ID A0A1V6SZS5_9EURO Unreviewed; 254 AA.
AC A0A1V6SZS5;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=mRNA 3'-end-processing protein {ECO:0000256|RuleBase:RU369008};
GN ORFNames=PENSTE_c016G05649 {ECO:0000313|EMBL:OQE19003.1};
OS Penicillium steckii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=303698 {ECO:0000313|EMBL:OQE19003.1, ECO:0000313|Proteomes:UP000191285};
RN [1] {ECO:0000313|Proteomes:UP000191285}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 24891 {ECO:0000313|Proteomes:UP000191285};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
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:OQE19003.1}.
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DR EMBL; MLKD01000016; OQE19003.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6SZS5; -.
DR STRING; 303698.A0A1V6SZS5; -.
DR OrthoDB; 33612at2759; -.
DR Proteomes; UP000191285; 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; 3.30.1370.210; -; 1.
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; 2.
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};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664,
KW ECO:0000256|RuleBase:RU369008};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU369008};
KW Reference proteome {ECO:0000313|Proteomes:UP000191285};
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 41..68
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 91..113
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 114..142
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 143..167
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 168..194
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT ZN_FING 41..68
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 91..113
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 114..142
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 143..167
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 168..194
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 220..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..243
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 254 AA; 28847 MW; 72922211F6327E76 CRC64;
MAADVQSTAA HLLSAEPTRD PSFNEFSFSP FLRKSFGFGL ASDVPVCKAY SEGHCPLGPA
CPDRHPTPSR VTTSTTTASG LAPSTTHGSL VCKHFLKGLC KKGVKCEYLH EYNLRRMPEC
QSFSRSGYCP NGDDCLYQHV REEARLPPCE HYDQGFCELG PLCAKRHVRR RLCMYYLAGF
CPEGKGCANA HPRWSENLPR PTMKTEKTEE ELEYERALIR EEQEREKERE REWRSERGRG
GGFMRGRYRG RGRG
//
