ID   MUB1_ASPTN              Reviewed;         603 AA.
AC   Q0CW83;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=MYND-type zinc finger protein samB;
DE   AltName: Full=Suppressor of anucleate metulae protein B;
GN   Name=samB; ORFNames=ATEG_02051;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) 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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the MUB1/samB family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CH476596; EAU37013.1; -; Genomic_DNA.
DR   RefSeq; XP_001211229.1; XM_001211229.1.
DR   AlphaFoldDB; Q0CW83; -.
DR   SMR; Q0CW83; -.
DR   STRING; 341663.Q0CW83; -.
DR   EnsemblFungi; EAU37013; EAU37013; ATEG_02051.
DR   GeneID; 4316474; -.
DR   VEuPathDB; FungiDB:ATEG_02051; -.
DR   eggNOG; ENOG502QTM3; Eukaryota.
DR   HOGENOM; CLU_014851_0_0_1; -.
DR   OMA; HWCVAAT; -.
DR   OrthoDB; 1167239at2759; -.
DR   Proteomes; UP000007963; 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   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR002893; Znf_MYND.
DR   Pfam; PF01753; zf-MYND; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
DR   PROSITE; PS01360; ZF_MYND_1; 1.
DR   PROSITE; PS50865; ZF_MYND_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Metal-binding; Reference proteome; Sporulation; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..603
FT                   /note="MYND-type zinc finger protein samB"
FT                   /id="PRO_0000393327"
FT   ZN_FING         558..599
FT                   /note="MYND-type; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT   REGION          133..239
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          269..347
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          361..398
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        195..218
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        275..325
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        376..398
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         574
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT   BINDING         577
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT   BINDING         595
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT   BINDING         599
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
SQ   SEQUENCE   603 AA;  67609 MW;  52EEFE80924D5846 CRC64;
     MREVNFSIPN VNKASVNITT TLYDRRALDC TSTLPLINSL NHLAYLTTSS ARIRDILTVD
     GGIERLVCIL KEGRSRDLME MWKWSLAFQC VVNIGVRGSE SVRTRVVEAD MVPVIATILD
     NYIKVVDKAR ARADPDTQRH SSRHHAKPVP TAGEPSARPS LLEQAAHTEQ RASRRQAPPP
     NIEIPPYFQD NHVADSNAMD ISSSPRAPMT SPPERSTFGQ EAHNHRTHDP RYLHPGHRQR
     AMQPLATALP PMDAADGFGL RPVRDTERLP SMLPGLQNGI TSQPDSPTTP SGPIQARNNA
     ATTVPVQRPT LRQQRSASGD SDDGNAESFS MEDGARSEAT SEPIVQNQME IDEVGDRQAM
     LNGVSDGHDL TVTDPSEGQE AETFNITHRS TVDGSTINNG NTQTNTALGL SPAQAANTTN
     SPNIVPSPYS LYFRDRSATA SQNVLTTMPR DEDVLMSLQL LAYVSKYCNL RSYFQNSHFV
     PKLKVDRELQ MFEDGSSPME TAEEEDEYLL PDDVNIFPLV EKFTVRHHSK DMQYWACVVM
     RNLCRKDESR GGIRQCAYYK CGKWEEFQRQ FAKCRRCRRT KYCSKDCQKA AWVYHRHWCH
     TTP