MUB1_ASPFU
ID MUB1_ASPFU Reviewed; 605 AA.
AC Q4WVI6;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=MYND-type zinc finger protein samB;
DE AltName: Full=Suppressor of anucleate metulae protein B;
GN Name=samB; ORFNames=AFUA_5G12230;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MUB1/samB family. {ECO:0000305}.
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DR EMBL; AAHF01000003; EAL91390.1; -; Genomic_DNA.
DR RefSeq; XP_753428.1; XM_748335.1.
DR AlphaFoldDB; Q4WVI6; -.
DR SMR; Q4WVI6; -.
DR STRING; 746128.CADAFUBP00005854; -.
DR EnsemblFungi; EAL91390; EAL91390; AFUA_5G12230.
DR GeneID; 3511434; -.
DR KEGG; afm:AFUA_5G12230; -.
DR VEuPathDB; FungiDB:Afu5g12230; -.
DR eggNOG; ENOG502QTM3; Eukaryota.
DR HOGENOM; CLU_014851_0_0_1; -.
DR InParanoid; Q4WVI6; -.
DR OMA; HWCVAAT; -.
DR OrthoDB; 1167239at2759; -.
DR Proteomes; UP000002530; Chromosome 5.
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; IBA:GO_Central.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR002893; Znf_MYND.
DR Pfam; PF01753; zf-MYND; 1.
DR SUPFAM; SSF48371; SSF48371; 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..605
FT /note="MYND-type zinc finger protein samB"
FT /id="PRO_0000393324"
FT ZN_FING 560..601
FT /note="MYND-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT REGION 134..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..174
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"
FT BINDING 576
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 579
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 597
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 601
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
SQ SEQUENCE 605 AA; 67975 MW; E50D8BDA17C86BF8 CRC64;
MREVNFNIPN VNKASVNITT TLYDRRALDC TSTLPLINSL NHLAYLTTSS ARIRDILTVD
GGIERLVCIL KEGRSRDLME MWKWSLAFQC VVNIGVRGSE SVRTRVVEAD MVPVIATILD
NYIKVVDKAR ARADSESQRQ SSRHHSKAVP TSNDVSGRPS FLEQPLTAEQ RTSRRHAPPS
IEIPPQPFFQ ENHVADSNVL DVTSPSRVPM TSPPERSAFG QDVHHRRTND GRFAHGNHRH
RMQPLATALP SMDATDGFGL RPVRDNERLP SMLPGFHTGL TSQPDSPTTP NAPVQPRSSA
QATIARQRPS LRQQQSASGE SDDGNGDGST MDEDPASTEA AEPIVGLQNR MDIDDVGDRD
TILGGVSDSH DLTVTDPSEE QEAETFNITH RSTVDGSMIN TDNAQNNAAL GLSPTQAADN
ANSPALVPSP YSLYFRDRTT TAAHGVLTTM PRDEDVLMSL QLLAYVSKYC NLRSYFQHSH
FVPKLKIDRE LQMLEEGTSP IEFPEDEDEY LLPDDVNIFP LVEKFTVRHH SKDMQYWACV
VMRNLCRKDE SRGGIRQCAY YKCGKWEEFQ RQFAKCRRCR RTKYCSKDCQ KAAWVYHRHW
CHTTP
