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Database: UniProt
Entry: A0A0M9F5X9_FUSLA
LinkDB: A0A0M9F5X9_FUSLA
Original site: A0A0M9F5X9_FUSLA 
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
//
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