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Database: UniProt
Entry: L8FMY9_PSED2
LinkDB: L8FMY9_PSED2
Original site: L8FMY9_PSED2 
ID   L8FMY9_PSED2            Unreviewed;       636 AA.
AC   L8FMY9;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 39.
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=GMDG_05392 {ECO:0000313|EMBL:ELR02325.1};
OS   Pseudogymnoascus destructans (strain ATCC MYA-4855 / 20631-21) (Bat
OS   white-nose syndrome fungus) (Geomyces destructans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=658429 {ECO:0000313|EMBL:ELR02325.1, ECO:0000313|Proteomes:UP000011064};
RN   [1] {ECO:0000313|Proteomes:UP000011064}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4855 / 20631-21 {ECO:0000313|Proteomes:UP000011064};
RG   The Broad Institute Genome Sequencing Platform;
RA   Cuomo C.A., Blehert D.S., Lorch J.M., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA   Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E.,
RA   Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA   Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA   Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The genome sequence of Geomyces destructans 20631-21.";
RL   Submitted (SEP-2010) 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; GL573281; ELR02325.1; -; Genomic_DNA.
DR   RefSeq; XP_012743820.1; XM_012888366.1.
DR   AlphaFoldDB; L8FMY9; -.
DR   VEuPathDB; FungiDB:GMDG_05392; -.
DR   HOGENOM; CLU_014851_0_0_1; -.
DR   InParanoid; L8FMY9; -.
DR   OrthoDB; 2787008at2759; -.
DR   Proteomes; UP000011064; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011064};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00134}.
FT   DOMAIN          590..631
FT                   /note="MYND-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50865"
FT   REGION          137..196
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          219..252
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          287..366
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        140..167
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        223..241
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   636 AA;  70712 MW;  498EC0B0A535A5BB CRC64;
     MREVNFSIPN VNKASVGITT ALYDRRALDC TSTLPLINSL NHLAYLTTSS ARIRDILTVD
     GGVERLVCLL KAGRSKDMMD MWKWNLGFQC VVNIGVRGSE PVRTRVVEAD MVPVIATILD
     NYIKVVDRCR EKAEEAKQKA IQEQGSSGRH GSRSSQKVTS FGNRSGRVDA ENRTFRRQAP
     PPSIEIPASS ANAPASADFA ATDATPTNAA FSLTSPERTT FAGSHHHHHH HHRHHHRNQD
     PRHTPHFAPP SRHQIQPLAT AIPSMDATDG FNIRPARDVE RLPSMVPYHH SGLTSQPDSP
     TTPLPPTQLR SPTTRPVPAS NPTARARRRP SIRHQTSMGG EQEDPNGDSM VSDESGEPDI
     ATASTDIQTS VGIQDISMDD EGDSMITAVE TPLGLTTPTV SEAQDAGTFN ITHRSAIDGS
     LIADATTPTG PPMGLSPAQT NMANNSPAIM ITTIPRYLLD RPTPANAQVL AAMPRDEDVL
     MSLQLLAYVS KYCNLRKYFQ RSHLVPKLKI GKELHLLDQD DSSCHAQAED GCESDEEEEY
     LLPDDFNIFP LVEKFTVRHH SQDMQYWAGV VMRNLCRKDD TRGGIRQCAY YQCGKWEEFT
     RQFAKCRRCR RTKYCSKECQ KSAWVYHRHW CVEASQ
//
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