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Database: UniProt
Entry: A0A2G7GA82_9EURO
LinkDB: A0A2G7GA82_9EURO
Original site: A0A2G7GA82_9EURO 
ID   A0A2G7GA82_9EURO        Unreviewed;       605 AA.
AC   A0A2G7GA82;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=MYND-type zinc finger protein samB {ECO:0000256|ARBA:ARBA00019873};
DE   AltName: Full=Suppressor of anucleate metulae protein B {ECO:0000256|ARBA:ARBA00031540};
GN   ORFNames=AARAC_006880 {ECO:0000313|EMBL:PIG89525.1}, BDV24DRAFT_124995
GN   {ECO:0000313|EMBL:KAE8345887.1};
OS   Aspergillus arachidicola.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=656916 {ECO:0000313|EMBL:PIG89525.1, ECO:0000313|Proteomes:UP000231358};
RN   [1] {ECO:0000313|EMBL:PIG89525.1, ECO:0000313|Proteomes:UP000231358}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 117610 {ECO:0000313|EMBL:PIG89525.1,
RC   ECO:0000313|Proteomes:UP000231358};
RA   Moore G., Beltz S.B., Mack B.M.;
RT   "Genome sequence for an aflatoxigenic pathogen of Argentinian peanut,
RT   Aspergillus arachidicola.";
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KAE8345887.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CBS 117612 {ECO:0000313|EMBL:KAE8345887.1};
RG   DOE Joint Genome Institute;
RA   Kjaerbolling I., Vesth T., Frisvad J.C., Nybo J.L., Theobald S.,
RA   Kildgaard S., Isbrandt T., Kuo A., Sato A., Lyhne E.K., Kogle M.E.,
RA   Wiebenga A., Kun R.S., Lubbers R.J., Makela M.R., Barry K., Chovatia M.,
RA   Clum A., Daum C., Haridas S., He G., LaButti K., Lipzen A., Mondo S.,
RA   Riley R., Salamov A., Simmons B.A., Magnuson J.K., Henrissat B.,
RA   Mortensen U.H., Larsen T.O., Devries R.P., Grigoriev I.V., Machida M.,
RA   Baker S.E., Andersen M.R.;
RT   "Friends and foes A comparative genomics study of 23 Aspergillus species
RT   from section Flavi.";
RL   Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|ARBA:ARBA00025097}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the MUB1/samB family.
CC       {ECO:0000256|ARBA:ARBA00010655}.
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DR   EMBL; ML737118; KAE8345887.1; -; Genomic_DNA.
DR   EMBL; NEXV01000053; PIG89525.1; -; Genomic_DNA.
DR   OrthoDB; 2787008at2759; -.
DR   Proteomes; UP000231358; Unassembled WGS sequence.
DR   Proteomes; UP000325558; 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   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; PS50865; ZF_MYND_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000231358};
KW   Sporulation {ECO:0000256|ARBA:ARBA00022969};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00134}.
FT   DOMAIN          560..601
FT                   /note="MYND-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50865"
FT   REGION          133..181
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          194..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        194..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"
SQ   SEQUENCE   605 AA;  67652 MW;  951A3AB1AD846489 CRC64;
     MREVNFSIPN VNKASVNITT TLYDRRALDC TSTLPLINSL NHLAYLTTSS ARIRDILTVD
     GGIERLVCIL KEGRSRDLME MWKWSLAFQC VVNIGVRGSE SVRTRVVEAD MVPVIATILD
     NYIKVVDKAR ARADSENQRH SSRHHPKAAP AAGDVTGRPS FPDQSSNSEQ RTSRRQAPPP
     SIEIPAFLHQ NTNAPDANAM DVTSSPRAPM TSPPERSTFG QEAHIHRSHD GRHLHTGHRH
     RAMQPLATAL PPMDTADGFG LRPVRDTERL PSMLPTLHNG ITSQPDSPTT PNGPVQPRSH
     VQTSAARQRP TLRQQQSASG DSDDGNGEGS TLGDNAGSAE TSEPIVGLQN EMEIDEVSDR
     QTMIDGVSNS HDLTVTDPSE GQEAETFNIS HRSTVDGSII NNDTTQTNTA LGLSPTQAAN
     NANSPALVPS PYTLYFRDRS AVPQNVLTTM PRDEDVLMSL QLLAYVSKYC NLRSYFQHSH
     LVPKLKVDRE LQMLEEGASP IEPPEEEEEY MLPDDVNIFP LVEKFTVRHH SKDMQYWACV
     VMRNLCRKDE SRGGIRQCAY YKCGKWEEFQ RQFAKCRRCR RTKYCSKDCQ KAAWVYHRHW
     CHTTP
//
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