ID   A0A0G2EU08_9EURO        Unreviewed;      1215 AA.
AC   A0A0G2EU08;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Putative filamentation protein {ECO:0000313|EMBL:KKY25631.1};
GN   ORFNames=UCRPC4_g01702 {ECO:0000313|EMBL:KKY25631.1};
OS   Phaeomoniella chlamydospora.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Phaeomoniellales; Phaeomoniellaceae; Phaeomoniella.
OX   NCBI_TaxID=158046 {ECO:0000313|EMBL:KKY25631.1, ECO:0000313|Proteomes:UP000053317};
RN   [1] {ECO:0000313|EMBL:KKY25631.1, ECO:0000313|Proteomes:UP000053317}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCRPC4 {ECO:0000313|EMBL:KKY25631.1};
RA   Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT   "Distinctive expansion of gene families associated with plant cell wall
RT   degradation and secondary metabolism in the genomes of grapevine trunk
RT   pathogens.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KKY25631.1, ECO:0000313|Proteomes:UP000053317}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCRPC4 {ECO:0000313|EMBL:KKY25631.1};
RA   Morales-Cruz A., Amrine K.C., Cantu D.;
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in endocytosis. {ECO:0000256|ARBA:ARBA00002550}.
CC   -!- SIMILARITY: Belongs to the YPP1 family.
CC       {ECO:0000256|ARBA:ARBA00038251}.
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:KKY25631.1}.
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DR   EMBL; LCWF01000040; KKY25631.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G2EU08; -.
DR   OrthoDB; 2727302at2759; -.
DR   Proteomes; UP000053317; Unassembled WGS sequence.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR23083:SF464; TETRATRICOPEPTIDE REPEAT DOMAIN 7, ISOFORM A; 1.
DR   PANTHER; PTHR23083; TETRATRICOPEPTIDE REPEAT PROTEIN, TPR; 1.
DR   Pfam; PF13181; TPR_8; 1.
DR   SMART; SM00028; TPR; 5.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS50005; TPR; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000053317};
KW   TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT   REPEAT          1011..1044
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REGION          727..936
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1071..1135
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        729..743
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        758..782
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        790..810
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        811..837
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        838..853
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        854..885
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        918..935
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1215 AA;  134728 MW;  33200DD4D05E0BFE CRC64;
     MSVRERDKAQ RYIDSLDSAR CNGAWNEVPE YIRKVRKHAP SRNCLITTAT AEYQVATFSE
     SRPSTSSSTL STALPSLIPD LLSAIDKETE YLQDRLQAQT CLAWIHWNLA EPALAASRLP
     KDYSAVLSDF SKETPSRLTG WTEVCLIKGA CLKGTAQSQA GHLRESLETF QSLLPWITSS
     ITGTAFSKQR SYWTDQFLAQ LALVASKDEE ILFNQRELAL QAFRHWAIRA QKQQNVGSDI
     GFGFVFPSQP QIWKAYFQFL SRLIQKSYEY PDDSDLAPKL QQYVEYKRVE SMYENVLMKT
     VRFPKAHDSS LEIEGWVEQV IRNWRVLCGP QWTDEELGQG GKNAVGRVVL DVLYRAATKT
     FHSTLVLRRL FQVHKSLAEF DLAYKALDTY IEIVKRGRAK AEKAGEPATD IDDEETIVRT
     LSEGIDGLCC FGSAEQAEKA NDIADLLDEW IGASKVAAVG KTDGVDDIIE SQQVLEPADS
     EASAIAHRSI GIAQAQWARY TPFSEDRSAI RKEAISHLES AIAYRSPAFA NYESYFALGL
     LLAETRDLDG AVQYVKEALT STELAAAIPD APDYERERQM IPLWHLLALV LSGRQDYETA
     ERACEGALRQ FPSPATLFGT GHHKHINGTT NEKRDQQIVS TGLVDKMDAL ELERLLEIRM
     TEIALTEVVE GPEIAVNSTN ELLSLFARLF GRLGINLEDR PPVVDSVPPK TSAGTIKSFR
     GSIFSRRKAA RSSGRQSVLP DRTSTIPEKE LVRSPSAANN APAIQVTDEN QRLQSHNAPP
     MRRSSSAHHK LQRREGSINR KLRERSMERA NSRPSSSYAT SSHRPSFETG REGLSRNPSF
     KQQDHKAHTN DEVIEQSNGR TTLESTDPAT LPPPASATAG VTESPTAKQE LPEIAHNNRH
     DTVPPPPGHK DQPPEQDIRL PSASSQTQPS PQFTDAEAQK RAIGILVKIW LLIASLYRRA
     TMFEDSSEAI SEAQRHSTAI EALTASTQGS SAKAFADPGW NSTKSSDELM ADIYAERGLL
     SLARTSPHEA IDHFEQALIY LPHHGKATVA LATILLDIYA QKIPAERFQS GTDSALHSTS
     PTIHPNKPLN STCTPPSTIS SVTNPKPNNI SPSVNGTTSN SDNAMTAEEP AESLRKTPSN
     LNRLAARDRA YGLLAAYTKL GAGWDDSEAW FTLARAYEES SEIDKAREVL WWCVELEDTK
     PIRHWRNLGS GGYVL
//