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Database: UniProt
Entry: F2Q460_TRIEC
LinkDB: F2Q460_TRIEC
Original site: F2Q460_TRIEC 
ID   F2Q460_TRIEC            Unreviewed;       878 AA.
AC   F2Q460;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Choline kinase {ECO:0000313|EMBL:EGE08928.1};
GN   ORFNames=TEQG_07883 {ECO:0000313|EMBL:EGE08928.1};
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: 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}.
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DR   EMBL; DS995790; EGE08928.1; -; Genomic_DNA.
DR   AlphaFoldDB; F2Q460; -.
DR   VEuPathDB; FungiDB:TEQG_07883; -.
DR   eggNOG; KOG2686; Eukaryota.
DR   HOGENOM; CLU_012712_4_0_1; -.
DR   Proteomes; UP000009169; 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:EGE08928.1};
KW   Transferase {ECO:0000313|EMBL:EGE08928.1}.
FT   DOMAIN          279..357
FT                   /note="Choline kinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04428"
FT   REGION          1..145
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          179..206
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          245..286
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          306..325
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          378..399
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          674..697
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          769..807
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..60
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        69..134
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        179..197
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        378..395
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        781..795
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   878 AA;  97529 MW;  EF19BA9F8C442C18 CRC64;
     MDSSTRPSTQ KNLKPISTSV ATSNAPASAP VGQSVEEQQQ QQQPYTTTPD TTGTRKTFRS
     GKKGVSTRPG LPKSSSASLK SVSSQISHLS LDRSNSDLST SSNANTHNNI TGLPTTSAPS
     DEDRLSSSIS SFPALPPPTS EPQSFLFRSS TADDVSIQAQ YHALLGQVHQ WLHQEKSKLG
     LPSTSTSTST AKSPRLIPRS TSAPLKGDLL GDTSTSADAQ IPESTLALEK LEKILSQYST
     DALSGPAGAP WRRRRGGSWG QGKRGYGLKG LRRGSASDSD YTDNEMSVPS ADVVLDNSKT
     LLYSGGEADS DIATQPEGSK PGSGKDKEYW LHFKSEIVRL THTLGFKGWR RVPLDAGGEV
     EVVRLSGALT NAVYQVSPPK DMSKYSQSTS SQGLPRKPPP KLLLRIYGPQ VEHLIDREHE
     LQVLRRLGKR NIGPRVLGTF KNGRFEQYLH ARTLTTRDLR IPETSIQIAK RMRELHEGID
     LLPKERDGGP GLWKNWDKWV NRCEKVTTWL DSEILADHNE GKSAKEPWRK RGFVCGVPWE
     TFRGMVDRYR QWLAASFGGM EEITRRLIFA HNDTQYGNLL RLEPSGESPL LLPANEHKQL
     IVIDFEYAAA NMRGAEFANH FTEWCYNYHD EDRPWRCHTT WYPTLEEQKR FIRAYLTHRP
     RLISETNNNI YPSGQNFSTS SVSSTMTTPG LRPTYTSSPR VAPLSLDTYT PSVPFSISKD
     DQIDEELEVE VQKLLHEARV WRIANSAMWV AWGIVQAKVP GLEAAVAGTS TPVAHTSTTD
     PASDKNDKEA ALNSDESTDD ASTTPTQETV DVQQMLAATD QALQEVEVDE AADEFDYLAY
     AQDRALFFWA DILAIGLIKE EELPMEMLEH IKRRIVEY
//
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