ID   MUB1_ASPOR              Reviewed;         605 AA.
AC   Q2U685;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=MYND-type zinc finger protein samB;
DE   AltName: Full=Suppressor of anucleate metulae protein B;
GN   Name=samB; ORFNames=AO090120000340;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
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; AP007166; BAE62930.1; -; Genomic_DNA.
DR   RefSeq; XP_001824063.1; XM_001824011.2.
DR   AlphaFoldDB; Q2U685; -.
DR   SMR; Q2U685; -.
DR   STRING; 510516.Q2U685; -.
DR   EnsemblFungi; BAE62930; BAE62930; AO090120000340.
DR   GeneID; 5996322; -.
DR   KEGG; aor:AO090120000340; -.
DR   VEuPathDB; FungiDB:AO090120000340; -.
DR   HOGENOM; CLU_014851_0_0_1; -.
DR   OMA; HWCVAAT; -.
DR   Proteomes; UP000006564; Chromosome 5.
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..605
FT                   /note="MYND-type zinc finger protein samB"
FT                   /id="PRO_0000393326"
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