ID F2PMQ9_TRIEC Unreviewed; 430 AA.
AC F2PMQ9;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=ethanolamine kinase {ECO:0000256|ARBA:ARBA00038874};
DE EC=2.7.1.82 {ECO:0000256|ARBA:ARBA00038874};
GN ORFNames=TEQG_02215 {ECO:0000313|EMBL:EGE03177.1};
OS Trichophyton equinum (strain ATCC MYA-4606 / CBS 127.97) (Horse ringworm
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=559882 {ECO:0000313|Proteomes:UP000009169};
RN [1] {ECO:0000313|Proteomes:UP000009169}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4606 / CBS 127.97 {ECO:0000313|Proteomes:UP000009169};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine
CC biosynthesis; phosphatidylethanolamine from ethanolamine: step 1/3.
CC {ECO:0000256|ARBA:ARBA00037883}.
CC -!- SIMILARITY: Belongs to the choline/ethanolamine kinase family.
CC {ECO:0000256|ARBA:ARBA00038211}.
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; DS995726; EGE03177.1; -; Genomic_DNA.
DR AlphaFoldDB; F2PMQ9; -.
DR VEuPathDB; FungiDB:TEQG_02215; -.
DR eggNOG; KOG4720; Eukaryota.
DR HOGENOM; CLU_012712_1_1_1; -.
DR Proteomes; UP000009169; Unassembled WGS sequence.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd05157; ETNK_euk; 1.
DR Gene3D; 3.90.1200.10; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR PANTHER; PTHR22603; CHOLINE/ETHANOALAMINE KINASE; 1.
DR PANTHER; PTHR22603:SF66; ETHANOLAMINE KINASE; 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:EGE03177.1};
KW Transferase {ECO:0000313|EMBL:EGE03177.1}.
FT REGION 160..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 430 AA; 48718 MW; F4BF9E816460B164 CRC64;
MPSACTQPVG CHEVRYIPLS YNHADSQASA LRLVLTLNPH WKDAQGRIEF VRFTDGITNT
LLKIILRAPG LSEEEIDKEA VLMRAYGNNS EIIIDRERET KSHALLASRG LAPPLLARFA
NGLLYRFVRG QAASPDDLTK PAIWRGVARR LGQWHAALPI SDAPSDAPSP GTRDGDSLSL
SSSDSEIRPV QESTAVEDDI TPINTRFEGP NLWTTLQNWI LALPKSTDQE RTRRKNLQKE
YERILSEFDD GSGLGEEGMV FAHCDLLSAN VIIQPRPKES TLSDGAAETV DFIDYEYAIP
SPTAFELANH FAEWAGYDCD FSRLPTRSIR RSFLEEYVES FAQHRELPES KEKTVDSLFD
DVDRYRGLPG FYWGVWALIQ ATISRIDFDY ASYAEERLTE YWAWRREQDG SRSKAGEKMP
LREQRWAQEA
//
