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Database: UniProt
Entry: A0A150UUW8_9PEZI
LinkDB: A0A150UUW8_9PEZI
Original site: A0A150UUW8_9PEZI 
ID   A0A150UUW8_9PEZI        Unreviewed;       587 AA.
AC   A0A150UUW8;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=HAUS augmin-like complex subunit 6 N-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=M433DRAFT_448513 {ECO:0000313|EMBL:KYG41883.1};
OS   Acidomyces richmondensis BFW.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Acidomyces.
OX   NCBI_TaxID=766039 {ECO:0000313|EMBL:KYG41883.1, ECO:0000313|Proteomes:UP000075602};
RN   [1] {ECO:0000313|EMBL:KYG41883.1, ECO:0000313|Proteomes:UP000075602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BFW {ECO:0000313|EMBL:KYG41883.1,
RC   ECO:0000313|Proteomes:UP000075602};
RX   PubMed=26973616; DOI=10.3389/fmicb.2016.00238;
RA   Mosier A.C., Miller C.S., Frischkorn K.R., Ohm R.A., Li Z., LaButti K.,
RA   Lapidus A., Lipzen A., Chen C., Johnson J., Lindquist E.A., Pan C.,
RA   Hettich R.L., Grigoriev I.V., Singer S.W., Banfield J.F.;
RT   "Fungi Contribute Critical but Spatially Varying Roles in Nitrogen and
RT   Carbon Cycling in Acid Mine Drainage.";
RL   Front. Microbiol. 7:238-238(2016).
CC   -!- SIMILARITY: Belongs to the ADIP family.
CC       {ECO:0000256|ARBA:ARBA00009291}.
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:KYG41883.1}.
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DR   EMBL; JPDO01000566; KYG41883.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A150UUW8; -.
DR   STRING; 766039.A0A150UUW8; -.
DR   Proteomes; UP000075602; Unassembled WGS sequence.
DR   InterPro; IPR021622; Afadin/alpha-actinin-bd.
DR   Pfam; PF11559; ADIP; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000075602}.
FT   REGION          156..208
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          341..534
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          546..568
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          70..132
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        188..207
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        350..387
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        388..408
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        443..457
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        500..519
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   587 AA;  63972 MW;  FD18C59A6AE94AA9 CRC64;
     MMDHETLRTA STYLNNLLLA RGLLRPPVAS GIDFVKPTRD ARAHTINLIH DLLLRDDRAR
     DQRDATAHLL RQLRAESTRQ AEEISRLTAR AETEARAAAQ ARAAQEKAEA EVKRLEGRVK
     ALKEEAGRLK TSLAQTKAGC ATEVRKRDLE LSRLKGHLQG QQRGGKHPGG GVGAVVGPNL
     TISGGVAERR QKQEEQQQQR DVQDPEYSLR QETNSFLTSL AQSLSEENDT LLTHLRHALH
     TLHDLLNLPA PPPCNPQPDS LAADLSRALS ALTSLLRDPN FVPLEELLER EEEIARLRAG
     WEHMEARWRD LLSLMEGWRR RMEEGGHTVD LEDLRRGIGM VSPVRRGGGE GGKNEVEDLS
     ITEEASERSA DDGDHRSSKH EVASHRRRST SASPTSPRKN NARKQLHNVF SPPSCFDLRP
     RANSNPASSP LPRAGDAAPP TSDPDSDSDS DSPPLTVAEK LQQAELAAAA AAAAAASASP
     TNKKPVPLAD RPNPPPSSKS APASDFSEPP FTQSKRSARL SFGVDGANDH EDDTLGQLVS
     AASPVQAVGA KRTKIRGRPK KRRKSTLTAE ELERLIFTGG DGADEAE
//
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