ID   A0A397GMX6_9EURO        Unreviewed;       606 AA.
AC   A0A397GMX6;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=MYND-type zinc finger protein samB {ECO:0000256|ARBA:ARBA00019873};
DE   AltName: Full=Suppressor of anucleate metulae protein B {ECO:0000256|ARBA:ARBA00031540};
GN   ORFNames=CDV56_106746 {ECO:0000313|EMBL:RHZ52225.1};
OS   Aspergillus thermomutatus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=41047 {ECO:0000313|EMBL:RHZ52225.1, ECO:0000313|Proteomes:UP000215305};
RN   [1] {ECO:0000313|EMBL:RHZ52225.1, ECO:0000313|Proteomes:UP000215305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HMR AF 39 {ECO:0000313|EMBL:RHZ52225.1,
RC   ECO:0000313|Proteomes:UP000215305};
RA   Parent-Michaud M., Dufresne P.J., Fournier E., Martineau C., Moreira S.,
RA   Perkins V., De Repentigny L., Dufresne S.F.;
RT   "Draft genome sequence of azole-resistant Aspergillus thermomutatus
RT   (Neosartorya pseudofischeri) strain HMR AF 39, isolated from a human nasal
RT   aspirate.";
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in determination of the onset of polarized growth
CC       and morphogenesis. Plays a role in the regulation of branching in
CC       hyphae and spore formation. {ECO:0000256|ARBA:ARBA00025097}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the MUB1/samB family.
CC       {ECO:0000256|ARBA:ARBA00010655}.
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:RHZ52225.1}.
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DR   EMBL; NKHU02000138; RHZ52225.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A397GMX6; -.
DR   VEuPathDB; FungiDB:CDV56_106746; -.
DR   OrthoDB; 2787008at2759; -.
DR   Proteomes; UP000215305; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   Gene3D; 6.10.140.2220; -; 1.
DR   InterPro; IPR016024; ARM-type_fold.
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; SSF48371; ARM repeat; 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:UP000215305};
KW   Sporulation {ECO:0000256|ARBA:ARBA00022969};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00134}.
FT   DOMAIN          561..602
FT                   /note="MYND-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50865"
FT   REGION          133..188
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          201..224
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          259..356
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        144..177
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        277..326
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   606 AA;  67905 MW;  7950477FB60C2D3D CRC64;
     MREVNFSIPN VNKASVNITT TLYDRRALDC TSTLPLINSL NHLAYLTTSS ARIRDILTVD
     GGIERLVCIL KEGRSRDLME MWKWSLAFQC VVNIGVRGSE SVRTRVVEAD MVPVIATILD
     NYIKVVDKAR ARADSESQRQ SSRHHSKPVS TSNDASGRSS FLGQSSTAEQ RTSRRQAPPP
     SIEIPPQPFF QENHVADSNV LDVTSPPRVP MTSPPERSTF GQDVHHHRTN DGRFAHANHR
     HRMQPLATAL PSMDAADGFG LRPVRDNERL PSMLPGFHTG LTSQPDSPTT PNAPVQPRSS
     AQDTIARQRP SLRQQQSASG ESDDGNGEGS TMDDDPASTD AAEPIVGLQN RMDIDDVGER
     DTILGGVSDS HDLTVTDPSE EQEAETFNIT HRSTVDGSMI NTDNAQNNAT LGLSPAQAAD
     NANSPALVPS PYSLYFRDRT ATAAHGVLTT MPRDEDVLMS LQLLAYVSKY CNLRSYFQHS
     HFVPKLKIDR ELQMLEEGTS PIELPEEEDE YLLPDDVNIF PLVEKFTVRH HSKDMQYWAC
     VVMRNLCRKD ESRGGIRQCA YYKCGKWEEF QRQFAKCRRC RRTKYCSKDC QKAAWVYHRH
     WCHTTP
//