714 AA; 296713 MW; 92D6D65A9FC0E34B CRC64;
MIGRRLLSAA NSFRARPLRI TRLGKKTASM HNTGERRWNP DPAILRVDDT YYIAVSSFTY
FPGVPIYRSR DLANWELVSH ALQKPQQLQL NGISSGNGVW APGFSHIDGR FYITSMTRWG
DDPDNRTWPR IWWTSSEDLE TWTDLVWAEP YGIDPELFRD PDSGKTYLLL MGPNNNYDRV
WGITQCEVDL RSGKCTGPYF NTWNGTLPHD AKSRPEGPKM FKREGWYYLL LAEGGTSTGH
RATIGRSKSP EGPWEAAPNN PLIYNGADQA LTIQSTGHAT FTETPGGAWF ASLLARRNVK
GASPLGREAF LVNVTWADGW PTLNGGRYLV PSQFTEGDVV RKPWVDNFEG AKLDLSWYQV
RTPYAENYRL LGDAGNSTSG KMTGGLVLNP NVFTLSDRDV PAAIFHKQTS LNMTFSATLL
PTAGVLGPRQ QVGISAYLSD VKSHSRHPLS DQRQVFESSL LSSGLTTWLQ SVIACGPGRE
QIRECSSNLK RRMSQPNRLD NELLTTPSEL SFNSATPSMA AGSDASSVRR RRARFTARPF
KFRPPTIRFR SRRPSQNLNN SPYMSPGPYH SDDNHIESEP EFRWSSSNLS ISTDATSIPS
DDATTKSTPG RQLVRARSVP GRGTVGLRQR SQQNRQPGRV GLTLPDGRGR TYHISVAPGP
LQDSPTPARA KIEAPPVQAP VSQAPAPQAK GKGKGKGGRN KRKGGGAQAR QVEALKESAK
TSQDTPSSVV SNEEASAARS RSTSRHKGEE ILLKQVEELK GEVKSLQDGQ SSTARDLENA
LDKISVISAE KKDVERRLAE ASAPSSVVRG FEHQYQMVDD AQSSLTTHSK HSRSPSKGLQ
EVQGLQQDKA DLEAKVSELE KDLTLYKDFK VCLEAKCDEL QDEIKQQEER FKTDSEKLRS
DVEDVEDLRK TQDTAHIARI VSLELLKESL QAKAQALEAE IARKDFEYGE FTTERDQLSK
YKDAWVEEKK DLESRVEVLE SEKSKLEEQT KALEETIKGL ETERDSIQAH VVELEKTNGE
LQSKVGGLED DKSTIVSKSE KLKTKVDRLK GENGNLRTQV SSLLKDQDDH TSQVLTLSAE
RDGLKEENIT LKAMSEAGSV LGSVVGSRVG RWVASEMGSQ APSEVGSVAS KATGKAPSEV
GSTVSKASKA SSAVSKKSSN SGTKAPSQVG SLVSVKEEAD AEDDAATTVS DATVKPDEKT
SEVGATPASG DSSAPDIIEV TESEAGEPAT EPEAAVKEAP SAESTADPEQ AALLATLQTQ
KTELETRNAT LQEEASKVET LTTERDDLAS RLATAELDAA QLPTLREENG GLATQLAETN
AALESAMAAH AAANGEVDGL KAEVTSLRSR LSSPSRRSGS TRSSRKDGDK AKQLVVVRDP
NDRGQMSGLS FLKSQVMMQN NLQPSLSIPR LLSDISKPNQ TNISQIRAAR EKDLETLSQI
TKAILLVVQK ADIIAATNSL HSEATLATAQ DMFWVKPFKM ATSEQDMPFI RNLASSDRRI
RTKALASLQT YLTAQRKLDH LTALKLWKGL FFAMWMCDKP VPQQNLANDM ADLYASLPGA
KPTDASKPFE ANANCSQPKL SSLRLPTKKF RGDQVNIQAL QDGDFRAGYA LHKEPGVKCP
PDRRIRTKAL ASLQTYLTAQ RKLDHLTALK LWKGLFFAMW MCDKPVPQQN LANDMADLYA
SLPGAKPTDA SKPDSNDNVT IWFTAAYEVL APQWTEIDVL RMEKFLRLVR RMFAAQLRWV
GDKQWATERQ DKTIALLKQW HFESEGDVGR VPPGLRLHAL DIWVDEMERV GLFEGEGEEA
ETKLAFAHRL RAELIEPLTS CPIKSVRTSA RAELEDERLP WNEGKMDEDA DGAEAVGEEG
GDDDDDEWDG SPDTTIALYN VLWAERDGTN LHITHAQPTS KHKFRPVTAT VDISANSTEA
VDQLVEALLF RAYGQAKRQK RAKVLVNPHA GPGGAVNKWH HDVEPLFKVA RMTIDMQKTV
RSGEAIAIAR DLDIAQFDTI VACSGDGLPH EIINGLGVRA DSRHALEKIA VCQIPCGSGN
ALSCSTFGTY QAGEAALALI KGVDTVIDLT SITTGEERKL SFLSQVVGII AEADLGTEHM
RWMGNHRFTV GVAQRIFKKK AYPCDVAVKI ELDDKETIRT HYREKLNAAP VTMTKADGAG
LPPLKYGTIN DALPEDGWVS VKYDNMGNFY AGNMPLVAPE SNFFPASLPN DGLLDLVTID
SDISILKQIG ILTAVGDDST AFFASADVNY RKVTAYRFTP RNQKDGYISI DGEKFPFAPF
QAEIHPGLGK TYSKTGRQKT MSLPKSGDHP PAALPPIDIK PLLKRLWPVP LNGPQVTADE
IAEAISHFFT ARVSQAQAAS LLISLHFTNL DRRADVMAKS AYVMRQAAAA VDLPSLDRVV
KAKGLAEGGY GGGLCDIVGT GGDAYNTFNI STTASILASA LLAVSKHGNK ASTSKSGSAD
LVAHMQPRAP VITDVSPATL EKVYAATNYA FLFAPVFHPG MRFVAPIRKE LPWRTIFNLL
GPLANPVEDA LEARVIGVAR KELGPVFAEA LTIAGSRKAM IICGDEELDE VSCAGPTLIW
RLREGPDGVV RTDHFTVEPA DFGLPTHQLD EVSPGKEPAE NAEILRRILS GEVADDDPIM
EFVLLNTAAL FVVSGICEAD SSSMGPGDDG NVITERGPGG ERWKEGVRRA RWAVKSGAAW
KQWSAFVDVT NGFA
//
