ID A0A0M9F5X9_FUSLA Unreviewed; 255 AA.
AC A0A0M9F5X9;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=mRNA 3'-end-processing protein {ECO:0000256|RuleBase:RU369008};
GN ORFNames=FLAG1_00515 {ECO:0000313|EMBL:KPA46652.1};
OS Fusarium langsethiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=179993 {ECO:0000313|EMBL:KPA46652.1, ECO:0000313|Proteomes:UP000037904};
RN [1] {ECO:0000313|EMBL:KPA46652.1, ECO:0000313|Proteomes:UP000037904}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fl201059 {ECO:0000313|EMBL:KPA46652.1,
RC ECO:0000313|Proteomes:UP000037904};
RA Lysoe E., Divon H.H., Terzi V., Orru L., Lamontanara A., Kolseth A.-K.,
RA Frandsen R.J., Nielsen K., Thrane U.;
RT "The draft genome sequence of Fusarium langsethiae, a T-2/HT-2 mycotoxin
RT producer.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the cleavage factor I (CF I) involved in pre-
CC mRNA 3'-end processing. {ECO:0000256|ARBA:ARBA00024826,
CC ECO:0000256|RuleBase:RU369008}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU369008}.
CC -!- SIMILARITY: Belongs to the CPSF4/YTH1 family.
CC {ECO:0000256|ARBA:ARBA00008907, ECO:0000256|RuleBase:RU369008}.
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:KPA46652.1}.
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DR EMBL; JXCE01000003; KPA46652.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M9F5X9; -.
DR OrthoDB; 33612at2759; -.
DR Proteomes; UP000037904; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0031124; P:mRNA 3'-end processing; IEA:UniProtKB-UniRule.
DR Gene3D; 4.10.1000.10; Zinc finger, CCCH-type; 2.
DR InterPro; IPR045348; CPSF4/Yth1.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR PANTHER; PTHR23102:SF24; CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR SUBUNIT 4; 1.
DR PANTHER; PTHR23102; CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR SUBUNIT 4-RELATED; 1.
DR Pfam; PF00642; zf-CCCH; 2.
DR Pfam; PF14608; zf-CCCH_2; 3.
DR SMART; SM00356; ZnF_C3H1; 5.
DR SUPFAM; SSF90229; CCCH zinc finger; 2.
DR PROSITE; PS50103; ZF_C3H1; 5.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00723}; mRNA processing {ECO:0000256|RuleBase:RU369008};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU369008};
KW Reference proteome {ECO:0000313|Proteomes:UP000037904};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|RuleBase:RU369008};
KW RNA-binding {ECO:0000256|RuleBase:RU369008};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00723};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00723}.
FT DOMAIN 37..64
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 73..100
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 101..129
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 130..157
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 159..182
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT ZN_FING 37..64
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 73..100
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 101..129
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 130..157
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 159..182
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 179..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..231
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..255
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 255 AA; 28981 MW; BADCA6E55F3CD3DA CRC64;
MPAAVESPAS AILNHSATPY NFRFSPFLQQ TYQVGLSPDR PVCKAFQSGH CPNGTRCPER
HVSDSKTSQP TGGLNSLVCK HWLRGLCKKG EHCEFLHEYN LRKMPECNFF MRNGYCSNGD
ECLYLHIDPQ SRLPPCPHYD MGFCPLGPNC SKKHVRRKLC VFYLAGFCPD GPDCKEGAHP
KWSKDLEKPT LKSEEKKDEE VRMELSQDDM DRQRDQQRDR DRDDGGRHRG GHGGHGGHGG
RGKWRGRGRY RARGH
//