ID B0Y788_ASPFC Unreviewed; 1189 AA.
AC B0Y788;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=NACHT and Ankyrin domain protein {ECO:0000313|EMBL:EDP49269.1};
GN ORFNames=AFUB_072950 {ECO:0000313|EMBL:EDP49269.1};
OS Aspergillus fumigatus (strain CBS 144.89 / FGSC A1163 / CEA10) (Neosartorya
OS fumigata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=451804 {ECO:0000313|EMBL:EDP49269.1, ECO:0000313|Proteomes:UP000001699};
RN [1] {ECO:0000313|EMBL:EDP49269.1, ECO:0000313|Proteomes:UP000001699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CEA10 / CBS 144.89 / FGSC A1163
RC {ECO:0000313|Proteomes:UP000001699};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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DR EMBL; DS499599; EDP49269.1; -; Genomic_DNA.
DR AlphaFoldDB; B0Y788; -.
DR EnsemblFungi; EDP49269; EDP49269; AFUB_072950.
DR VEuPathDB; FungiDB:AFUB_072950; -.
DR HOGENOM; CLU_000288_34_23_1; -.
DR PhylomeDB; B0Y788; -.
DR Proteomes; UP000001699; Unassembled WGS sequence.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 3.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR24123; ANKYRIN REPEAT-CONTAINING; 1.
DR PANTHER; PTHR24123:SF60; NACHT AND ANKYRIN DOMAIN PROTEIN (AFU_ORTHOLOGUE AFUA_6G07030); 1.
DR Pfam; PF13401; AAA_22; 1.
DR Pfam; PF12796; Ank_2; 3.
DR Pfam; PF13637; Ank_4; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 13.
DR SUPFAM; SSF48403; Ankyrin repeat; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 9.
DR PROSITE; PS50088; ANK_REPEAT; 13.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 209..346
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|Pfam:PF13401"
FT REPEAT 641..673
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 675..707
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 708..740
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 741..774
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 776..808
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 809..841
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 842..874
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 875..908
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 909..941
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 942..976
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 977..1019
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1022..1056
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1057..1089
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
SQ SEQUENCE 1189 AA; 131453 MW; 7DF03EFA5A55A3E0 CRC64;
MMVDTPAIRK RLAQASQSTR AARRSLLDGR EPQDYQQKAV LLLSEILDLL YEIREQLSGE
EEKWVVAQER LDSLDDFLNY FMSTIRALEY YFQPGGVSSR HYRKSLLERT FLPRLEQFKS
LILVVLQAES IEKSFTEREL RNAVRRYGAL ETVESRAISE YDGDFYNITG PISSKNFMSL
ADLCNKRQQG TCQWIFQEEK YKSWLFGAQR VLYCRGPPGA GKTFLAASIT DSLQRTFTTP
DVAVVFLFCQ VENGDEESSS ISLLANILAQ LVYRKRSASY CTASLYRSEE FAKGRASAKA
YQNAIRAEVD HFSKIFVIVD GLDTSPEKDR ILNRLQKLPD HTQLLITLRE TGYAQKDDSI
LALAHSEDLE TYISTRLDQI AGFVSLLKQY STQEELKQAI VGQVVEKSHG LFLLARLHMD
LLSRCNDAPL LQRALLHLPD SLYDAYAESM KQLASHNLYA SRCIFWTLYT CRPLTVAELK
TAVFFEPQNG VAQKEPSSFE NILLVETAGL LEVDPMTGTV HLIHQTAREY LTGAVARVFF
PTARKHLAET CLTVIMPDEV VDDCYMNQGT TSRNSKGSLH SYAATYWGYH AQEASEEEQT
TQVLIGAFIN KLCWRRPPVL QDYISETMGI PQQLGLGKYF ADWTALHVLA FFGITGKAKR
LIEKGADVNA RDNQLGITPL HCAAHRGNEE MVELLLDYKA EINAICKNGN TAMHYAAEQG
KRKVIKILQA RRASSRVVNR QGLTALHSAI GTAYDEATVP LLIKTRSDMD YPNVITGDTA
LHIAIELRRQ RIVLFLLEKG ANPNVPNNKG LTPLQLAAKT DNCEALSVLL ERSAKVEVRS
MLGSRALHLA ASEGNWIAFD ILLIGGADIN AWSDNGESLL HEQSRKASDT AIASHLLEHG
ANLETRTSQG YTPLQCAAMS GNKAMFFFLL ARGAKVDVET PKGETFLHIT SPSNQESLDI
LKSLLELGLD VKATCSNGWT PLHQTVFMGT GAPDIEFDKT SEYIKLLLSH GADINAAALS
ATGETPLHLA TIAPMPRPSL VSLLIDLGAS VNTITHEGKT PLHLAAAQGC ESIFRVLLGA
GADTKIKIPT SSVENEDGGG GQTPLDIAHK HPIGALWFDD MGNLQFSAED PQRSSLATAT
TIEIGSDSET DDDMRGSTLV GEEGSHWGST LSSQIIPSTL SSQVISIIE
//
