ID A0A2L2SV87_9HYPO Unreviewed; 658 AA.
AC A0A2L2SV87;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
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};
OS Fusarium venenatum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=56646 {ECO:0000313|EMBL:CEI39595.1, ECO:0000313|Proteomes:UP000245910};
RN [1] {ECO:0000313|Proteomes:UP000245910}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A3/5 {ECO:0000313|Proteomes:UP000245910};
RA King R.;
RL Submitted (OCT-2014) 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; LN649232; CEI39595.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2L2SV87; -.
DR OrthoDB; 2787008at2759; -.
DR Proteomes; UP000245910; Chromosome iiii.
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:UP000245910};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00134}.
FT DOMAIN 612..653
FT /note="MYND-type"
FT /evidence="ECO:0000259|PROSITE:PS50865"
FT REGION 131..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 310..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 429..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..154
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..386
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..449
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 658 AA; 72808 MW; 6A348710B37E3A8B CRC64;
MREVNFSIPN VNKASVGITT ALYDRRALDC TSTLPLINSL NHLAYLTTSS ARIRDILTVD
GGIERLVCIL KQGRSKDMMG MWKWNLAFQC VVNIGVRGTE NVRTRVVEAD MVPVIATILD
NYTKAVDKCR EKAEEAKQKQ NYDNHRHRGH EYRQNPKPSS SNSASATASA SSSSSSVAVA
ASAFGHRSSS RVDTIEQRSR RHGPPPSIDV SASYAGPSTA APQTHPQQQS LDTAMGGSQW
PQSASERSAS WGSTRHQPLR VRGLEDRHAT TSAPRQTMQP LATVVSNTDT VEGFVRPVRD
IDRLASMAPF GSTDLVSQPT SPTTPLPPPQ MRSPTVRPAS ALGPSGRSRR RPSIRHQNST
ADADDINGDS MPSDESPETE MTGTDNLQSA VGIQDITMED GDTMLGGTAL DLATPTVSET
HQEASTFNIN HRSPMDGSLT NNNAPTPVPA IGLSPNRPAM TTPPQPPLAA TTVPRYLLDR
NFVPNPQMVA AMPREEDVLM SLQLLAYVSK YCGLRSYFQK SHLVPRLKIG KELAAIDKDI
TAMDEEEDVP EVYDEDADDE EYLLPNDFNL FPLVEKFTVR YHSTDMQYWA GVVMRNLCRK
DDTRGGIRQC AYYQCGKWEE YTRQFAKCRR CRRTKYCSKE CQKSAWAFHR HWCVAATQ
//
