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Database: UniProt
Entry: A0A395MGE6_9HYPO
LinkDB: A0A395MGE6_9HYPO
Original site: A0A395MGE6_9HYPO 
ID   A0A395MGE6_9HYPO        Unreviewed;      1242 AA.
AC   A0A395MGE6;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Ankyrin repeat protein {ECO:0000313|EMBL:RFN46936.1};
GN   ORFNames=FIE12Z_8823 {ECO:0000313|EMBL:RFN46936.1};
OS   Fusarium flagelliforme.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium incarnatum-equiseti species complex.
OX   NCBI_TaxID=2675880 {ECO:0000313|EMBL:RFN46936.1, ECO:0000313|Proteomes:UP000265631};
RN   [1] {ECO:0000313|EMBL:RFN46936.1, ECO:0000313|Proteomes:UP000265631}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 13405 {ECO:0000313|EMBL:RFN46936.1,
RC   ECO:0000313|Proteomes:UP000265631};
RX   PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA   Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA   Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA   Busman M., Gutierrez S.;
RT   "Evolution of structural diversity of trichothecenes, a family of toxins
RT   produced by plant pathogenic and entomopathogenic fungi.";
RL   PLoS Pathog. 14:e1006946-e1006946(2018).
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:RFN46936.1}.
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DR   EMBL; PXXK01000278; RFN46936.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A395MGE6; -.
DR   STRING; 2594813.A0A395MGE6; -.
DR   Proteomes; UP000265631; Unassembled WGS sequence.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 3.
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; IPR003593; AAA+_ATPase.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
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; PF13401; AAA_22; 1.
DR   Pfam; PF12796; Ank_2; 3.
DR   PRINTS; PR01415; ANKYRIN.
DR   SMART; SM00248; ANK; 8.
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; 4.
DR   PROSITE; PS50088; ANK_REPEAT; 5.
PE   4: Predicted;
KW   ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265631}.
FT   DOMAIN          444..572
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|Pfam:PF13401"
FT   REPEAT          871..903
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          904..937
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          1043..1069
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          1076..1096
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          1111..1152
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1242 AA;  141070 MW;  5F8F58E1CEC4EF76 CRC64;
     MAWDTSSSMD ESQDTTGERE AEVYLPPEKY TVGWICALRC ELKAARTMLD EEHVALRVQS
     EQDGNNYLLG RIGPHNVAIT SLPQAGNNRG ATAAKSMQTT FPNMKFCLMV GVGGGVPSKD
     PSWNDVRLGD IVVSEPTENS GGVIQYDMGK REIGGFVRRG TLNKPPGLLL AAMKTLHTTK
     NLSKGISDLV NDKLGDEEDP EEEWTYPKRA KDVLFNTDHY QTTKSTDLLV ACGAALLLPA
     TYLQVWREDY ENRRSGFLWY LRYKPVRRTP RSTNTPRIHY GNIGSGNSVV KNAVERDELA
     KRDNVVCFEM EAAGIMDDFP CLVIRGISDY ADSYKRWDWQ PYAAAVAAAY GKKLLLTISP
     IGVQGMKAIG QIKHGVQRID RRTKRLVRNQ ELQDEEKFLN WLAPIDHGSK HRDVLRQRQA
     ETGQWVLESE KFQKWLCASK PETLLCPGMP GAGKTFIAAT IIDHLQQRFR DDTNIAVVYI
     YCDFDRQNEQ TADNLIATLV KQLARLRPGT LSRLYQDHQR NQTRPSWEEM LKTLHTVAAT
     YTKIFLVVDA VDECQDYGTR KRFLQAIFDL QAQTRTNILG TSRHDTKIQQ KFQNSAVLEI
     HARNQDIERY IDGNMHKLPD FVENNLGLCS KIKKEIIARV DGMFLLATLY LNLLIGQISE
     NDLMEVSSML PTGGKAYDET YDRCMERIER QIGKRRDLAK KLLAWVTCAE RPLKESELEH
     ALAVKIGQSS LDKGDIPQEM VEVCAGLVRI DHESREIRLV HFTTKEYFRR TQERWFPEAQ
     YVIAMTCITY LGFDTFQSGI CETEREMEAR IRTNPFYYYA ANYWDQHARH ISQIQQDIAL
     RFLTDSAKIE AYAQAMYATR NGRFIPWRDN RGKTGLHLVA DCGLNNFAEI LLQAGCELNT
     RDETEMTPLS IAATRGWTDI VRRLLMEKNV DVNAIDMNTR TPRTPLNIAA WQGHHSVVKK
     LLKHPAIEIN FHQDSHGTAL SIAAEKGHVE TVNLLLKERN IDVNAREFYG QTALARAARA
     GKDEVVGLLL TAVDVDIDHV NCIGRTALML ASSEGNVAIT KRLLEHGADW KKQCSFGKTA
     LHVAAHGGHL EIVKLLATEK YRVILDIQDR DGRTALHLAS WVSPWNRKRG KLGKDIVEIL
     LANGADSRVK TFSGETAKDI AASRKKWGRH VQWNPARWKR LPNRYIEGRN GHGYVATEEP
     GDVWQNSQYD GNNSTYYDIY QQNTGRFRTR NEEALCRAFT RR
//
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