ID C6H592_AJECH Unreviewed; 1422 AA.
AC C6H592;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Lipase/serine esterase {ECO:0000313|EMBL:EER44834.1};
GN ORFNames=HCDG_00413 {ECO:0000313|EMBL:EER44834.1};
OS Ajellomyces capsulatus (strain H143) (Darling's disease fungus)
OS (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=544712 {ECO:0000313|EMBL:EER44834.1, ECO:0000313|Proteomes:UP000002624};
RN [1] {ECO:0000313|Proteomes:UP000002624}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H143 {ECO:0000313|Proteomes:UP000002624};
RA Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B.,
RA Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.M.,
RA Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S.,
RA Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J.,
RA Yandava C., Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S.,
RA Nino-Vega G., San-Blas G., Taylor J.W., Mendoza L., Galagan J.E.,
RA Nusbaum C., Birren B.W.;
RT "The genome sequence of Ajellomyces capsulatus strain H143.";
RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the putative lipase ROG1 family.
CC {ECO:0000256|ARBA:ARBA00007920}.
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DR EMBL; GG692419; EER44834.1; -; Genomic_DNA.
DR STRING; 544712.C6H592; -.
DR VEuPathDB; FungiDB:HCDG_00413; -.
DR HOGENOM; CLU_238899_0_0_1; -.
DR OMA; EDGHHAP; -.
DR Proteomes; UP000002624; Unassembled WGS sequence.
DR GO; GO:0016301; F:kinase activity; IEA:InterPro.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR017438; ATP-NAD_kinase_N.
DR InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR InterPro; IPR007751; DUF676_lipase-like.
DR InterPro; IPR044294; Lipase-like.
DR InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR PANTHER; PTHR12482:SF70; LIPASE ROG1-RELATED; 1.
DR PANTHER; PTHR12482; UNCHARACTERIZED; 1.
DR Pfam; PF00781; DAGK_cat; 1.
DR Pfam; PF05057; DUF676; 2.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
DR PROSITE; PS50146; DAGK; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000002624}.
FT DOMAIN 127..277
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT REGION 663..686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 725..749
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 783..835
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 884..903
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1036..1105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1141..1181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1262..1318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1342..1389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 797..817
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 884..899
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1036..1076
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1157..1181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1294..1316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1342..1368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1422 AA; 156804 MW; 05AB4D0BB05028B2 CRC64;
MSTLSQGLVD IEHVSHNTST NSLTYIPTGQ EKHGSGKIQA VIQEDRIVAV VPCPEDSRLT
SYIWLEASDP PPPAGLPDKQ KQPEYPYVLK RFEAAGECPA SLREFIGSPQ SHLYPAKLSA
SSSTNPADRN NLHIIISTLS GTHQATLFYT TLLKPLLATL HLHEHQDYCT HVTSSADTIT
HLTQTIFRPR AQRGIAQTII LLAGDGGLVE IIQGLTAVRA ADDFVSPVVA LVPMGTGNAT
AHSAGIVSGR DATMGLRGLV SGVAKRLPMF AARTSRGAEP LDGRLWFVHF GPLKSEAVME
VMQLAYDEGR HVVDMRDVVG YEEVEAVRIE FCEGETEERW RRICIDGMIL VVQDGQQLSQ
GNLAGETIGT EIRSGGRDRF LSGQQLQRKK QWAESGERKT VCKGGETAEK RRRRSDCAYL
TTTLRPTPSF SNARPDKCTP AQPSSLKRSV RFAKLSMLVT PRLYRLAQIP DNGSRAPFSY
HPSFNTLTGW DVEPAEYERA AEMLLVHQVG SVRVGEVVRF TLTYTPFADR ILPTPTELFV
KVRNTSAIPL RAAYLHGPYT LYTSCYPASF DPNRKYEDHE TRGLPQFEPN LKAGGAFDSV
IPVPEDVQSS TSAADQQSIT WIIEIASQVI FSTTAAVNFE VLVGRDLKSL ELGIGNSTSL
PVPGHVRELA RRNSKSKHKN PPGPMKGVYS TAVKLVIDDT ASLWSTPRFP SWSEKEDLRN
LEMEQTEIAT ESQRDSEANS AGEAENRKKR RKVHFVVLTH GLHSNIGADM LYLKESIDAA
SRKAREDARN ERNKAKNSHP SQPAVPTQDV SDTPSVDRQH TASEEDDDDD EHVIVRGFPG
NVVRTERGIQ YLGKRLAKYV LLMTYPDQPY LPLKESRSKF RAFAGNKDST GSSGRASHSG
SAIYRHEPKK SDYGYQITSI SFIGHSLGGL VQTYAIAYIQ KHSPEFFDCI KPINFVALAS
PFLGLSNENP IYKFRNRTVY SNVVNDGIVP LRTSCLLFLD WRGLDRVEKA RRESGWVGTM
AEWGWAEITG ANVNTNSIRS TKRPTNSVPT NSANDDTRTI RRSQTVGNNE LAETPWTDGP
SRSPCAEPAR GDSFHQEDGH HAPPKTTILE AAGDVLKPPL PSTEYILDPS TRARTIFHDR
VYHPSDIPPP PPKKNRSFFP TSSTSSLPSP TETAKSIDNQ SNNSLIQTTS DSVLGTTSGM
KVEEKIARAY HRDLSWRKVL VRLEPDAHNN IIVRRMFANA YGWPVVKHLV DTHFANTTAA
KTADEFESGA ERAMPTSRSP SESGKEVIGQ VDPPGKSSTL TIQQPKPENQ HPPESSETMD
ALRALLSPAT PNRILPYAKT DITNSIDPHQ PTMSVSRMSS SQSKTSHADS SRWTDRYFDD
EDGEGYDSQD EAHFAGSGIP EDCEVYRTAA SARGVGNGRI GG
//
