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Database: UniProt
Entry: A0A395HUM3_ASPHC
LinkDB: A0A395HUM3_ASPHC
Original site: A0A395HUM3_ASPHC 
ID   A0A395HUM3_ASPHC        Unreviewed;       981 AA.
AC   A0A395HUM3;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=SWI-SNF complex subunit {ECO:0000313|EMBL:RAL09914.1};
DE   Flags: Fragment;
GN   ORFNames=BO97DRAFT_373514 {ECO:0000313|EMBL:RAL09914.1};
OS   Aspergillus homomorphus (strain CBS 101889).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1450537 {ECO:0000313|EMBL:RAL09914.1, ECO:0000313|Proteomes:UP000248961};
RN   [1] {ECO:0000313|EMBL:RAL09914.1, ECO:0000313|Proteomes:UP000248961}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 101889 {ECO:0000313|EMBL:RAL09914.1,
RC   ECO:0000313|Proteomes:UP000248961};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the proteasome subunit S9 family.
CC       {ECO:0000256|ARBA:ARBA00007454}.
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DR   EMBL; KZ824299; RAL09914.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A395HUM3; -.
DR   STRING; 1450537.A0A395HUM3; -.
DR   VEuPathDB; FungiDB:BO97DRAFT_373514; -.
DR   OrthoDB; 9355at2759; -.
DR   Proteomes; UP000248961; Unassembled WGS sequence.
DR   GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR   CDD; cd10568; SWIB_like; 1.
DR   Gene3D; 1.25.40.570; -; 1.
DR   Gene3D; 1.10.245.10; SWIB/MDM2 domain; 1.
DR   InterPro; IPR000717; PCI_dom.
DR   InterPro; IPR040780; Rpn6_C_helix.
DR   InterPro; IPR040773; Rpn6_N.
DR   InterPro; IPR019835; SWIB_domain.
DR   InterPro; IPR036885; SWIB_MDM2_dom_sf.
DR   InterPro; IPR003121; SWIB_MDM2_domain.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR10678:SF2; 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT 11; 1.
DR   PANTHER; PTHR10678; 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT 11/COP9 SIGNALOSOME COMPLEX SUBUNIT 2; 1.
DR   Pfam; PF01399; PCI; 1.
DR   Pfam; PF18503; RPN6_C_helix; 1.
DR   Pfam; PF18055; RPN6_N; 1.
DR   Pfam; PF02201; SWIB; 1.
DR   SMART; SM00753; PAM; 1.
DR   SMART; SM00088; PINT; 1.
DR   SMART; SM00151; SWIB; 1.
DR   SUPFAM; SSF47592; SWIB/MDM2 domain; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS50250; PCI; 1.
DR   PROSITE; PS51925; SWIB_MDM2; 1.
PE   3: Inferred from homology;
KW   Proteasome {ECO:0000256|ARBA:ARBA00022942};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248961}.
FT   DOMAIN          224..393
FT                   /note="PCI"
FT                   /evidence="ECO:0000259|PROSITE:PS50250"
FT   DOMAIN          751..828
FT                   /note="DM2"
FT                   /evidence="ECO:0000259|PROSITE:PS51925"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          422..444
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          467..505
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          518..538
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          598..617
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          626..677
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          934..957
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        486..502
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        598..614
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         981
FT                   /evidence="ECO:0000313|EMBL:RAL09914.1"
SQ   SEQUENCE   981 AA;  109498 MW;  2EC122EE25886D32 CRC64;
     MAPSPTTAGR IEEARTLAKN DPSKAESILK ETLSQGIGST EASSRDYENA LVSLGELYRD
     QKKPQEIAEL IKTSRDSFSS FAKAKTAKLV RQLLDLFSEI PNTLDIQVSV IKSCIEWAVA
     ERRSFLRQNL ETRLVAIYMQ KQTYYDALTL INSLLRELKR LDDKLMLVEV QLLESRVYHA
     LGNQAKARAA LTAARTSAAS VYTPPNLQAG LDMQSGMLHA EDKDFNTSFS YFIEALEGYS
     SLDEGEKATA ALQYMLLCKI MLNLVDDVTN LLGSKQAQKY ASPRLEAMKA VARAHADRSL
     EEYEKALSDY RFELGSDAFI RNHLRRLYDA MLEQNLIKVI EPFSRVELDH IAKMVGLDTQ
     QVERKLSQMI LDKVIIGVLD QGAGCLIVFD ETERDQAYDA ALDTIAKLSN VVEELYTNQA
     SLLDSSPPRT SRLPRPTSFP SEPPLNPSLQ FLLLHWAPAM NAPIPPNYGR GFPPQAAQRS
     PATPRRGPQA PAPMPAPMSQ HGVPPQLLPI QQRSMMAANA ANEAALRRSR KPTDKNIPDG
     IEEVVIGEGV QQYKSLRDVE KRLDAAIVRK RLDIQDSISK TVKKYRTMRI WISNTVDNQP
     WQNASGQNGA SNPGSGRYKV RIEGRLLDDD SDPTAPEDSD EEDSTAADDQ AGKNGDAMEQ
     DGPGATKTKT KAATSSKRLQ QRFSHFFKSV TIDFDKPATT NPEDVKPITW NKPQLPPNAV
     TLPPTADFDS IQFSRASQEN LNVTVSLVRD ETPERYKLSK ELAEVLDVEE ETRSGIVLGI
     WDYIRAMGLQ EDEEKRLVRC DHRLRSIFNR DQMFFPQIPE SIGPHTSPID PIKLPYTIRV
     DSDFHNDPTP TVYDIQVALE DPLRSKMLAL TQNPQYTAAM RQISTLDDQV ALIVQALTHS
     RARHSFFTAL SKDPATFLRR WVNSQRRDLE TILGEATRGG GEDASGPEFR RGGTDGAWDT
     PVAREAVRYM LAKPEAAMGR A
//
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