ID A0A0S7DYZ7_9EURO Unreviewed; 414 AA.
AC A0A0S7DYZ7;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Pre-mRNA-splicing factor {ECO:0000313|EMBL:GIM41021.1};
GN ORFNames=ALT_005466 {ECO:0000313|EMBL:GIM41021.1};
OS Aspergillus lentulus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=293939 {ECO:0000313|EMBL:GIM41021.1};
RN [1] {ECO:0000313|EMBL:GIM41021.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IFM 54703 {ECO:0000313|EMBL:GIM41021.1};
RA Kusuya Y., Sakai K., Kamei K., Takahashi H., Yaguchi T.;
RT "Draft Genome sequence of the pathogenic filamentous fungus Aspergillus
RT lentulus IFM 54703T.";
RL Genome Announc. 4:e01568-15(2016).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the RRM CWC2 family.
CC {ECO:0000256|ARBA:ARBA00008024}.
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:GIM41021.1}.
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DR EMBL; BCLY01000012; GIM41021.1; -; Genomic_DNA.
DR STRING; 293939.A0A0S7DYZ7; -.
DR VEuPathDB; FungiDB:TMP_alenIFM54703_6618; -.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR CDD; cd12360; RRM_cwf2; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR039171; Cwc2/Slt11.
DR InterPro; IPR034181; Cwc2_RRM.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR032297; Torus.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR PANTHER; PTHR14089:SF2; PRE-MRNA-SPLICING FACTOR CWC2; 1.
DR PANTHER; PTHR14089; PRE-MRNA-SPLICING FACTOR RBM22; 1.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF16131; Torus; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF90229; CCCH zinc finger; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW mRNA splicing {ECO:0000256|ARBA:ARBA00023187};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW Spliceosome {ECO:0000256|ARBA:ARBA00022728};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
SQ SEQUENCE 414 AA; 45449 MW; C9989B35B4D204B7 CRC64;
MAETAVVDPP HATEPTPLPT ESTEPSSLTP SDENALTQPS ETAVAATTDA DGTQKKTKKI
IRRKRRPARP QVDPATLKSE PPPQTGTVFN IWYNKWSGGD REDKYLSKHA APSRCNIAKD
SGYTRADKVP GSYFCLFFAR GVCPKGHECE YLHRLPTLHD LFNPNVDCFG RDKFSDYRDD
MGGVGSFTRQ NRTLYVGRIH VTDDIEEVVS RHFAEWGQID RIRVLTSRGV AFVTYTNEAN
AQFAKEAMAH QSLDHNEILN VRWATVDPNP LAQKREARRL EEQAAEAVRR ALPAEFVAEL
EGRDPEARKK KKIEGSFGLE GYEAPDDVWY ARTKELEDAG RAGQLEAPEQ HLMIEAASSS
SSAALPSQSE NSGIFSSSTV AALRGLAGGN VTTQKAPANS GGPLVAYGSD DDSD
//
