ID A0A423VL83_9PEZI Unreviewed; 805 AA.
AC A0A423VL83;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE RecName: Full=Choline kinase N-terminal domain-containing protein {ECO:0000259|Pfam:PF04428};
GN ORFNames=VSDG_07917 {ECO:0000313|EMBL:ROV91640.1};
OS Valsa sordida.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX NCBI_TaxID=252740 {ECO:0000313|EMBL:ROV91640.1, ECO:0000313|Proteomes:UP000284375};
RN [1] {ECO:0000313|EMBL:ROV91640.1, ECO:0000313|Proteomes:UP000284375}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YSFL {ECO:0000313|EMBL:ROV91640.1,
RC ECO:0000313|Proteomes:UP000284375};
RA Yin Z., Huang L.;
RT "Host preference determinants of Valsa canker pathogens revealed by
RT comparative genomics.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC -!- PATHWAY: Phospholipid metabolism. {ECO:0000256|ARBA:ARBA00025707}.
CC -!- SIMILARITY: Belongs to the choline/ethanolamine kinase family.
CC {ECO:0000256|ARBA:ARBA00038211}.
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:ROV91640.1}.
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DR EMBL; LJZO01000042; ROV91640.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A423VL83; -.
DR STRING; 252740.A0A423VL83; -.
DR Proteomes; UP000284375; Unassembled WGS sequence.
DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IEA:InterPro.
DR CDD; cd05157; ETNK_euk; 1.
DR Gene3D; 3.90.1200.10; -; 1.
DR InterPro; IPR007521; Choline_kin_N.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR PANTHER; PTHR22603; CHOLINE/ETHANOALAMINE KINASE; 1.
DR PANTHER; PTHR22603:SF93; RE24176P; 1.
DR Pfam; PF04428; Choline_kin_N; 1.
DR Pfam; PF01633; Choline_kinase; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000284375}.
FT DOMAIN 256..328
FT /note="Choline kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04428"
FT REGION 1..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 146..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..56
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..166
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 805 AA; 90185 MW; 418052182CACEDC9 CRC64;
MPPTPLNAQG QPIRPALKTE DDATRTPPSG PVKAVHIAEP EPLPPDEPRP KREFAASVSG
KRLSGRPPMP KTDSSRTSLI SQNSIDTIDL SGNHSTPSLV QLPEDSAIQG NQQQAANHPQ
SHRIDRASEK LLSQVADWLQ REKIKRETKK PRKHHHHHHH LRRKLKKSRP EEATAGEEVE
NEDEDPLRRT ASNESNSSDV SLDRLQRILD DSMAALGLNS ISHYNAKLGR RSSHRKKLAS
RSSQYLNRAA ASSDTDFVDG DVLVPSCDAV LDNSKTLKYS QAGPDDSVSV CSKREEKERQ
AWITFKNEII RLAHTLRLKG WRRVPLDSGD EIQVERLSGA LTNAVYVVTP PENLPESEVS
KKKPTKVLLR IYGPHVEQLI DRDNELSILK RLARKKIGPR LLGTFKNGRF EQFFNAAPLT
PEALREPDTS KQIAKRMREL HEGIDLLEDE KDEGPTVFRN WDNWVDNVER RSLFLDQVAA
SHDPNAPVGP ADAWKKCGFV CGLEWPKFKA MVDKYREFLI QYYGPAKLRE KLVFAHNDTQ
YGNILRVQPD DEKSPLMHPE NEHKQLIVID FEYASANTPG LEFANHFTEW SYNYHDLSTS
HACNAEGYPT PEEQKRFLKA YVNHRPKFAT SSSSANSDYD VTPGATPLLA PQNPSSSIVE
FMLDARVPPG GWKEEERRAA EASEEKVREL MEETRVWRAM NSAQWVAWGI VQAKIPGYSE
AAPDGDVPVS PVSSVGTVTG ADLGAEGGDG SAAGGRGADE EAGFDYLSYA HERALFFWGD
CVQMGLVRLE DLPERLRGRV KIVDY
//