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Database: UniProt
Entry: E4ZZE9_LEPMJ
LinkDB: E4ZZE9_LEPMJ
Original site: E4ZZE9_LEPMJ 
ID   E4ZZE9_LEPMJ            Unreviewed;       907 AA.
AC   E4ZZE9;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   27-MAR-2024, entry version 55.
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=LEMA_P110090.1 {ECO:0000313|EMBL:CBX96744.1};
OS   Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8)
OS   (Blackleg fungus) (Phoma lingam).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC   Plenodomus; Plenodomus lingam/Leptosphaeria maculans species complex.
OX   NCBI_TaxID=985895 {ECO:0000313|Proteomes:UP000002668};
RN   [1] {ECO:0000313|Proteomes:UP000002668}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8
RC   {ECO:0000313|Proteomes:UP000002668};
RX   PubMed=21326234; DOI=10.1038/ncomms1189;
RA   Rouxel T., Grandaubert J., Hane J.K., Hoede C., van de Wouw A.P.,
RA   Couloux A., Dominguez V., Anthouard V., Bally P., Bourras S.,
RA   Cozijnsen A.J., Ciuffetti L.M., Degrave A., Dilmaghani A., Duret L.,
RA   Fudal I., Goodwin S.B., Gout L., Glaser N., Linglin J., Kema G.H.J.,
RA   Lapalu N., Lawrence C.B., May K., Meyer M., Ollivier B., Poulain J.,
RA   Schoch C.L., Simon A., Spatafora J.W., Stachowiak A., Turgeon B.G.,
RA   Tyler B.M., Vincent D., Weissenbach J., Amselem J., Quesneville H.,
RA   Oliver R.P., Wincker P., Balesdent M.-H., Howlett B.J.;
RT   "Effector diversification within compartments of the Leptosphaeria maculans
RT   genome affected by Repeat-Induced Point mutations.";
RL   Nat. Commun. 2:202-202(2011).
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; FP929129; CBX96744.1; -; Genomic_DNA.
DR   RefSeq; XP_003840223.1; XM_003840175.1.
DR   AlphaFoldDB; E4ZZE9; -.
DR   EnsemblFungi; CBX96744; CBX96744; LEMA_P110090.1.
DR   GeneID; 13283290; -.
DR   eggNOG; ENOG502QTM3; Eukaryota.
DR   HOGENOM; CLU_014851_0_0_1; -.
DR   InParanoid; E4ZZE9; -.
DR   OMA; QDMQYWA; -.
DR   OrthoDB; 2787008at2759; -.
DR   Proteomes; UP000002668; Genome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 6.10.140.2220; -; 1.
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; 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   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002668};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00134}.
FT   TRANSMEM        224..252
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          862..903
FT                   /note="MYND-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50865"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          416..526
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          568..629
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        461..483
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        487..512
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        568..586
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   907 AA;  99780 MW;  A1944A94E8AF7EBA CRC64;
     MAQDGRGWQS SALGEGPPSC NAQPAASPAH IHPASGQSVF LSLQPHHPPK LLPSTIHPPS
     IHHPSTNTTT TTISTITAIL LPAFPFEHYT LQNHLLHLHH HHPTLFHSTT AITSSHPSPS
     PSPVRWLPGS LALAHVLLHP VLVDEYPSRS TPLPLKWNWA DEAKQTPAPP PPPPTLLHNA
     HPRLHPALGY RRSWTDTPKT LANPRASPLT LHLPHTIVHH HHNITVIATG AAAAAAVVVV
     VVVVAVAAAF ALRPSPPSIP SVCYGTTTAS ASTAPNMREV NFSIPNANKA SVGITTALYD
     RRALDCTSTL PLINSLNHLA YLTTSSARIR DILTVDGGIE RLICILKEGR SKEMMDMWKW
     NLAFQCIFNI GVRGSENVRT RVVEADMVPV IATILDNYIK VVDKCRARAE ADLHRSGRLG
     SSNRHHSSRS GDMASSASHR ADRTRRSIPP PIEIPPTPVD SAVAENTQPL PSFSLSSPPE
     RTTFTRGRPP HHHHHHHHHH HHHHHHHHRS HEARGAGFGA VGTTSRNIGQ PLATALPSMD
     TTPDAFALRP VRDADRLPSM LPALQREITS HSQPESPTTP SAPLARQSSP RPALARTRRR
     PSIRHQLSAS GDSDLEAQQD ELSTEAVAAA GPAVSEPIVG IQNNEINMAD IVDNGELLDG
     GATPVPVAAR SEETDENNQT FNITHVPSLD GSLINPINTP PTTNALPGFT PMQPAISVIN
     ATNPPPPWYP RYTQDRNATA GVLAAMPRDE DVLMSLQLLA YVSKYCNLRT YFQKSHLVPK
     LKIGTDLQVL DGETSTPKAC RDEELEEELE EYELPDDFNI FPLVEQFTVR HHTSDMQYWA
     SVVMRNLCRK DDSRGGIRQC AYYQCGRWEE YTRQFAKCRR CRRTKYCSKE CQKSAWVFHR
     HWCVAAS
//
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