ID A0A178F4N7_TRIRU Unreviewed; 1543 AA.
AC A0A178F4N7;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Ankyrin repeat protein {ECO:0000313|EMBL:OAL66955.1};
GN ORFNames=A7C99_2352 {ECO:0000313|EMBL:OAL66955.1};
OS Trichophyton rubrum (Athlete's foot fungus) (Epidermophyton rubrum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=5551 {ECO:0000313|EMBL:OAL66955.1, ECO:0000313|Proteomes:UP000243015};
RN [1] {ECO:0000313|EMBL:OAL66955.1, ECO:0000313|Proteomes:UP000243015}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CMCC(F)T1i {ECO:0000313|Proteomes:UP000243015};
RA Zhan P., Tao Y., Liu W.;
RT "Genome sequencing of Trichophyton rubrum CMCC(F)T1i isolated from hair.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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:OAL66955.1}.
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DR EMBL; LHPM01000012; OAL66955.1; -; Genomic_DNA.
DR VEuPathDB; FungiDB:TERG_04622; -.
DR VEuPathDB; FungiDB:TERG_12164; -.
DR Proteomes; UP000243015; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008081; F:phosphoric diester hydrolase activity; IEA:InterPro.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR CDD; cd14483; SPX_PHO81_NUC-2_like; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR030395; GP_PDE_dom.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR InterPro; IPR004331; SPX_dom.
DR PANTHER; PTHR22958:SF23; DEPENDENT KINASE INHIBITOR PHO81, PUTATIVE (AFU_ORTHOLOGUE AFUA_4G06020)-RELATED; 1.
DR PANTHER; PTHR22958; GLYCEROPHOSPHORYL DIESTER PHOSPHODIESTERASE; 1.
DR Pfam; PF12796; Ank_2; 3.
DR Pfam; PF03009; GDPD; 1.
DR Pfam; PF03105; SPX; 1.
DR PRINTS; PR01217; PRICHEXTENSN.
DR SMART; SM00248; ANK; 7.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF51695; PLC-like phosphodiesterases; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 3.
DR PROSITE; PS51704; GP_PDE; 1.
DR PROSITE; PS51382; SPX; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000243015};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 177..199
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 484..650
FT /note="SPX"
FT /evidence="ECO:0000259|PROSITE:PS51382"
FT REPEAT 799..823
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 898..931
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 933..965
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 1189..1495
FT /note="GP-PDE"
FT /evidence="ECO:0000259|PROSITE:PS51704"
FT REGION 1..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 330..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1488..1509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..104
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..421
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..477
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1495..1509
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1543 AA; 168118 MW; 8D018F3FB3ACB107 CRC64;
MAAMSTGGGG MPTSDPPKPT TNPEPSQPPT SAPPPTTSNE PTKPSDPPTS QPSPTPPPPS
SEPSKPPTSE PSKPPTSAPP SSPNPEPTSK PSSPPPPPSP TTSDSPSPTS QNPSPTTPEQ
SSTTIIITST ASLPSNPNPT RPAPSSSSSS TSSSAPTLPP GSGSGNGNGG LSAGGTIAIA
VVVPVVSVAL IIILLLFWYR KRKARKLAEE ERKQEIEEYR FNPNNDPTLP AVGMYDTDVA
LKDTSAAAAA GAGGAAASGG YRGWGTTSNS RHAPTNTASS GGADSSAMYG REVSPVEESF
HMADDEQRQG LGRVEPAAAG IPKALHIGQP PVQQQQQQQQ PLQHQQQVPI QHQNASNIHR
GLSNASSAYS TGAQSDMSDD MMPPGAPAGA QYYEESAYYP DGQGAGYSHG HSSSHGHDQT
SLGPQPVIRD VSARRNTRIE SPSNTGDSGD IEAEAAEKGQ EETTLEQRSD SQRQTRARKQ
RRAMKFGKQI QRRQLDLPEY AASFFNYKAL KKLIKQLSAT PTIPAQGAAQ EQSSDVLDAQ
AALRANKEVF FFRLEREIEK VNVFYLQKEA EFSLRLKTLL DKQRMIQSRR TVSNSKAPAN
FVALIEGFQQ FDGDLNKLQQ FVEVNETAVS KILKKWDKTS KRAVEVQPCF NREVLRDLSD
RATTARLELE AWAEGENIQF NAPRQADRPA SIAEEDDSDL HILNSAAATG NLQPLRDWLS
KIQLSPDAAD HLTRIFLTAI NEYPDEVLTL LLETNLVDVH AEDDINERNC LHEAVISGRQ
FVFDAALERG VDISQADVYG RIPLHYACMH GRVGMVHSLL EKGLSTIDYT DHDNFTPLIH
SIIKDQVSCV EQLLSHNARI NPTSESDHIP LNLACQHASL ALIKILLERD AKFLPDAEGL
YPQHLVARSC RSSAVLLLLK DHGADLDQRD KLYQWTPLFH AAAEGCVGCL RTLLDCGVDA
DALDEKGLPA MYYAVWEGHL ECMKLLWSQR ISRPIAGQTP LDVLNNGPKY RDAMTATLTP
LSDERKQIPA LEVDGIPDLS LPPPIIPLRH YGHNFLDNKT FVQIHFNPPS ADPIVFYQTG
RYAAARLTIS SKMTDLIPRN VMLPLQEDSR FISFHIDKLE NFAIDFEIFP TFGSKVIAKT
VALPDVFEND GRSSGHCCLP VFDPRLRAIG EIRFNFQVIK PYYGDPLEIT HFATYWKATS
AFDAEHNGQV TGSSLSGDYV QIFVQMTRDL VPVLYPEFTI MHHGVRIPIS HLSIEEFKAI
GREHPPPSNI IIASSESNST GNSSTSSLLP SLAAMSITDI PTAHRLLATS FLTLEEVLLH
LPTSIHVNLC ILYPSPAEQK ELDLRLTFNI NNFADAILTH VFNHARASRL ANPDFMRSVV
FTSYNVGICV ALNWKQPNYP VLLCNDLGQP RDSNTSSIQS PASPPSFSSP AIQYSGRASL
SIKESARIAQ SNNLMGLMCR SSLLNVMPSL AESIKELGLV LVADTSDESA ERRRQQNAGS
VNANSTSHAG FGGTNDALFR MPGNVNGVMR ETGVLRFNDS IDM
//
