ID A0A1Q8RR38_9PEZI Unreviewed; 250 AA.
AC A0A1Q8RR38;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-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=CCHL11_07865 {ECO:0000313|EMBL:OLN86772.1};
OS Colletotrichum chlorophyti.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum.
OX NCBI_TaxID=708187 {ECO:0000313|EMBL:OLN86772.1, ECO:0000313|Proteomes:UP000186583};
RN [1] {ECO:0000313|EMBL:OLN86772.1, ECO:0000313|Proteomes:UP000186583}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NTL11 {ECO:0000313|EMBL:OLN86772.1,
RC ECO:0000313|Proteomes:UP000186583};
RA Gan P., Narusaka M., Tsushima A., Narusaka Y., Takano Y., Shirasu K.;
RT "Draft Genome Assembly of Colletotrichum chlorophyti a pathogen of
RT herbaceous plants.";
RL Submitted (NOV-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|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:OLN86772.1}.
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DR EMBL; MPGH01000109; OLN86772.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q8RR38; -.
DR STRING; 708187.A0A1Q8RR38; -.
DR OrthoDB; 33612at2759; -.
DR Proteomes; UP000186583; 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; 1.
DR Pfam; PF14608; zf-CCCH_2; 2.
DR Pfam; PF18345; zf_CCCH_4; 1.
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:UP000186583};
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 38..65
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 77..99
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 100..128
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 129..156
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 158..181
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT ZN_FING 38..65
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 77..99
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 100..128
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 129..156
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 158..181
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 184..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..234
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..250
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 250 AA; 28553 MW; FEB567782FB0EFCB CRC64;
MAAVASRPET NQILTHAPTA TSFAFTPFLR QAYRHELSSD RPQCKPFLAG HCPLGAACPD
RHTSSTSSNP SGGPSLVCKH WLRGLCKKGE SCEFLHEYNL RKMPECNFFM RNGYCSNGEE
CLYLHIDPQS KLPPCPHYDK GFCPLGPRCS KKHVRRKLCV YYLVGFCPEG PTCKYGAHPR
WRTDLEKPSP KVEGEDETKK DGDREDGEMQ HMRDRQRDMH DDRGHGDRRH GGRGGKWRDR
GNRRFRGRGH
//
