ID   MUB1_NEOFI              Reviewed;         606 AA.
AC   A1DDX0;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=MYND-type zinc finger protein samB;
DE   AltName: Full=Suppressor of anucleate metulae protein B;
GN   Name=samB; ORFNames=NFIA_075020;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC   / WB 181;
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}.
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DR   EMBL; DS027696; EAW17577.1; -; Genomic_DNA.
DR   RefSeq; XP_001259474.1; XM_001259473.1.
DR   AlphaFoldDB; A1DDX0; -.
DR   SMR; A1DDX0; -.
DR   STRING; 36630.CADNFIAP00007966; -.
DR   EnsemblFungi; EAW17577; EAW17577; NFIA_075020.
DR   GeneID; 4586154; -.
DR   KEGG; nfi:NFIA_075020; -.
DR   VEuPathDB; FungiDB:NFIA_075020; -.
DR   eggNOG; ENOG502QTM3; Eukaryota.
DR   HOGENOM; CLU_014851_0_0_1; -.
DR   OMA; HWCVAAT; -.
DR   OrthoDB; 1167239at2759; -.
DR   Proteomes; UP000006702; 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..606
FT                   /note="MYND-type zinc finger protein samB"
FT                   /id="PRO_0000393329"
FT   ZN_FING         561..602
FT                   /note="MYND-type; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT   REGION          134..188
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          203..225
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          262..353
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          365..384
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        277..326
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         577
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT   BINDING         580
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT   BINDING         598
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT   BINDING         602
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
SQ   SEQUENCE   606 AA;  67926 MW;  010D3E5E6ED23D96 CRC64;
     MREVNFSIPN VNKASVNITT TLYDRRALDC TSTLPLINSL NHLAYLTTSS ARIRDILTVD
     GGIERLVCIL KEGRSRDLME MWKWSLAFQC VVNIGVRGSE SVRTRVVEAD MVPVIATILD
     NYIKVVDKAR ARADSESQRQ SSRHHSKAVP TSNDASGRSS FLEQSSTAEQ RTSRRHAPPP
     SIEIPPQPFF QENHVADSNV LDVASPPRVP MTSPPERSTF GQDVHHHRTN EGRFAHGNHR
     HRMQPLATAL PSMDAADGFG LRPVRDNERL PSMLPGFHTG LTSQPDSPTT PNAPVQPRSS
     AQATIARQRP SLRQQQSASG ESDDGNGDGS TMDEDPASTE AAEPIVGLQN RMDIDDVGER
     DTILGGVSDS HDLTVTDPSE EQEAETFNIT HRSTVDGSMI NTDNAQNNAA LGLSPTQAAD
     NANSPALVPS PYSLYFRDRT TTAAHGVLTT MPRDEDVLMS LQLLAYVSKY CNLRSYFQHS
     HFVPKLKIDR ELQMLEEGTS PIDLPEEEDE YLLPDDVNIF PLVEKFTVRH HSKDMQYWAC
     VVMRNLCRKD ESRGGIRQCA YYKCGKWEEF QRQFAKCRRC RRTKYCSKDC QKAAWVYHRH
     WCHTTP