ID A0A135TF33_9PEZI Unreviewed; 794 AA.
AC A0A135TF33;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Choline/ethanolamine kinase {ECO:0000313|EMBL:KXH46717.1};
GN ORFNames=CNYM01_06395 {ECO:0000313|EMBL:KXH46717.1};
OS Colletotrichum nymphaeae SA-01.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=1460502 {ECO:0000313|EMBL:KXH46717.1, ECO:0000313|Proteomes:UP000070054};
RN [1] {ECO:0000313|EMBL:KXH46717.1, ECO:0000313|Proteomes:UP000070054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA-01 {ECO:0000313|EMBL:KXH46717.1,
RC ECO:0000313|Proteomes:UP000070054};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum nymphaeae SA-01.";
RL Submitted (FEB-2014) 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:KXH46717.1}.
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DR EMBL; JEMN01001140; KXH46717.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135TF33; -.
DR Proteomes; UP000070054; Unassembled WGS sequence.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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 Kinase {ECO:0000313|EMBL:KXH46717.1};
KW Transferase {ECO:0000313|EMBL:KXH46717.1}.
FT DOMAIN 252..326
FT /note="Choline kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04428"
FT REGION 1..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 615..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..164
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 794 AA; 88203 MW; 7BDA59BF2B352FC3 CRC64;
MSSSSSPQIT GQQQPLRSAM KTDEECASNT AKVVQIAEPE ADAVAPPPPA PPSDHHHKRQ
YAANMAKRLT GRMGLTSSSS SRSSPVMEPS PGPSSDDATA AAAAAAAAAA AAQPSHHHHR
HGHKAHYESQ KLLAQLNDWL EHEKKKKAAR KSKTSPRRRS PQSKTKKERS PAAETADPTA
QPAAPRSRSD SIDSDSSDVS FDRLQRIIED SMASMGISSV PQMSPKVGRR PSLRHKKSLS
RSMLHRTASS DTDYIGEDVI VPTCDAILDN SKTLSYSGGG KSTDDLTLGG QADEKEKAWE
TFKNEIVRLA HTLRIKGWRR VPLDSGNSVI VQRLSGALTN AVYVVSPPED LEEVPGKKPP
PKLLLRIYGL EALIDRENEL SVLRRLARKK IGPRLLGCFT NGRFEEYFNS ITLTPNDLRD
PDTSKQIAKR MRELHFGIDV LEREKDEGPA VLKNWDAWLG NVEKKICALD EGVRNGNCVF
RDRGYVCGVE WKQFKELYDK YRELALSAYK GHAIRERLVF AHNDTQYGNI LRMRPEDEKS
PLLKPANEHK QLVVIDFEYA AANVPGLEFA NHFTEWSYNY HHESLPFVCN TAVYPTIQEQ
RRFLKAYVEH RPQYTHGGAS TPRLTPAGAA DGSSAVGTPA LLPTSSSSSI VEFMLDARVP
PNHWKEEERR AEEAVEAEIK ELYEETRLWR GINSAQWVAW GVVQAKVPGF ESQEEIEQQE
KQAQNEAAAA AGDADAKAEV QAAAEAEDEG DEYDYLGYAQ ERAFFFLGDC VLMGIVKKEE
LPEDVQARLK IVDY
//
