MUB1_EMENI
ID MUB1_EMENI Reviewed; 590 AA.
AC O42631; C8VR00; Q5BHA2;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=MYND-type zinc finger protein samB;
DE AltName: Full=Suppressor of anucleate metulae protein B;
GN Name=samB; ORFNames=AN0078;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
RX PubMed=8889518; DOI=10.1093/genetics/144.2.533;
RA Kruger M., Fischer R.;
RT "Isolation of two apsA suppressor strains in Aspergillus nidulans.";
RL Genetics 144:533-540(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=9427754; DOI=10.1093/emboj/17.1.204;
RA Kruger M., Fischer R.;
RT "Integrity of a Zn finger-like domain in SamB is crucial for morphogenesis
RT in ascomycetous fungi.";
RL EMBO J. 17:204-214(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
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:0000269|PubMed:9427754}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9427754}.
CC -!- DISRUPTION PHENOTYPE: Produces partial defects in sexual reproduction
CC and suppresses an apsA deletion mutation. Changes the colony morphology
CC and inhibits sexual spore formation. {ECO:0000269|PubMed:8889518}.
CC -!- SIMILARITY: Belongs to the MUB1/samB family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ000996; CAA04448.1; -; Genomic_DNA.
DR EMBL; AACD01000003; EAA65256.1; -; Genomic_DNA.
DR EMBL; BN001308; CBF90245.1; -; Genomic_DNA.
DR RefSeq; XP_657682.1; XM_652590.1.
DR AlphaFoldDB; O42631; -.
DR SMR; O42631; -.
DR STRING; 162425.CADANIAP00002674; -.
DR EnsemblFungi; CBF90245; CBF90245; ANIA_00078.
DR EnsemblFungi; EAA65256; EAA65256; AN0078.2.
DR GeneID; 2875849; -.
DR KEGG; ani:AN0078.2; -.
DR VEuPathDB; FungiDB:AN0078; -.
DR eggNOG; ENOG502QTM3; Eukaryota.
DR HOGENOM; CLU_014851_0_0_1; -.
DR InParanoid; O42631; -.
DR OMA; HWCVAAT; -.
DR OrthoDB; 1167239at2759; -.
DR Proteomes; UP000000560; Chromosome VIII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:1990304; C:MUB1-RAD6-UBR2 ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IMP:AspGD.
DR GO; GO:0043935; P:sexual sporulation resulting in formation of a cellular spore; IMP:AspGD.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR InterPro; IPR002893; Znf_MYND.
DR Pfam; PF01753; zf-MYND; 1.
DR PROSITE; PS01360; ZF_MYND_1; 1.
DR PROSITE; PS50865; ZF_MYND_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Metal-binding; Reference proteome; Sporulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..590
FT /note="MYND-type zinc finger protein samB"
FT /id="PRO_0000393328"
FT ZN_FING 546..587
FT /note="MYND-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT REGION 133..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 297..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 562
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 565
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 583
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 587
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
SQ SEQUENCE 590 AA; 66272 MW; ED14880BA16845FD CRC64;
MREVNFSIPN VNKASVNITT TLYDRRALDC TSTLPLINSL NHLAYLTTSS ARIRDILTVD
GGIERLVCIL KEGRSNNLME MWKWSLAFQC VVNIGVRGSE NVRTRVVEAD MVPVIATILD
NYIKVMDKVR ARSDSEAQRH RHHQLHHKIT PTASDSTSRS SFSDASSNEQ RTSRRQPPPT
HIEIPPFFHD TRAVESNAAD VPSPPRAPMT SPPERSTFGQ DTYAHRSHAP LRHRAIQPLA
TAIPSMDAAD GSGLRPVRDT ERLPSMLPAA FNELASQPDS PTTPSGAGHI RSNVHVPIGT
HARPPLSQHQ STSGDSDDAN GEDSIMADDT GSGQSRRPII GLQSRMDIDD DADRQTVIDS
VTDSSHDLTV TDTTSDGQES ETFNITHRSA VDGSIITNDN AQAVNNANSP PIVPSPYSLY
FRDRTNIATQ NFLNTMPREE DVLMSLQLLA YVSKYCNLRS YFQNSHFVPK LKIDRELRML
DEGASPVELI EEEDEYLLPD DVNIFPLVEK FTARHHSKDM SYWACVVMRN LCRKDESRGG
IRQCANYKCG KWEEFTRQFA KCRRCRRTKY CSKDCQKAAW LYHRHWCATP
