ID   MUB1_ASPCL              Reviewed;         597 AA.
AC   A1CBG9;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=MYND-type zinc finger protein samB;
DE   AltName: Full=Suppressor of anucleate metulae protein B;
GN   Name=samB; ORFNames=ACLA_015250;
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
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; DS027049; EAW13087.1; -; Genomic_DNA.
DR   RefSeq; XP_001274513.1; XM_001274512.1.
DR   AlphaFoldDB; A1CBG9; -.
DR   SMR; A1CBG9; -.
DR   STRING; 5057.CADACLAP00000739; -.
DR   PRIDE; A1CBG9; -.
DR   EnsemblFungi; EAW13087; EAW13087; ACLA_015250.
DR   GeneID; 4706354; -.
DR   KEGG; act:ACLA_015250; -.
DR   VEuPathDB; FungiDB:ACLA_015250; -.
DR   eggNOG; ENOG502QTM3; Eukaryota.
DR   HOGENOM; CLU_014851_0_0_1; -.
DR   OMA; HWCVAAT; -.
DR   OrthoDB; 1167239at2759; -.
DR   Proteomes; UP000006701; 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..597
FT                   /note="MYND-type zinc finger protein samB"
FT                   /id="PRO_0000393321"
FT   ZN_FING         552..593
FT                   /note="MYND-type; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT   REGION          133..230
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          268..287
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          292..341
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        158..177
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        179..203
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        211..228
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        299..328
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         568
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT   BINDING         571
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT   BINDING         589
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT   BINDING         593
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
SQ   SEQUENCE   597 AA;  66569 MW;  D53AEDCF59D76CD0 CRC64;
     MREVNFSIPN VNKASVNITT TLYDRRALDC TSTLPLINSL NHLAYLTTSS ARIRDILTVD
     GGIERLVCIL KEGRSGDLME MWKWSLAFQC VVNIGVRGSE SVRTRVVEAD MVPVIATILD
     NYIKVVDKAR ARADSESHKQ SSRHHPKSVP APSDSSGRPA FLEQSSASEN RTSRRQAPPP
     SIEIPPQPLF IDVTSPPRVP MTSPPERSTF GQDVHNHRTN DTRYAHPSHR HRTMQPLATA
     LPPMDTADGF GLRPVRDNER LPSMLPALHT GLTSQPDSPT TPNAPVQPRS IAQATHARHR
     PSLRQQLSAS GESDDGNGES STMEDESTPA ETAEPIVGLQ NRMDIDDVGN REAIIGGVSE
     SHDLTVTDPS EGQEAETFNI THRSTVDGSM INTDNAQNNA ALGLSPAQAA DTATSPALVP
     SPYSLYFRDR STAAAQGVLT TMPRDEDVLM SLQLLAYVSK YCNLRSYFQN SHFVPKLKID
     RELQMLEEGT SPIEPAEEED EYLLPDDVNI FPLVEKFTVR HHSKDMQYWA CVVMRNLCRK
     DEARGGIRQC AYYKCGKWEE TARQFAKCRR CRRTKYCSKD CQKAAWVYHR HWCHSTP