ID A0A0L1J1B3_ASPNO Unreviewed; 2059 AA.
AC A0A0L1J1B3;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KNG85228.1};
GN ORFNames=ANOM_006343 {ECO:0000313|EMBL:KNG85228.1};
OS Aspergillus nomiae NRRL 13137.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1509407 {ECO:0000313|EMBL:KNG85228.1, ECO:0000313|Proteomes:UP000037505};
RN [1] {ECO:0000313|EMBL:KNG85228.1, ECO:0000313|Proteomes:UP000037505}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 13137 {ECO:0000313|EMBL:KNG85228.1,
RC ECO:0000313|Proteomes:UP000037505};
RA Moore M.G., Shannon B.M., Brian M.M.;
RT "The Genome of the Aflatoxigenic Filamentous Fungus Aspergillus nomius.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the proteasome subunit S3 family.
CC {ECO:0000256|ARBA:ARBA00007912}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KNG85228.1}.
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DR EMBL; JNOM01000167; KNG85228.1; -; Genomic_DNA.
DR RefSeq; XP_015406151.1; XM_015551599.1.
DR STRING; 1509407.A0A0L1J1B3; -.
DR GeneID; 26808147; -.
DR OrthoDB; 25272at2759; -.
DR Proteomes; UP000037505; Unassembled WGS sequence.
DR GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR GO; GO:0030234; F:enzyme regulator activity; IEA:InterPro.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0046165; P:alcohol biosynthetic process; IEA:UniProt.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:InterPro.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0043386; P:mycotoxin biosynthetic process; IEA:UniProt.
DR GO; GO:0042176; P:regulation of protein catabolic process; IEA:InterPro.
DR CDD; cd21675; SMP_TEX2; 1.
DR CDD; cd00685; Trans_IPPS_HT; 1.
DR Gene3D; 1.10.600.10; Farnesyl Diphosphate Synthase; 1.
DR InterPro; IPR013586; 26S_Psome_reg_C.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR000092; Polyprenyl_synt.
DR InterPro; IPR033749; Polyprenyl_synt_CS.
DR InterPro; IPR031468; SMP_LBD.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR10758:SF2; 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT 3; 1.
DR PANTHER; PTHR10758; 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT 3/COP9 SIGNALOSOME COMPLEX SUBUNIT 3; 1.
DR Pfam; PF01399; PCI; 1.
DR Pfam; PF00348; polyprenyl_synt; 1.
DR Pfam; PF08375; Rpn3_C; 1.
DR SFLD; SFLDS00005; Isoprenoid_Synthase_Type_I; 1.
DR SMART; SM00753; PAM; 1.
DR SMART; SM00088; PINT; 1.
DR SUPFAM; SSF48576; Terpenoid synthases; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50250; PCI; 1.
DR PROSITE; PS00444; POLYPRENYL_SYNTHASE_2; 1.
DR PROSITE; PS51847; SMP; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Lipid transport {ECO:0000256|ARBA:ARBA00023055};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Reference proteome {ECO:0000313|Proteomes:UP000037505};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transport {ECO:0000256|ARBA:ARBA00023055}.
