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Database: UniProt
Entry: A0A0C9T764_PAXIN
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ID   A0A0C9T764_PAXIN        Unreviewed;       931 AA.
AC   A0A0C9T764;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=MYND-type domain-containing protein {ECO:0000259|PROSITE:PS50865};
GN   ORFNames=PAXINDRAFT_171771 {ECO:0000313|EMBL:KIJ11535.1};
OS   Paxillus involutus ATCC 200175.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Boletales; Paxilineae; Paxillaceae; Paxillus.
OX   NCBI_TaxID=664439 {ECO:0000313|EMBL:KIJ11535.1, ECO:0000313|Proteomes:UP000053647};
RN   [1] {ECO:0000313|EMBL:KIJ11535.1, ECO:0000313|Proteomes:UP000053647}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200175 {ECO:0000313|EMBL:KIJ11535.1,
RC   ECO:0000313|Proteomes:UP000053647};
RG   DOE Joint Genome Institute;
RA   Kuo A., Kohler A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA   Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA   Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA   Hua S.X.;
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000053647}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200175 {ECO:0000313|Proteomes:UP000053647};
RG   DOE Joint Genome Institute;
RG   Mycorrhizal Genomics Consortium;
RA   Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA   Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA   Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT   "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the MUB1/samB family.
CC       {ECO:0000256|ARBA:ARBA00010655}.
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DR   EMBL; KN819378; KIJ11535.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C9T764; -.
DR   HOGENOM; CLU_006990_1_0_1; -.
DR   OrthoDB; 2787008at2759; -.
DR   Proteomes; UP000053647; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 6.10.140.2220; -; 1.
DR   InterPro; IPR002893; Znf_MYND.
DR   PANTHER; PTHR47442; MYND-TYPE ZINC FINGER PROTEIN MUB1; 1.
DR   PANTHER; PTHR47442:SF1; MYND-TYPE ZINC FINGER PROTEIN MUB1; 1.
DR   Pfam; PF01753; zf-MYND; 1.
DR   SUPFAM; SSF144232; HIT/MYND zinc finger-like; 1.
DR   PROSITE; PS50865; ZF_MYND_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053647};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00134}.
FT   DOMAIN          712..754
FT                   /note="MYND-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50865"
FT   REGION          241..394
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          484..547
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          593..652
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          770..792
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          816..847
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          892..931
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        276..302
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        347..364
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        371..385
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        600..626
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   931 AA;  100400 MW;  053509FAFC5CB79E CRC64;
     MRESNFAFPA QNRACVCISS QLYDRRALDT TSPLPLFNSL HHLTYLTSTS PRIREIMTMD
     GGLERLVRML HDFCMCPPPP ENPNIIYGLS PSNSRPPKLV PTLNPPTFDK HAAYRFSLAF
     QCVVNIGVRG SESIRSRVVQ AGTLDAVGCI LEAWLANKGF AVGPNASPTG LPRESREQRL
     ARRQALAEQR QRDGAAELTR ALQRQITAEE IVQQERATGG ADITVDEDVL MVDVSVDDTP
     SDISVMPDTS SRPVYIPLSR PGRPTYHRSL SSRETDPHTS TETSTNATPS SGTPTTGIVN
     GRERSGTIIA RPVWGEPSGT NGTLRPRLPR TRIRMTASPD ESTDNSRPET ETEDDGDADV
     DMEQSHDTDD TTPSSHATLR APRVPTRTMT QRPRRVVGIM ADAPETAASE VNVDAHIIIN
     HGQGGVVDSE GVGVVGVEAG IVSLEPNDDF AMGAPPGAPG AMDETVPARN MHGVDVPLLD
     RRTRTAPDAT PRATVIALPP SGAVNAPGGA TMRGGATGPA RGDHASTLPG PTALGPSHVH
     HHRDTDSGPF KDEDVLLSLQ LLAYLSKYPH VRQAFYKLRL SFHPAAANLP ADPTAQQPVA
     GPSAVRSTVP ASAQPTKETH GFFRAFTSSS ARGKEKEKAP ITSPSSTPTP PLRMTNVFSL
     VERFTFRPSS SDNDLPHPPP KLPPEIQYWA GVIMRNACRK DDNRGGIRQC ANMLCGKWET
     YPREFAKCRR CRKAKYCGKE CQSNAWSEGH RFWCSAKDGD EAEYPGHADH FHGGDGTGPD
     AGAAARAERR AERERLARER AGGGGLIPVN PVHLPPHSNA PLPPPVQPTR QRVSALPPTQ
     PVPPLLPLPM PAFMRNRRRA ETVSGAPSAA GLTSPGRPMY RHEIAWLADG RGRDAHEGAG
     GGAPGPAHPH AQLPNMMWEP PTQGDNDMVL G
//
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