ID T0LZ46_COLGC Unreviewed; 1156 AA.
AC T0LZ46;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Ankyrin repeat protein nuc-2 {ECO:0008006|Google:ProtNLM};
GN ORFNames=CGLO_03077 {ECO:0000313|EMBL:EQB56876.1};
OS Colletotrichum gloeosporioides (strain Cg-14) (Anthracnose fungus)
OS (Glomerella cingulata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum gloeosporioides species complex.
OX NCBI_TaxID=1237896 {ECO:0000313|EMBL:EQB56876.1, ECO:0000313|Proteomes:UP000015530};
RN [1] {ECO:0000313|Proteomes:UP000015530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cg-14 {ECO:0000313|Proteomes:UP000015530};
RX PubMed=23902260; DOI=10.1094/MPMI-03-13-0080-R;
RA Alkan N., Meng X., Friedlander G., Reuveni E., Sukno S., Sherman A.,
RA Thon M., Fluhr R., Prusky D.;
RT "Global aspects of pacC regulation of pathogenicity genes in Colletotrichum
RT gloeosporioides as revealed by transcriptome analysis.";
RL Mol. Plant Microbe Interact. 26:1345-1358(2013).
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:EQB56876.1}.
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DR EMBL; AMYD01000641; EQB56876.1; -; Genomic_DNA.
DR AlphaFoldDB; T0LZ46; -.
DR STRING; 1237896.T0LZ46; -.
DR eggNOG; KOG0504; Eukaryota.
DR eggNOG; KOG1161; Eukaryota.
DR eggNOG; KOG2421; Eukaryota.
DR HOGENOM; CLU_002842_1_0_1; -.
DR OMA; LCTALNW; -.
DR OrthoDB; 4907at2759; -.
DR Proteomes; UP000015530; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0008081; F:phosphoric diester hydrolase activity; IEA:InterPro.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd08578; GDPD_NUC-2_fungi; 1.
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; IPR001995; Peptidase_A2_cat.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR InterPro; IPR004331; SPX_dom.
DR PANTHER; PTHR24189; MYOTROPHIN; 1.
DR PANTHER; PTHR24189:SF50; MYOTROPHIN-RELATED; 1.
DR Pfam; PF12796; Ank_2; 3.
DR Pfam; PF03105; SPX; 1.
DR SMART; SM00248; ANK; 8.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF51695; PLC-like phosphodiesterases; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 2.
DR PROSITE; PS50088; ANK_REPEAT; 3.
DR PROSITE; PS50175; ASP_PROT_RETROV; 1.
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}; Reference proteome {ECO:0000313|Proteomes:UP000015530};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1156
FT /note="Ankyrin repeat protein nuc-2"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004567663"
FT DOMAIN 143..306
FT /note="SPX"
FT /evidence="ECO:0000259|PROSITE:PS51382"
FT REPEAT 542..569
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 574..607
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 609..641
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 626..719
FT /note="Peptidase A2"
FT /evidence="ECO:0000259|PROSITE:PS50175"
FT DOMAIN 853..1153
FT /note="GP-PDE"
FT /evidence="ECO:0000259|PROSITE:PS51704"
SQ SEQUENCE 1156 AA; 127746 MW; 48524EAA1BEC1022 CRC64;
MHLLVFFELS LYLVSTVAPS CSPTGLIIPA CKRTPRATNT LSGLLLLPQA THATQEPPRA
NLILLSAVSK TLLPPVDVTQ YILVAVTHLA CRGDRRKLAE LFSVILHTFA CRLLPPACKY
WSDSISLLFK RIPSPSDAVI SRTKFGKQIQ KRQLEVPEYA ASFVNYKALK KLIKKLSATP
TLSAQIDPLR SAISIDSQAA LQANKATFFF QLERELEKVN AFYLQKEAEL KVRLKTLLDK
KKVLQSRNGV SRRSAKFTTL EEGFQQFASD LNKLQQFVEI NGTAFSKILK KWDKTSKSKT
KELYLSRAVE VQPFFNATVI SELSDQATTS LQELGAWAEG DHVTFEPRND HIVSSQHLLG
TDEGDADTLL LDTVISGNLE ALRDLLVRMR SAAAGSSSGS ELSLMERITR TFLAAIHEAP
KETLQVLLET GLVDIQSEDD INERNCLHQA AIYGNNFVLE YGITKGVAVD RTDVYGRVPL
HYASMHGRLD MLDALSTANA QTIDLIDHDN FTPLVHSIIH GHLQCVERLL VKSARIDPVS
DADHVPLNLA CEHGSLAIVE LLLKHGAQIL PDAEGLYPQH LVARSGQRPE LLLLLKNYGA
NLDQIDKLYG WTPLVHAASE GNVPCLHALL EVGADPNIVD EKDLPAMYYA AWEGHLECMK
LLTPYNARTK PSPMVTHSGG LVPMLTSSGP EPMALDPDAI PELELPPPII PLRRYGHNFL
DTKTVIQISF EENGDQPLVF FHDGKYPAAR LTISSKVSDL IPKNIMLPFQ EDTRLVSFQI
DNLESFTLDF DVFPTYGAKI IAKTVALPNT FKALLSSSGK CCLPLFDPRL RAIGQISFHT
QVIKPFNGKP LEITDFETYW KATSQFDRSP STFVTGSSLS GDFVRLFVQH TSDGIPVLWP
RWTIACGGID LPISRLTMEQ FNTITSKSPS RDELSSLPSK PLDAIADVHR VLATAGIPLN
EALALLPHGM HVNIQVLYPT PEEERTQGLG PSQDLNTFVD SLLTIVFDHA RAQRAQSLES
VRSVVFSSYN PSLCTALNWK QPNFPVFLCN DLGREDSMSP PDIIQSHGRR SASIKEVVRI
AQSNNFMGLI CCSRLLEMVP ALVDAIKSHG LALVTDKSLD PSNNNILSDP FPRLPKGVDG
VLKSHGVLRF NESIDV
//
