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Database: UniProt
Entry: E3Q4M0_COLGM
LinkDB: E3Q4M0_COLGM
Original site: E3Q4M0_COLGM 
ID   E3Q4M0_COLGM            Unreviewed;      1236 AA.
AC   E3Q4M0;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=NACHT domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=GLRG_01179 {ECO:0000313|EMBL:EFQ26035.1};
OS   Colletotrichum graminicola (strain M1.001 / M2 / FGSC 10212) (Maize
OS   anthracnose fungus) (Glomerella graminicola).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum graminicola species complex.
OX   NCBI_TaxID=645133 {ECO:0000313|Proteomes:UP000008782};
RN   [1] {ECO:0000313|Proteomes:UP000008782}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M1.001 / M2 / FGSC 10212 {ECO:0000313|Proteomes:UP000008782};
RX   PubMed=22885923; DOI=10.1038/ng.2372;
RA   O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA   Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA   Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA   Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA   Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA   Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA   Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA   Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA   Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA   Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA   van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA   Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA   Ma L.-J., Vaillancourt L.J.;
RT   "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT   by genome and transcriptome analyses.";
RL   Nat. Genet. 44:1060-1065(2012).
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DR   EMBL; GG697333; EFQ26035.1; -; Genomic_DNA.
DR   RefSeq; XP_008090055.1; XM_008091864.1.
DR   AlphaFoldDB; E3Q4M0; -.
DR   STRING; 645133.E3Q4M0; -.
DR   EnsemblFungi; EFQ26035; EFQ26035; GLRG_01179.
DR   GeneID; 24406544; -.
DR   VEuPathDB; FungiDB:GLRG_01179; -.
DR   eggNOG; KOG0504; Eukaryota.
DR   HOGENOM; CLU_000288_34_2_1; -.
DR   OrthoDB; 2329944at2759; -.
DR   Proteomes; UP000008782; Unassembled WGS sequence.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 4.
DR   Gene3D; 3.40.50.1580; Nucleoside phosphorylase domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR007111; NACHT_NTPase.
DR   InterPro; IPR035994; Nucleoside_phosphorylase_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001995; Peptidase_A2_cat.
DR   PANTHER; PTHR24188; ANKYRIN REPEAT PROTEIN; 1.
DR   Pfam; PF12796; Ank_2; 3.
DR   Pfam; PF13637; Ank_4; 2.
DR   Pfam; PF05729; NACHT; 1.
DR   PRINTS; PR01415; ANKYRIN.
DR   SMART; SM00248; ANK; 11.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF53167; Purine and uridine phosphorylases; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 11.
DR   PROSITE; PS50088; ANK_REPEAT; 11.
DR   PROSITE; PS50175; ASP_PROT_RETROV; 2.
DR   PROSITE; PS50837; NACHT; 1.
PE   4: Predicted;
KW   ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008782}.
FT   DOMAIN          421..568
FT                   /note="NACHT"
FT                   /evidence="ECO:0000259|PROSITE:PS50837"
FT   REPEAT          880..912
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          913..945
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          951..979
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          980..1012
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          1017..1046
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          1048..1080
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          1081..1113
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          1114..1146
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          1147..1179
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          1164..1187
FT                   /note="Peptidase A2"
FT                   /evidence="ECO:0000259|PROSITE:PS50175"
FT   REPEAT          1180..1212
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          1197..1210
FT                   /note="Peptidase A2"
FT                   /evidence="ECO:0000259|PROSITE:PS50175"
FT   REPEAT          1213..1236
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
SQ   SEQUENCE   1236 AA;  136507 MW;  BC547805C3F6C763 CRC64;
     MTALKRLQHP QMYTVGWITA LDKELTAAQA ALEERHQKPE NFRKHPKDTN SYVWGRIGDH
     NVVIASLAAG KYGTVSAATT AWSMISSLPH LRFGLMVGIG AGIPRLADNV DIRLGDIAVS
     QPTGTSPGVV QYDIGKLEDD GQFKRVGSLA PPPEVLLKGL AALKAEHRLK GPRVRDILDD
     MLQRHPRLAE ESDDAAFVHQ GAQNDRLFEA SSVHVERPDP QSTTRACEHC DPKKEIRRRA
     RRSIDPVVHY GVIASGNSVV KDGISRDDIT RRLGCNSICF EMEAAGLMDN FPCLVIRGIC
     DYADTHKNDR WQNYSAATAA AFAKELLEVI DSDDVERASR IDEVIEQHYL HYVAVHEDVS
     QIRSITNDMH QSLHSREVMR WLSPPDPSTN DNKALQQRHE GTGQWLLDSE EYLKWKTTPN
     SSLWLYGNPG CGKTILSSIV IKDLRTQSCS QSLLYFYFDF TDTSKQSLEK AIRSLIAQLY
     SQSEDVQTPL DTLCSTYKGH SRQPSIDVLI STFESMVQKI GEVWIVLDAL DECQTRTAPK
     NEGLLCWVQS ILNSSQANVH LLLTSRPDHD IKTELEKFVN DQILLQSDLV TKDIRVYYMI
     AVLISIAKLN RFRWVSCQLE ALEKCPDPLS LRKTLQSLPR TLDETYARVL SKIPPEHEQN
     AKRILQFLAF SERPLRIEEA VDLIAVATES KPRFDAKNRM PEPSEISLYC PSLVAIVSRG
     GKDGGKKVKE MQLAHFSVKE YLISDRLETN VSESFREPLA RASIVEICLV YLLELNHSLS
     LSNIRQSYPF AQYAARYWMN HAIQTEGSKI HHLIKEFCLH KDSPKTCYRL YSPDRPSEKE
     PKSFLREKTP LLYYVSYGGI VCAVEEVLKN GADVNAQGGR YGNALQAASA EGHTDIVHIL
     INKGADVNAQ GGRYGNALQA ASQRGHTDIV HILINKGAEV NAQGGSWYRD ALRAASAEGR
     TDIVHILIDK GADINAQGGR YGNALQAASQ GGHTDIVHIL IDKGADVNAQ GGSWYGNALQ
     AASQGGHADI VHILINKGAD VNAQDGSRYG NALQAASQGG HTDIVHILIE NGANASVANK
     DGQTPIYMAS QNGHIEVVKL LLNNGADASV ANKDGQTSIH IASQNGYIEV VKLLLDKGAD
     VTVPDHNGWT PLIWASSNGH LEVVKLLLDK GADVTVLDHN GWTPLVWASS NGHLEVVKLL
     LDKGADATVV DYYNITPLSV ASREGHTSIA KFLLSR
//
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