ID A0A0L1IPV8_ASPNO Unreviewed; 1837 AA.
AC A0A0L1IPV8;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=NACHT domain-containing protein {ECO:0000259|Pfam:PF05729};
GN ORFNames=ANOM_010167 {ECO:0000313|EMBL:KNG81380.1};
OS Aspergillus nomiae NRRL 13137.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1509407 {ECO:0000313|EMBL:KNG81380.1, ECO:0000313|Proteomes:UP000037505};
RN [1] {ECO:0000313|EMBL:KNG81380.1, ECO:0000313|Proteomes:UP000037505}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 13137 {ECO:0000313|EMBL:KNG81380.1,
RC ECO:0000313|Proteomes:UP000037505};
RA Moore M.G., Shannon B.M., Brian M.M.;
RT "The Genome of the Aflatoxigenic Filamentous Fungus Aspergillus nomius.";
RL Submitted (JUN-2014) 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:KNG81380.1}.
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DR EMBL; JNOM01000455; KNG81380.1; -; Genomic_DNA.
DR RefSeq; XP_015402303.1; XM_015555423.1.
DR STRING; 1509407.A0A0L1IPV8; -.
DR GeneID; 26811971; -.
DR OrthoDB; 1786434at2759; -.
DR Proteomes; UP000037505; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0009116; P:nucleoside metabolic process; 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 PANTHER; PTHR46082:SF11; AAA+ ATPASE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR46082; ATP/GTP-BINDING PROTEIN-RELATED; 1.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 3.
DR Pfam; PF05729; NACHT; 1.
DR SMART; SM00248; ANK; 16.
DR SUPFAM; SSF48403; Ankyrin repeat; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF53167; Purine and uridine phosphorylases; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 5.
DR PROSITE; PS50088; ANK_REPEAT; 9.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Reference proteome {ECO:0000313|Proteomes:UP000037505}.
FT DOMAIN 410..565
FT /note="NACHT"
FT /evidence="ECO:0000259|Pfam:PF05729"
FT REPEAT 870..902
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 904..936
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 937..969
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 970..1002
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1003..1035
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1069..1101
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1102..1134
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1630..1662
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1663..1695
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 308..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1735..1754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1736..1754
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1837 AA; 204822 MW; 860ACB1B14B8F6AD CRC64;
MLSSNRTYDD YTVGWICALH IELTAAMAML DVIHPSLPPR DGDDNHYTLG QIGTHNVAVA
CLPAGLKGTN SAATVAAQMR ATFGSIGFGL LVGIGGGVPS DLHDIRLGDV VIGMPGVRSG
GIIQYDFGKT VAEGKFVHTG YLNTPPVVLL TAMNTLRARL ELSGEGQVLK TLSPNLPDSF
SKPSAPDQLF KAEYSHVGGV YTCQECDSSE EVARENRQHS SPFIHYGTIA SGNEVMRDGR
TRDRLRDEYD VLCFEMEAAG LMNTFPCAVV RGICDYADSH KTKQWQSYAA ATAAAYARDL
LFVVDSTASA KPRKRKPQPD EWSVGSSTKR RMSRVVKEED GNGSGWTARF GQISGRDHST
TETKCLAAFN VCAYKEHKNR NDNRYEGTCE WFLHDPKFIH WRDSAQSSLL WVSADPGCGK
SVLAKSLIDG ELQMSTHRTT CFFFFKDDNP EQSSLENALC AILHQLFSAH RNLIKCALPD
FNADKASFVK SAHKLWEILL SAISDMDSTN FVFIIDALDE CERRGRHELI ERLTCLHSES
DKRFSRAKFL VTSRPHSDIE RRFESCPSIR LAGEEKIGTI SDEIDVVITE KLNQLQTSLD
PEIQRYLREK LQSTKQRTYL WVRLIFQMIE EVIDERYYLT EEDEEVRGLF ESLPASVDQA
YSNILQNTKK SGPAVRILGI VLAATRPLTV RELNVALSLK GKEFSPMDVH LVPEREFRIR
VRNLCSLFVT VVDSKVYLIH HTARDFLMST ALRAGAASGW KGSISLSQSH QIIMSQCAIY
LRMPFFDDKR IIRDQTLELR HRPWSDDIAE DTHPYPFLDY AAKNWVNHLH ASGRVSSEVI
MLQDLCHTGY HRFQTWFQIY WSCKKSRCPR GFTDLIAAAY FGFADRVKAL LEEGANKDEK
DLTYGRSPLL WAAYCNQFAV VQLLLGNEVN RNLADNEGRT ATSLAAEAGA ANIVAMLVRV
GSDLTLKDLN GWCPLMWAVD RAQISVAKVL MDHKVDISSR DRYGKTSLWV AVEKGNDVLL
EALLQEGADP NIRVGFDQTP LSSAIGKCQR RMVKLLLDHG AEVKSTIGFG TTTVCLAAEK
GDLEITRLLV QKGADPSAPD RNGQTAIMIA AEHGHEGVFN YLLQNGVSLD SGSQTPLFAA
LKNGHESIAD RLIRKLKTTS SGASIIRKTM LQAAAQGLQQ IVEFLYFTAL DIGSRQECAM
EALTSSISSR HMSTVRFLLD QLLGIDMQDY GAMAPILMAI EYGNYEHVQK VFQDKVIKHH
STDTTDEITQ SEETAIDRRS AINDLLQHGW EPARSDKDGN TMLEISIIHN WYPRIAWELL
QLRVFPADIL KRCARRCVRE GHPTALKALL QYSPDEVLES QIITDLFKEA IDKEDVGTIA
LLTSFRGKRD SKLRSLYLRA IKDGLVDMAS IQIEEEGFSE SQLNELLSIA CVQCRAGIVK
ALLSAGAGAK KDREDPNVTE ALNASMKQND TRIMQLLLKG GTYPTKQLEE IMLWACHHGF
IEIVEPLLHA GVCPTYVNEQ GDSPVSMALM GHHDDIVKLL STWMDSPTPG AAMAEGNVTK
ANQERSNPNI WSAAPKRIRI VDMARIEGDY RMQTSMMFTA IRFDDRDLMA DVLQSGIVNL
DLDDDDRRTN LFTPLTWAVW SGNLDIVQML LDSGVNPNTS GSFGETAVSL AIRARQELIL
KLLIDHGAYC SFQDKWGKTP LVWAARYNTP MIPLLLGQGF KNPVRYISHS STTLKEDASA
EPKAKEDVHG PAAEAKAKKP FLQLAPDNDT SCMTFDRGSE RCVRTRYYCT NDIMKFPYTD
EDGSVYKSAA ECLVHPHNGL TTHGSIQNMP LYLEITA
//
