ID A0A1L9NLM0_ASPTC Unreviewed; 605 AA.
AC A0A1L9NLM0;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
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=ASPTUDRAFT_185981 {ECO:0000313|EMBL:OJI90119.1};
OS Aspergillus tubingensis (strain CBS 134.48).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=767770 {ECO:0000313|EMBL:OJI90119.1, ECO:0000313|Proteomes:UP000184304};
RN [1] {ECO:0000313|Proteomes:UP000184304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 134.48 {ECO:0000313|Proteomes:UP000184304};
RX PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT "Comparative genomics reveals high biological diversity and specific
RT adaptations in the industrially and medically important fungal genus
RT Aspergillus.";
RL Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
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; KV878176; OJI90119.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L9NLM0; -.
DR VEuPathDB; FungiDB:ASPTUDRAFT_185981; -.
DR OMA; QDMQYWA; -.
DR Proteomes; UP000184304; 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:UP000184304};
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..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 268..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 605 AA; 67665 MW; A42F9AEA5C0948D5 CRC64;
MREVNFSIPN VNKASVNITT TLYDRRALDC TSTLPLINSL NHLAYLTTSS ARIRDILTVD
GGIERLVCIL KEGRSRDLME MWKWSLAFQC VVNIGVRGSE SVRTRVVEAD MVPVIATILD
NYIKVVEKAR ARADSENQRH SSRHHAKGAP ITSDAPSRPV YVDQSTNTEQ RPSRRQAPPP
HIEIPPFYQD SHASDSNAMD ITSSPRVPVT SPPERSTFGQ DAHNLRSNDT RYAHAAHRYR
VMQPLATALP PMDAADGFGL RPVRDTERLP SMLPGFQNGL ASQPDSPTTP SGPAQLRSNT
QAPSARPRPT LRQQQSASGE SDDGNGEGST LGDDPGSGET TEPIVGIQNR MEIDDDGDRQ
TVLEGVSNTH DLTVNDTSES QEAETFNITH RSTVDGSMIN NDATRTNGAL GLSPTQAPNT
TNSPAVVPSP YSLYVRDRST TAVQGVLTTM PKDEDVLMSL QLLAYVSKYC NLRSYFQHSH
LVPKLKVDRE LQMLEDGVSP IEPPEEEDEY LLPDDVNIFP LVEKFTVRHH SKDMQYWACV
VMRNLCRKDE SRGGIRQCAY YKCGKWEEFQ RQFAKCRRCR RTKYCSKDCQ KAAWVYHRHW
CHTTP
//
