ID A0A0D1BV76_USTMA Unreviewed; 1033 AA.
AC A0A0D1BV76;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=PLD phosphodiesterase domain-containing protein {ECO:0000259|PROSITE:PS50035};
GN ORFNames=UMAG_06066 {ECO:0000313|EMBL:KIS65977.1};
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631 {ECO:0000313|EMBL:KIS65977.1, ECO:0000313|Proteomes:UP000000561};
RN [1] {ECO:0000313|EMBL:KIS65977.1, ECO:0000313|Proteomes:UP000000561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021 {ECO:0000313|Proteomes:UP000000561};
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kamper J., Kahmann R., Bolker M., Ma L.J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Muller O., Perlin M.H., Wosten H.A.,
RA de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G., Snetselaar K., McCann M.,
RA Perez-Martin J., Feldbrugge M., Basse C.W., Steinberg G., Ibeas J.I.,
RA Holloman W., Guzman P., Farman M., Stajich J.E., Sentandreu R.,
RA Gonzalez-Prieto J.M., Kennell J.C., Molina L., Schirawski J.,
RA Mendoza-Mendoza A., Greilinger D., Munch K., Rossel N., Scherer M.,
RA Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B., Meng S.,
RA Ho E.C., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J., Deelstra H.J.,
RA Ortiz-Castellanos L., Li W., Sanchez-Alonso P., Schreier P.H.,
RA Hauser-Hahn I., Vaupel M., Koopmann E., Friedrich G., Voss H., Schluter T.,
RA Margolis J., Platt D., Swimmer C., Gnirke A., Chen F., Vysotskaia V.,
RA Mannhaupt G., Guldener U., Munsterkotter M., Haase D., Oesterheld M.,
RA Mewes H.W., Mauceli E.W., DeCaprio D., Wade C.M., Butler J., Young S.,
RA Jaffe D.B., Calvo S., Nusbaum C., Galagan J., Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [2] {ECO:0000313|Proteomes:UP000000561}
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021 {ECO:0000313|Proteomes:UP000000561};
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CM003160; KIS65977.1; -; Genomic_DNA.
DR RefSeq; XP_011392427.1; XM_011394125.1.
DR AlphaFoldDB; A0A0D1BV76; -.
DR STRING; 237631.A0A0D1BV76; -.
DR EnsemblFungi; KIS65977; KIS65977; UMAG_06066.
DR GeneID; 23565778; -.
DR KEGG; uma:UMAG_06066; -.
DR VEuPathDB; FungiDB:UMAG_06066; -.
DR eggNOG; ENOG502QUKR; Eukaryota.
DR InParanoid; A0A0D1BV76; -.
DR OMA; AKFCVVD; -.
DR OrthoDB; 1700675at2759; -.
DR Proteomes; UP000000561; Chromosome 21.
DR GO; GO:0030572; F:phosphatidyltransferase activity; IEA:UniProt.
DR GO; GO:0032049; P:cardiolipin biosynthetic process; IEA:UniProt.
DR CDD; cd00138; PLDc_SF; 1.
DR Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
DR InterPro; IPR025202; PLD-like_dom.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR PANTHER; PTHR21248; CARDIOLIPIN SYNTHASE; 1.
DR PANTHER; PTHR21248:SF22; PHOSPHOLIPASE D; 1.
DR Pfam; PF13091; PLDc_2; 1.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 3.
DR PROSITE; PS50035; PLD; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000000561};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 341..368
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 211..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 522..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 604..703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 713..732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 998..1033
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..281
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..553
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..643
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..731
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 998..1014
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1018..1033
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1033 AA; 113159 MW; 001CD13003C91E1A CRC64;
MPICGSSHIR DEATEKAHRS AGTQVGPFQD ARPQSSQPTI TSAVAADPAL APSAAAKHLF
PVPSAAKRGV LRFKIKEQLE EGRGKHWVWD KGAVHHSNRE PDDQELELVR LKYGYKPTDQ
GGPSRLYLMI LADCLLPLPR NPMSGVVSPP LLATTGIAPL SIFSTGPDII GHYYDCIVAA
RREVILLTNY WQGGKNVDRI ADALRELNRR VQQRRKRQAL DARSNGQSTS AANPSHTPQQ
EKAAKQQADL LHQQGAPGSI SRTEKDHDGF THDDQDIELG PPTAEERVVV KLMWDRGPQT
LADLFRLRKP VPPSMWKANG LPTENEIPNL TMEILNYHRP LMGTFHAKLL IVDRQVALIN
SNNIQDRPNV EACVRLEGDI VNSVYDHALI SWGNPLQPPL PCLTAPAPVA PSPAAFMTGS
QSTLPSLTVE KLKQLALNVR QRLHDEDTAT EVEKERSMQS PMSFHFGDVV DQVMRRDSLG
ATKGAAPAIR FPTNDQHVDG EKAARNAGAL WAQKVLGERF SHFQSSTSNK ADKSDTEPLP
HDKAGPTQPP HHKKNFADMV EALMKKEGHK PPAWAEGALE VFGLGQSSSK NVAEAVRRNP
RPKAALASGV NVPTAVAEED HGEQLDWRGS IEVEEESLDG ARSHTAIDDG STSPKPALSS
VGSDEAAPAV SKDLAAAEDE AVGKTTQPSS EDSAISAAPA ISDGVLQTRQ EAITESSTAK
EKEEVPGSIG YRRVHRRTLS QISKSSAAER LSAITKSLDF ANNSKVQGEI KAEQLSDEKL
SALNDVLDFQ PYVFHKPHEP VPMALVNRRP HGTPGHSDIR NPQDAAWLAG FRYAKKHVFI
QSPTLNASPI KAAVLAAVRR HVTVELWLDL GFNDKSESMP FQGGTNEQVV TGFYRQLRRE
GKGDEKYLEV YWYTGKDMTR PLNAVRKQRN CHVKFAAFDG QVAVLGSGNQ DTQSWFHSQE
INVMVDSKQI VDEWMAALTR NQSTKLYGMV DQRDGIWRGR DGQELVDTGK DQGKEKATAT
PPASTTPPAT LKA
//