FT DOMAIN 352..537
FT /note="PCI"
FT /evidence="ECO:0000259|PROSITE:PS50250"
FT DOMAIN 1422..1615
FT /note="SMP-LTD"
FT /evidence="ECO:0000259|PROSITE:PS51847"
FT REGION 1..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1632..1656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1676..1717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1758..1841
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1883..2043
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 570..597
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 12..84
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..159
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1694..1717
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1904..1918
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2008..2023
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2025..2041
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2059 AA; 226691 MW; 2BB1580CBC77F0F4 CRC64;
MPAERRSLRS NSKSDSSSSA NGEKARSASQ NSSSNKDKVA PTRATASKTK GTRAASSNNT
SNSGMGEQRD QPRTNGSEPT ENGLNGSEDV EMGEDTAGAP TSSFNANKDR KGDEKMTVVV
PPTKGSRLSG DKGQDQEGDV AMEGAEGDES QKPEPEVDPR AKAIQDIKTN FTLLERAVAH
FDPRFTLRVL RSISSMRKHI TSDVLAEVLV ESYPPSSPTA SFLLEAIGEA GAFENAVASS
KMDVESEKTK SNSKEILPEI DTYLSILVQI YLYDNKEIQR GAKFSTSLIE RLRTINRRTL
DSLAARVYFY YSLFFEQIAP LPPSPAATVT TIRQPLLAAL RTAVLRKDVD TQATVMTLLL
RNYLSTSHIS QADLLISHNH FPQSASNNQI ARARGFYQAS HKLLVVVELL MGDIPDRAIF
RQPALERAMH PYFLLVQAVS VGDLDGFLSI VNTHSTTFRK DGTYTLILRL RQNVIKTGIR
MMSLSYSRIS LRDICLRLGL DSEESAEYIV AKAIRDGVIE ATLDHERGFM KSKEVGDIYA
TREPGEAFHE RIRACLSLHD ESVKAMRFPM NQHRLELKSA QEAREREREL AKEIQDGRCI
CFQRSVPARA KLRRQQLSTE IFGRLIFADF LNYAASHPNK LRPASTYALS SFHSPFRLLS
MKARAVPASG LVLPSRVTPS TSICWQCLRN DLISIQINSQ TRAYHPTRRK SASPFGAAVT
AAQTLFKGLP KAPPGISVDP LRIVGKELKF LTKNIRQLLG SGHPTLDKVA KYYTKSEGKH
MRPLLVLLMS QATALTPRHG RWSSTPSYTV NDPISSPSVL ADTNPDLNPL VSASVEGKYD
FSGDENILPT QRRLAEITEL IHTASLLHDD VIDNAVTRRS SSSANLQFGN KMAVLAGDFL
LGRASVALAR LRDPEVTELL ATVIANLVEG EFMQLKNTAS DEKNPVFTDE TISYYLQKTY
LKTASLISKS CRAAALLGDS TPQVVEAAYA YGRNLGLAFQ LVDDMLDYTV SDAELGKPSG
ADLELGLATA PLLFAWKQNP ELGPLVGRKF SQEGDVQRAR DLVYQSNGVE KTRDLAQEYA
DKAKAAISSF PDSEAKDGLL QMCEKTMNRR NSTGQGLVWF GASTASPFPS YPHDGPFDVT
ILIDRLLMGS LGSFLFVYIL GGLTFIPLVL SLVLLHAYFT LPSPPPVEHR CELAKDPLRR
PGDDQYSLKS GTDELAEKFH RTHESDVAAG YFAVCREYVP GGVNGKPPER TTPAGEVIAA
ESPSVYQTMY RSLFDRKQTP TIEPAKNNGK SGKRARNVFY IVLRHGHLML YDDANQVEVR
YVISLAHHDV NICGGEGEIQ EGELWLKRNA ICLSRRLESL ADLGGPTPPF FLFSENLSEK
EDFYFAMLQN QSRMRNSPDS PPKHQPFDVK HIVTLVQRLH SSEEQLQTRW INAVLGRLFL
AMYRTPEMEE FIRKKITKKI SRVNKPNFIS KIGLQRIDMG EGAPFIINPR LKDLTVDGNC
CVETDVQYTG NFRVEISATV RIDLGPRFKA REVDIVLAVV LKKLHGHLLI RFKPPPSNRA
WISFETMPSM DMDIQPIVSS KQITYGIILR TIESRIREVV AESVVQPFWD DIPFLDTATQ
RFRGGIWQRE IPTPDTKVDI PDESGAQPQT TGAEKGDFVD MLKTKDERTM SAPVLSESIP
ITMKSRKGSK GELERNNSSA SYTASEKFGS SPPRAIRSQT FSNAADPVLT ADNAKIDKVV
YDGKDAEKSS AASAMIEISN RSPPGSPNRS PNGSPPTDSH MPQDNASQSR DPSIVDSIES
VGEFSTDSSV RPSAVHKTSS SSLRSMAASS TASLNGNKPR RSTLETLARS VTSSTAAEKS
QVSLSLGTAT SVAKRWGWNM FGKGEHSVTH ESSRPAGTPE EPIGRGHPLP PPGTPLPRPE
SFAFKRNTVP VTKRKPVPHN ASPELQPKGD DKRRVSKPPL PRRKPIFSSG DSENLPDELL
VVEAPYDSGP NSPVVDVAPD KALPGPSTQR DSPPSNVVTK RSSDLWEKAN GHDRSSLVEG
TEADKHGMAI LSATDGIIP
//
