ID A0A1Y3N128_PIRSE Unreviewed; 422 AA.
AC A0A1Y3N128;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 22-FEB-2023, entry version 24.
DE RecName: Full=C3H1-type domain-containing protein {ECO:0000259|PROSITE:PS50103};
GN ORFNames=PIROE2DRAFT_69611 {ECO:0000313|EMBL:OUM61450.1};
OS Piromyces sp. (strain E2).
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales;
OC Neocallimastigaceae; Piromyces.
OX NCBI_TaxID=73868 {ECO:0000313|EMBL:OUM61450.1, ECO:0000313|Proteomes:UP000195826};
RN [1] {ECO:0000313|EMBL:OUM61450.1, ECO:0000313|Proteomes:UP000195826}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E2 {ECO:0000313|EMBL:OUM61450.1,
RC ECO:0000313|Proteomes:UP000195826};
RG DOE Joint Genome Institute;
RA Haitjema C.H., Gilmore S.P., Henske J.K., Solomon K.V., De Groot R.,
RA Kuo A., Mondo S.J., Salamov A.A., Labutti K., Zhao Z., Chiniquy J.,
RA Barry K., Brewer H.M., Purvine S.O., Wright A.T., Boxma B., Van Alen T.,
RA Hackstein J.H., Baker S.E., Grigoriev I.V., O'Malley M.A.;
RT "A Parts List for Fungal Cellulosomes Revealed by Comparative Genomics.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KZ150980; OUM61450.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y3N128; -.
DR STRING; 73868.A0A1Y3N128; -.
DR Proteomes; UP000195826; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008143; F:poly(A) binding; IEA:InterPro.
DR GO; GO:1900364; P:negative regulation of mRNA polyadenylation; IEA:InterPro.
DR GO; GO:0043488; P:regulation of mRNA stability; IEA:InterPro.
DR Gene3D; 4.10.1000.30; -; 1.
DR Gene3D; 4.10.1000.40; -; 2.
DR InterPro; IPR040366; Nab2/ZC3H14.
DR InterPro; IPR000571; Znf_CCCH.
DR PANTHER; PTHR14738; ZINC FINGER CCCH DOMAIN-CONTAINING PROTEIN 14; 1.
DR PANTHER; PTHR14738:SF29; ZINC FINGER CCCH DOMAIN-CONTAINING PROTEIN 14; 1.
DR Pfam; PF14608; zf-CCCH_2; 5.
DR SMART; SM00356; ZnF_C3H1; 5.
DR PROSITE; PS50103; ZF_C3H1; 2.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00723}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000195826};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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 257..290
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 366..390
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT ZN_FING 257..290
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 366..390
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 95..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 215..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 293..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..125
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 422 AA; 47252 MW; 013F482BBAA0FE0D CRC64;
MTDVSIEIPS VMNSKQKFNQ RLITSITQKL HNCKIASTPD DVSKIVNLLN EGKNREQLTE
EITTMFANDK DKIKSSFIDW LIGYSNACCT PTPEVETTEE LKSPSVKSDI ASLKEKAENK
SKSKRRISQS SRSRRSIIDT APLSPPPSPP KSSRASSVCS SDYEKSQKNI YHQKRLSRSA
NTLDLTSQVQ SEIMAQTLAL AAAAAVDIQL KNDKDVKRER RKSVRSIQST RSRKSSFSSV
KEEDTSRVRC QYWPTCKRGD QCKYWHPKEL CKKFPNCPNG DQCLYIHPAT TTPSKPQSSF
HRRISQSSIT PPDLSSSNDR VAVECKYGSN CTRPDCKFSH PSPAVAKLNK PQTKPAAPAQ
ESSKNSKSNV PCHYYPNCKN ADCPYMHPNT TPKTESVNVA CRYGSACNRP DCHFLHPGNR
RV
//
