ID   A0A2J6QJ23_9HELO        Unreviewed;      1197 AA.
AC   A0A2J6QJ23;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   13-SEP-2023, entry version 20.
DE   RecName: Full=Dilute domain-containing protein {ECO:0000259|PROSITE:PS51126};
GN   ORFNames=NA56DRAFT_668127 {ECO:0000313|EMBL:PMD26252.1};
OS   Hyaloscypha hepaticicola.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Hyaloscyphaceae; Hyaloscypha.
OX   NCBI_TaxID=2082293 {ECO:0000313|EMBL:PMD26252.1, ECO:0000313|Proteomes:UP000235672};
RN   [1] {ECO:0000313|EMBL:PMD26252.1, ECO:0000313|Proteomes:UP000235672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 7357 {ECO:0000313|EMBL:PMD26252.1,
RC   ECO:0000313|Proteomes:UP000235672};
RG   DOE Joint Genome Institute;
RA   Martino E., Morin E., Grelet G., Kuo A., Kohler A., Daghino S., Barry K.,
RA   Choi C., Cichocki N., Clum A., Copeland A., Hainaut M., Haridas S.,
RA   Labutti K., Lindquist E., Lipzen A., Khouja H.-R., Murat C., Ohm R.,
RA   Olson A., Spatafora J., Veneault-Fourrey C., Henrissat B., Grigoriev I.,
RA   Martin F., Perotto S.;
RT   "A degradative enzymes factory behind the ericoid mycorrhizal symbiosis.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the allantoicase family.
CC       {ECO:0000256|ARBA:ARBA00009242}.
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DR   EMBL; KZ613468; PMD26252.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2J6QJ23; -.
DR   STRING; 1745343.A0A2J6QJ23; -.
DR   OrthoDB; 1359946at2759; -.
DR   Proteomes; UP000235672; Unassembled WGS sequence.
DR   GO; GO:0004037; F:allantoicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000256; P:allantoin catabolic process; IEA:InterPro.
DR   CDD; cd15473; Myo5p-like_CBD_DIL_ANK; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR   HAMAP; MF_00813; Allantoicase; 1.
DR   InterPro; IPR005164; Allantoicase.
DR   InterPro; IPR015908; Allantoicase_dom.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR002710; Dilute_dom.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR037986; Myo5p-like_CBD_DIL.
DR   NCBIfam; TIGR02961; allantoicase; 1.
DR   PANTHER; PTHR16027; DILUTE DOMAIN-CONTAINING PROTEIN YPR089W; 1.
DR   PANTHER; PTHR16027:SF6; DILUTE DOMAIN-CONTAINING PROTEIN YPR089W; 1.
DR   Pfam; PF03561; Allantoicase; 2.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF01843; DIL; 1.
DR   SMART; SM00248; ANK; 3.
DR   SMART; SM01132; DIL; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 1.
DR   PROSITE; PS51126; DILUTE; 1.
PE   3: Inferred from homology;
KW   ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW   Reference proteome {ECO:0000313|Proteomes:UP000235672}.
FT   REPEAT          544..576
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          767..1062
FT                   /note="Dilute"
FT                   /evidence="ECO:0000259|PROSITE:PS51126"
FT   REGION          374..412
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          874..895
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1065..1109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1178..1197
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        390..412
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1079..1095
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1197 AA;  133748 MW;  D97354C21F43FF51 CRC64;
     MPFESEYKLE DVAATPVPAD KIDATFRSST IDLISAALGG KVLSFSDEWF AEASNLLTPA
     PPIRQPGKMV FSGAWYDGWE TRRHNTAPFD YVVIRLGVAS GIVEGIEIDT AFFSGNHAPA
     ISVEGVFSAN DEEVIGWKGE RGNWEPILDI QECGPSQRFG WKLAVPTKKA YTHVRLNMYP
     DGGIARFRLF GHAVPVFPDD KDAILDLAAA QNGGVAISCS DQHFGVISNL ILPGRGKDMG
     DGWETSRSRG KDHVDWAIIR LGAKGTIQQL IVDTAFFRGN FPQKVQVEAL DWSGDGEPGV
     LADGWTTVVE PSKCGPDKEH EFDSLVKDMP FTHVKLIMIP DGGVKRIRVL GKRIGENKSI
     VRTTCSPPRL AMDIGDNGGD LSSGFGDEGQ FQKKRPRELP DDLPKSLDDR KSVPSHYTAE
     TEMYDAWQGQ SQFLTTPVLA KPLQFSNLSL DDNEYDDDFT TQKIGDSDTR LMEMLAAQAA
     HRDGSVHEDE DAVALNDKLS EEEKKDILQK ALNMAASNGD VERIERILKG KAKEFVDVDA
     PDEEGTTPLI YASCFGHEPV VTALLDAGAK VDNQDKNQWS ALMWAMTNRH KGIAKALLDH
     GASPEVKSSS GRTAFDLVAP DSEISGYLHD SGYHIGSVGV TDDFYNPGFS QDRFEEEMAE
     NELRRRMMME SARDLEVDLG NVGIDDQPES PEELEEEAQD FDWSRCLHDQ MFVFQESELG
     RILDIIITNM TPQRSPSQKP VPANMIFLSA RYAHYHANQD LLAKLLLTAM DKINDVVETH
     QWDMTILAFW ISNATLLLHY LKKDAGLSGS TTEFQLQLAE LINEIFILII RDAERRMDKV
     LDSAMLDHET IPGFEDITFQ NEWKIFKRKN QVKEEPAERR FRPPSPKARA KPSPRNVTSL
     LSSTLFVLDL YDIHSVITAQ ILAQLLYWLG AELFNRIMSN RKYLARTKAM QIRMNISSLE
     DWARANNRQA EHYEHGSMTS TGEMTVDAAR RHLAPVIQLL QWLQCFSSLG ADDLEALVGT
     LQQLTRLTPQ QLIHSVKHYR PEVGEKGLPK SAMKYLINLQ REAQLRKERQ RTERRRSGMP
     TTPTKQGTNG EAPDTPDSNG KPIVPNTMRP LAPDELLGEE DDAPEHLLLD PALMLPFSLP
     TSTDMLVSYG AGFGGLNRER ERKYIPTVPP EFLAKLDLNG GRAQPTYNPS DWENEDV
//