ID   MUB1_ASPFC              Reviewed;         605 AA.
AC   B0Y1D1;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=MYND-type zinc finger protein samB;
DE   AltName: Full=Suppressor of anucleate metulae protein B;
GN   Name=samB; ORFNames=AFUB_059860;
OS   Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus
OS   fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=451804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CEA10 / CBS 144.89 / FGSC A1163;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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; DS499597; EDP51961.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0Y1D1; -.
DR   SMR; B0Y1D1; -.
DR   EnsemblFungi; EDP51961; EDP51961; AFUB_059860.
DR   VEuPathDB; FungiDB:AFUB_059860; -.
DR   HOGENOM; CLU_014851_0_0_1; -.
DR   PhylomeDB; B0Y1D1; -.
DR   Proteomes; UP000001699; 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; Sporulation; Zinc; Zinc-finger.
FT   CHAIN           1..605
FT                   /note="MYND-type zinc finger protein samB"
FT                   /id="PRO_0000393322"
FT   ZN_FING         560..601
FT                   /note="MYND-type; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT   REGION          134..187
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          203..352
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        144..174
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        276..325
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;  67948 MW;  E984934B9B7140F9 CRC64;
     MREVNFSIPN VNKASVNITT TLYDRRALDC TSTLPLINSL NHLAYLTTSS ARIRDILTVD
     GGIERLVCIL KEGRSRDLME MWKWSLAFQC VVNIGVRGSE SVRTRVVEAD MVPVIATILD
     NYIKVVDKAR ARADSESQRQ SSRHHSKAVP TSNDVSGRPS FLEQPLTAEQ RTSRRHAPPS
     IEIPPQPFFQ ENHVADSNVL DVTSPSRVPM TSPPERSAFG QDVHHRRTND GRFAHGNHRH
     RMQPLATALP SMDATDGFGL RPVRDNERLP SMLPGFHTGL TSQPDSPTTP NAPVQPRSSA
     QATIARQRPS LRQQQSASGE SDDGNGDGST MDEDPASTEA AEPIVGLQNR MDIDDVGDRD
     TILGGVSDSH DLTVTDPSEE QEAETFNITH RSTVDGSMIN TDNAQNNAAL GLSPTQAADN
     ANSPALVPSP YSLYFRDRTT TAAHGVLTTM PRDEDVLMSL QLLAYVSKYC NLRSYFQHSH
     FVPKLKIDRE LQMLEEGTSP IEFPEDEDEY LLPDDVNIFP LVEKFTVRHH SKDMQYWACV
     VMRNLCRKDE SRGGIRQCAY YKCGKWEEFQ RQFAKCRRCR RTKYCSKDCQ KAAWVYHRHW
     CHTTP