ID MUB1_ASPFN Reviewed; 605 AA.
AC B8NKS1;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=MYND-type zinc finger protein samB;
DE AltName: Full=Suppressor of anucleate metulae protein B;
GN Name=samB; ORFNames=AFLA_093250;
OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS / JCM 12722 / SRRC 167).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=332952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC 167;
RX PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT aflatoxin contamination of food and feed.";
RL Genome Announc. 3:E0016815-E0016815(2015).
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}.
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DR EMBL; EQ963480; EED49244.1; -; Genomic_DNA.
DR RefSeq; XP_002381145.1; XM_002381104.1.
DR AlphaFoldDB; B8NKS1; -.
DR SMR; B8NKS1; -.
DR EnsemblFungi; EED49244; EED49244; AFLA_093250.
DR VEuPathDB; FungiDB:AFLA_009560; -.
DR eggNOG; ENOG502QTM3; Eukaryota.
DR HOGENOM; CLU_014851_0_0_1; -.
DR OMA; QDMQYWA; -.
DR OrthoDB; 2787008at2759; -.
DR Proteomes; UP000001875; 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:1900735; P:positive regulation of flocculation; IEA:EnsemblFungi.
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; PS01360; ZF_MYND_1; 1.
DR PROSITE; PS50865; ZF_MYND_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Metal-binding; Sporulation; Zinc; Zinc-finger.
FT CHAIN 1..605
FT /note="MYND-type zinc finger protein samB"
FT /id="PRO_0000393323"
FT ZN_FING 560..601
FT /note="MYND-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT REGION 133..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 274..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..345
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 576
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 579
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 597
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 601
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
SQ SEQUENCE 605 AA; 67684 MW; F0712AA9CE4E06E2 CRC64;
MREVNFSIPN VNKASVNITT TLYDRRALDC TSTLPLINSL NHLAYLTTSS ARIRDILTVD
GGIERLVCIL KEGRSRDLME MWKWSLAFQC VVNIGVRGSE SVRTRVVEAD MVPVIATILD
NYIKVVDKAR ARADSENQRH SSRHHPKAAP AAGDVTGRPS FPDQSSNSEQ RTSRRQAPPP
SIEIPAFLHQ NTNAPDTNAM DVTSSPRAPM TSPPERSTFG QEAHIHRSHD GRHLHTGHRH
RAMQPLATAL PPMDTADGFG LRPVRDTERL PSMLPTLHNG ITSQPDSPTT PNGPVQPRSH
AQTSAARQRP TLRQQQSASG DSDDGNGEGS TLGDNAGSAE TSEPIVGLQN EMEIDEVSDR
QTMIDGVSNS HDLTVTDPSE SQEAETFNIS HRSTVDGSII NNDTTQTNTA LGLSPTQAAN
NANSPALVPS PYTLYFRDRS AVPQNVLTTM PRDEDVLMSL QLLAYVSKYC NLRSYFQHSH
LVPKLKVDRE LQMLEEGASP IEPPEEEEEY MLPDDVNIFP LVEKFTVRHH SKDMQYWACV
VMRNLCRKDE SRGGIRQCAY YKCGKWEEFQ RQFAKCRRCR RTKYCSKDCQ KAAWVYHRHW
CHTTP
//
