ID A0A0L1JCB6_ASPNO Unreviewed; 1788 AA.
AC A0A0L1JCB6;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Splicing factor 3B subunit 1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=ANOM_002927 {ECO:0000313|EMBL:KNG89053.1};
OS Aspergillus nomiae NRRL 13137.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1509407 {ECO:0000313|EMBL:KNG89053.1, ECO:0000313|Proteomes:UP000037505};
RN [1] {ECO:0000313|EMBL:KNG89053.1, ECO:0000313|Proteomes:UP000037505}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 13137 {ECO:0000313|EMBL:KNG89053.1,
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SF3B1 family.
CC {ECO:0000256|ARBA:ARBA00005754}.
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:KNG89053.1}.
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DR EMBL; JNOM01000039; KNG89053.1; -; Genomic_DNA.
DR RefSeq; XP_015409976.1; XM_015548184.1.
DR STRING; 1509407.A0A0L1JCB6; -.
DR GeneID; 26804731; -.
DR OrthoDB; 226540at2759; -.
DR Proteomes; UP000037505; Unassembled WGS sequence.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0000245; P:spliceosomal complex assembly; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 3.
DR Gene3D; 3.90.700.10; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR003953; FAD-binding_2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR021133; HEAT_type_2.
DR InterPro; IPR015016; SF3b_su1.
DR InterPro; IPR038737; SF3b_su1-like.
DR InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR PANTHER; PTHR12097:SF0; SPLICING FACTOR 3B SUBUNIT 1; 1.
DR PANTHER; PTHR12097; SPLICING FACTOR 3B, SUBUNIT 1-RELATED; 1.
DR Pfam; PF00890; FAD_binding_2; 1.
DR Pfam; PF08920; SF3b1; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF56425; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
DR PROSITE; PS50077; HEAT_REPEAT; 1.
PE 3: Inferred from homology;
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022728};
KW mRNA splicing {ECO:0000256|ARBA:ARBA00023187};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000037505};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Spliceosome {ECO:0000256|ARBA:ARBA00022728}.
FT DOMAIN 224..358
FT /note="Splicing factor 3B subunit 1"
FT /evidence="ECO:0000259|Pfam:PF08920"
FT REPEAT 762..800
FT /note="HEAT"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00103"
FT DOMAIN 1275..1763
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT REGION 106..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 164..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..190
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1788 AA; 196581 MW; AE35BC1589A3B2F9 CRC64;
MSDSDFEAVR RLQAERNAAA AGKKASLTES FDTTLYEREG ADRFAGYDTS IAVNGDDEEM
EDADGGHRLV GQYTATKSQM DEFAHGNGVE EEDILLGREK AARIADRETD YQKRRFNRGP
LTPTRADPFA ANTHANVEGE GQTYREVMAL RELEKEEERV QKLIAEKQAS GENDVAEHEA
TLKLEDKENA DAGSTVSVAT GRKRKQRWDV ASESTEAAPE APEPQEAKKK SRWDQTPSLP
VPGAAEEAPK RRSRWDQAPS ITSATPVGNQ GLATPMHPSQ AGAALIPTSF GTDISGRNAP
LSDEELDMML PGEADGYKIL DPPPGYAPIR NPARKLMSTP APMASATGVG GFMMQEPESA
RALGKQLPTE IPGVGDLQFF KPEDMAYFGK LMEGGDESVM SVDELKERKI MRLLLKVKNG
TPPMRKTALR QLTDNARQFG AGPLFNQILP LLMEKSLEDQ ERHLLVKVID RVLYKLDDLV
RPYVHKILVV IEPLLIDQDY YARVEGREII SNLAKAAGLA TMISTMRPDI DHVDEYVRNT
TARAFAVVAS ALGIPALLPF LRAVCRSKKS WQARHTGVKI VQQIPILMGC AILPHLKGLV
DCIADNLSDE QAKVRTVTAL AVAALAEAAN PYGIESFDEI LNPLWTGARK QRGKGLAAFL
KAVGYIIPLM DEEYANYYTS QIMEILLREF SSPDEEMKKV VLKVVSQCAS TDGVTASYLK
EHVLTDFFKS FWVRRMALDR RNYRQVVDTT VDLGQKVGVG EILERVVNNL KDESEPYRKM
TVETVEKLIA ALGAADISER LEERLIDGVL YAFQEQSIED IVILNGFGTA VNALGTRCKP
YLPQIVSTIL WRLNNKSATV RQQAADLISR IAMVMKQCGE DALMGKLGIV LYEYLGEEYP
EVLGSILGAL RSIVTVVGIN QMQPPIRDLL PRLTPILRNR HEKVQENTID LVGRIADRGP
ESVNAREWMR ICFELLDMLK AHKKGIRRAA NNTFGFIAKA IGPQDVLATL LNNLRVQERQ
SRVCTAVAIG IVAETCAPFT VLPALMNEYR VPELNVQNGV LKAMSFLFEY IGEMAKDYVY
AVTPLLEDAL IDRDQVHRQT AASVVKHIAL GVVGLGCEDA MVHLLNLVFP NIFETSPHVI
DRVIEAIDAI RMAVGTGVVM NYVWAGLFHP ARKVRTPYWR LYNDAYVQSA DAMIPYYPTL
EDDGLERSEF DRTSDIVLRS PALLCGCSAK VRGYESVLTQ SPTTQLYISK PIAKTSILNQ
TRAPLAVMAL PPHCDVLVIG GGNAGFCAAI SAVQSGAQKV IIIDKCPENW AGGNSYFTAG
AFRTTHGGLE DLLPIVNNVD PATAQKIDMS PYTAADFTND MERVTGKRAD RELSRVLVDD
SNATVKWLAE NGVRFQLSFN RQSYEVNGRI KFWGGLALKT QDGGKGLIQD HLRTAQKLGI
DVFFSTAAER LATDPVTRAV SSVSAVHHGQ VKVIKTNAVV LAAGGFEANS RMRAQFLGPH
WDTALVRGTP YNSGECLEIA IRDVSAKQVG NWSGCHCVAW DANAPANTGD REISNEFTKS
GYPLGIMINR QGSRFVDEGS DLRNYTYAMI GRQILHQPGH VAFQIWDSRT ISWLREEEYR
PEVVQHITAS SISELAAKCA AEHGLEDKDR FERTIHEFNN AVYESQRLNP GQQWDPAVKD
GLSTQSNACT LSVPKSNWAL PIDLPPFLAV KVSAGITFTF GGLEVNPETA AVVSSTTNCE
IPGLYCAGEM VGGLFYDNYP GGSGLTSGAV FGRRAGRAAA RASTIAVR
//
