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Database: UniProt
Entry: A0A1B7NIX8_9AGAM
LinkDB: A0A1B7NIX8_9AGAM
Original site: A0A1B7NIX8_9AGAM 
ID   A0A1B7NIX8_9AGAM        Unreviewed;       293 AA.
AC   A0A1B7NIX8;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=mRNA 3'-end-processing protein {ECO:0000256|RuleBase:RU369008};
GN   ORFNames=K503DRAFT_728288 {ECO:0000313|EMBL:OAX44712.1};
OS   Rhizopogon vinicolor AM-OR11-026.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Boletales; Suillineae; Rhizopogonaceae; Rhizopogon.
OX   NCBI_TaxID=1314800 {ECO:0000313|EMBL:OAX44712.1, ECO:0000313|Proteomes:UP000092154};
RN   [1] {ECO:0000313|EMBL:OAX44712.1, ECO:0000313|Proteomes:UP000092154}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AM-OR11-026 {ECO:0000313|EMBL:OAX44712.1,
RC   ECO:0000313|Proteomes:UP000092154};
RG   DOE Joint Genome Institute;
RA   Mujic A.B., Kuo A., Tritt A., Lipzen A., Chen C., Johnson J., Sharma A.,
RA   Barry K., Grigoriev I.V., Spatafora J.W.;
RT   "Comparative genomics of the ectomycorrhizal sister species Rhizopogon
RT   vinicolor and Rhizopogon vesiculosus (Basidiomycota: Boletales) reveals a
RT   divergence of the mating type B locus.";
RL   Submitted (JUN-2016) 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|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}.
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DR   EMBL; KV448122; OAX44712.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1B7NIX8; -.
DR   STRING; 1314800.A0A1B7NIX8; -.
DR   InParanoid; A0A1B7NIX8; -.
DR   OrthoDB; 33612at2759; -.
DR   Proteomes; UP000092154; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0031124; P:mRNA 3'-end processing; IEA:UniProtKB-UniRule.
DR   Gene3D; 4.10.1000.10; Zinc finger, CCCH-type; 2.
DR   Gene3D; 4.10.60.10; Zinc finger, CCHC-type; 1.
DR   InterPro; IPR045348; CPSF4/Yth1.
DR   InterPro; IPR000571; Znf_CCCH.
DR   InterPro; IPR036855; Znf_CCCH_sf.
DR   InterPro; IPR001878; Znf_CCHC.
DR   InterPro; IPR036875; Znf_CCHC_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; 1.
DR   Pfam; PF18345; zf_CCCH_4; 1.
DR   SMART; SM00343; ZnF_C2HC; 1.
DR   SMART; SM00356; ZnF_C3H1; 5.
DR   SUPFAM; SSF90229; CCCH zinc finger; 2.
DR   SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 1.
DR   PROSITE; PS50103; ZF_C3H1; 5.
DR   PROSITE; PS50158; ZF_CCHC; 1.
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|RuleBase:RU369008};
KW   Reference proteome {ECO:0000313|Proteomes:UP000092154};
KW   Repeat {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          40..69
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   DOMAIN          88..115
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   DOMAIN          116..144
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   DOMAIN          148..170
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   DOMAIN          172..194
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   DOMAIN          257..272
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50158"
FT   ZN_FING         40..69
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   ZN_FING         88..115
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   ZN_FING         116..144
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   ZN_FING         148..170
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   ZN_FING         172..194
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   REGION          192..248
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        192..215
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   293 AA;  32982 MW;  0F3DAC3FDC4DBFBA CRC64;
     MATNPLAGPS ALRDIVHPQF HQNNFPEELY IKNELGLKLD KDDQICRLSL TSTGCPLGPL
     HCPLRHTTPS SQNFQPPKQL PTHPRERERL ATVCKHWLRG LCKKGDACEF LHEYNLRRMP
     ECWWYAKYGY CSAGDECLYA HPKERRVECP DYKRGFCKLG PSCPRKHVRR VACQLYLTGF
     CPLGPDCPRG HPKPDLPSPK SYDPPSPPSN RDLGPPPPGY GRYADFDRGT MGPQVMSHGG
     GPNGSGPPRR NLDEVLCFKC GEKGHYANHC RNRNVPGNRG GLDRARRFGA MED
//
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