ID   A0A2I1FZK0_9GLOM        Unreviewed;      1162 AA.
AC   A0A2I1FZK0;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=MYND-type domain-containing protein {ECO:0000259|PROSITE:PS50865};
GN   ORFNames=RhiirA4_393943 {ECO:0000313|EMBL:PKY39802.1};
OS   Rhizophagus irregularis.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC   Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX   NCBI_TaxID=588596 {ECO:0000313|EMBL:PKY39802.1, ECO:0000313|Proteomes:UP000234323};
RN   [1] {ECO:0000313|EMBL:PKY39802.1, ECO:0000313|Proteomes:UP000234323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A4 {ECO:0000313|EMBL:PKY39802.1,
RC   ECO:0000313|Proteomes:UP000234323};
RA   Ropars J., Sedzielewska K., Noel J., Charron P., Farinelli L., Marton T.,
RA   Kruger M., Pelin A., Brachmann A., Corradi N.;
RT   "Genome analyses suggest a sexual origin of heterokaryosis in a supposedly
RT   ancient asexual fungus.";
RL   Submitted (OCT-2015) 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:PKY39802.1}.
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DR   EMBL; LLXI01000077; PKY39802.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2I1FZK0; -.
DR   VEuPathDB; FungiDB:FUN_013502; -.
DR   VEuPathDB; FungiDB:GLOIN_2v1662028; -.
DR   VEuPathDB; FungiDB:RhiirA1_410860; -.
DR   OrthoDB; 5474570at2759; -.
DR   Proteomes; UP000234323; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 6.10.140.2220; -; 2.
DR   Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 2.
DR   InterPro; IPR039448; Beta_helix.
DR   InterPro; IPR027974; DUF4470.
DR   InterPro; IPR006626; PbH1.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   InterPro; IPR002893; Znf_MYND.
DR   PANTHER; PTHR10237:SF13; DEFORMED EPIDERMAL AUTOREGULATORY FACTOR 1 HOMOLOG; 1.
DR   PANTHER; PTHR10237; DEFORMED EPIDERMAL AUTOREGULATORY FACTOR 1 HOMOLOG SUPPRESSIN; 1.
DR   Pfam; PF13229; Beta_helix; 2.
DR   Pfam; PF14737; DUF4470; 1.
DR   Pfam; PF01753; zf-MYND; 2.
DR   SMART; SM00710; PbH1; 7.
DR   SUPFAM; SSF144232; HIT/MYND zinc finger-like; 2.
DR   SUPFAM; SSF51126; Pectin lyase-like; 1.
DR   PROSITE; PS01360; ZF_MYND_1; 2.
DR   PROSITE; PS50865; ZF_MYND_2; 2.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000234323};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00134}.
FT   DOMAIN          1030..1071
FT                   /note="MYND-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50865"
FT   DOMAIN          1115..1157
FT                   /note="MYND-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50865"
SQ   SEQUENCE   1162 AA;  131055 MW;  6ECFB5A5ED500318 CRC64;
     MPPICIDGRG ATLFMNKCVV SNSRNSGGIL VISDAKAKIT NCNIYDIGLN AIEVRYGSSL
     YAERNEIHHN KQGVLVWLDA NEVTLIDNII RDNYAEGIYV NGNREPAISK KHKGFLPPGF
     REEAAFEPPP TLSYTKPSQT AVILKKNRIL KSGSFGISVE QGAKLRMEEN EVATSGTTGC
     VIKGGADAYL LDNKFHHNMS HGIEIGINYK GKVVVENNHI HFNKKGNFSQ PTADTFRDSS
     IIFGIETHQL FTPIKVINNK IEDNDSNEQE FVDFNVSSNR LGMHLFYEGE PFLYAIGNTY
     GFNLLKDLDI GAAISDKSYT ATTETSVIRT TSQVKSKQVS MFLGGVGDLR NIVETVHGLM
     NSTEGQIENF SIKLLFTIND FNPTILTRDL VLLEMISRLP DPKPQPFINI KNLYSQWNKD
     FVVSVTEILS VWGEKIISSN SYNKLSSCIQ SLIEAFENNI DTSNKKSKNI SFNKKLPSWI
     SFKYSSSTAS FVLRTLRCWQ ENKLTATALN WDTKQSGYLL VGGSSPETER LEDLKKYCKV
     YEDIDKYTCC QLPISSQAQT CNNEHEILRP GARRNMVNVT MLTVPTMEYN VFRTSSIFRA
     FQVACDIPRS GEKREDSIED LTLYDHLLLT LLPKLISLRA SLRGTSSVRI QVMPLLGDVI
     DILLCHLPSS VRFNAIDCSN LADYVSLLSI LLTAAPRLKD NSPLTLQLMK LSQPPAKPMK
     EFVEERLGLS LNILARLTGI TFLNAYYQDY AVYVTWNFDI TNKVEDKLDT LMTDVISVAN
     ICCTAHINRI KGLSVNILVR LFQIMIFRFP EKTMAQLLRT LFASDGFKKH IPNFVMHLVE
     LKTFMTLHLS WSMVIRLEEF KDLKVSIGRY TLRWKTDKIE KSKIFTLTNL TGMSKVHSEA
     EIWLRLIKPV PVGNVQRRKK EGSNSTSNFS NDQEPTHYYF DSVSLSAIEA PLITITFHLP
     VSFYDSHKDW ILECNVGSET ILLASKKLKL SNATQKSVYH DTWVDVSRTG DNNETEDYLT
     EKDDKDAKVC KRCGKMSTTR TGGGRCVKCK SVFYCSKDCQ KEDWKRHKKE CNFDPVIATK
     PTLSTLTDVS ITEENNKIKD NSEVEDNETK KNDACKRCGK TSTVGAGGGL CSKCKSVFYC
     SRDCQKEDWK RHKKVDCVGH GQ
//